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Conserved domains on  [gi|446108595|ref|WP_000186450|]
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MULTISPECIES: two-component sensor histidine kinase BarA [Enterobacteriaceae]

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

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List of domain hits

Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-918 0e+00

hybrid sensory histidine kinase BarA; Provisional


:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1760.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   1 MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHS 80
Cdd:PRK11107   1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  81 DIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYI 160
Cdd:PRK11107  81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSQNMLGYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 161 ALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI 240
Cdd:PRK11107 161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 241 NSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLK 320
Cdd:PRK11107 241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 321 TELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPD 400
Cdd:PRK11107 321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 401 NVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHG 480
Cdd:PRK11107 401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSETP 560
Cdd:PRK11107 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 561 LEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTPT 640
Cdd:PRK11107 561 LEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLSKPLSHT 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 641 RLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQ 720
Cdd:PRK11107 641 RLLPALLEPCHHKQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQ 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 721 MPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSGISSRVVTPEVN 800
Cdd:PRK11107 721 MPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPP 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 801 EIVVNPNATLDWQLALRQAAGKTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQ 880
Cdd:PRK11107 801 EPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQ 880
                        890       900       910
                 ....*....|....*....|....*....|....*...
gi 446108595 881 LIEQQLRSGTKEEDLEPELLELLDEMDNVAREASKILG 918
Cdd:PRK11107 881 LIEQQLRSGTSVEDLEPELLELLDEMENVARAAKKVLS 918
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-918 0e+00

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1760.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   1 MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHS 80
Cdd:PRK11107   1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  81 DIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYI 160
Cdd:PRK11107  81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSQNMLGYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 161 ALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI 240
Cdd:PRK11107 161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 241 NSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLK 320
Cdd:PRK11107 241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 321 TELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPD 400
Cdd:PRK11107 321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 401 NVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHG 480
Cdd:PRK11107 401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSETP 560
Cdd:PRK11107 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 561 LEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTPT 640
Cdd:PRK11107 561 LEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLSKPLSHT 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 641 RLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQ 720
Cdd:PRK11107 641 RLLPALLEPCHHKQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQ 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 721 MPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSGISSRVVTPEVN 800
Cdd:PRK11107 721 MPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPP 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 801 EIVVNPNATLDWQLALRQAAGKTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQ 880
Cdd:PRK11107 801 EPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQ 880
                        890       900       910
                 ....*....|....*....|....*....|....*...
gi 446108595 881 LIEQQLRSGTKEEDLEPELLELLDEMDNVAREASKILG 918
Cdd:PRK11107 881 LIEQQLRSGTSVEDLEPELLELLDEMENVARAAKKVLS 918
BarA5 COG4999
Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction ...
1-889 0e+00

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


Pssm-ID: 444023 [Multi-domain]  Cd Length: 921  Bit Score: 1029.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   1 MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHS 80
Cdd:COG4999    3 MTLRRRRRIILLLLLLLLILLLLLLFFFFFVYRYQLLQQQLSASIIIIIAAAAASSEYLMNKRRREQLLLLLLRRHHRHS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  81 DIVRAISVYDENNRLFVTSNFHLDPSSMQLGsnvPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSqNMLGYI 160
Cdd:COG4999   83 IIISAIDDNNNLNNLSNNNNNNLNLLLLQLP---PPSPPLLLLTRSDLILLLIPPISIIYEDESSEPSDNTAA-NPLGYI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 161 ALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI 240
Cdd:COG4999  159 AIELDLSSDRLQQYQEQFVATLLLLLLLLLALLFAYRLMRDVTVPITNMVNVVDRIRRRRLDSRVEGGMLGELLLLKNGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 241 NSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLK 320
Cdd:COG4999  239 NNMAMSLAAYHEEMQQNIDQATSDLRETLEQLEIQNVELDLAKKRAQEAARAKSEFLANMSHELRTPLNGVIGFTRQTLK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 321 TELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPD 400
Cdd:COG4999  319 TTLTPTQTDYLQTIERSANNLLNIINDILDFSKLEAGKLLLELIPFPFRDTLDEVVVLLALLAHEKGLELTLLLDNDVPE 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 401 NVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHG 480
Cdd:COG4999  399 DVIGDPLRIQQILQNLLGNAIKFTETGNIDIIVELRTQRQNSVELQVQVRDTGIGISERQQAQLFQAFFQADASISRRRG 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNP-NIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSET 559
Cdd:COG4999  479 GTGGGLVITQKLVKEMGGEIGFISRLSQGSTFWFTFFLLLNLaPALSDPLPLDRLQGKRLLYVEPNPAAAQATLDLLSQT 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 560 PLEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTP 639
Cdd:COG4999  559 PLEVTYSPTLEQLPEAHYDILLIGLPVTYRNTLADLTDKLAQALRMADCVILALPSTAQVLAEQLKAAGARACLSKPLSA 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 640 TRLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDI 719
Cdd:COG4999  639 TRLLPLLLDECLFELPLPAATPEAPLPPLVVAVVDDNANNLLLIALLLELVVQVVVCCSSGEAAAAAAAQQLDDILIMDI 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 720 QMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSgiSSRVVTPEV 799
Cdd:COG4999  719 QMPMMDGIAAEEIIRQLPHNNTTPIVAVAAAAAAGREELLLAGGMDDYLAKPIEEELLLLLLLRYQPGP--HTVPSPPPV 796
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 800 NEIVVNPNATLDWQLALRQAAGK--TDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKN 877
Cdd:COG4999  797 PPSLAPLVLLQASQLSLDAAAALqqALDALLLLLELLLLLLLELLEVLILRQEIDLLGALDLLHGLHSSLLCSGLLRLKG 876
                        890
                 ....*....|..
gi 446108595 878 LCQLIEQQLRSG 889
Cdd:COG4999  877 LLSLQLQLEPEE 888
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
171-889 5.07e-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: 312.87  E-value: 5.07e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  171 LQQYKEIFISSVMMLFCIGIALIfgWRLM-RDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI--------- 240
Cdd:TIGR02956 326 LSVAQFGLLITGMLGLVILVFIM--WRVVyRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIeafrdtaah 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  241 --------NSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVI 312
Cdd:TIGR02956 404 nlklqadeRQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGIL 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  313 GFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTL 392
Cdd:TIGR02956 484 GTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRL 563
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  393 NIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVekRALSNTKVQIEVQirDTGIGIPERDQSRLFQAFRQAD 472
Cdd:TIGR02956 564 NIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRV--SLNDDSSLLFEVE--DTGCGIAEEEQATLFDAFTQAD 639
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  473 AsiSRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHInldlnpniiiegPSTQClagkrlayvEPNSAAAQCT 552
Cdd:TIGR02956 640 G--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTL------------PLTRG---------KPAEDSATLT 696
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  553 LDilsetplevvysptfsALPPAHydmmllgiavtfrepltmqherlakavsmtdflmlalpchaqvnaeklkqdgigac 632
Cdd:TIGR02956 697 VI----------------DLPPQR-------------------------------------------------------- 704
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  633 llkpltptrllpaltefchhkqntllpvtdesklamtVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPF 712
Cdd:TIGR02956 705 -------------------------------------VLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAF 747
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  713 DLILMDIQMPDMDGIracELIHQL----PHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGS 788
Cdd:TIGR02956 748 DLALLDINLPDGDGV---TLLQQLraiyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGG 824
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  789 GISSR----VVTPEVNEIVVNPNATLDwQLALRQAAGKT---------DLA-------RDMLQMLLDFLPEVRNKVEEQL 848
Cdd:TIGR02956 825 KSNTEapvlSASPSFDSASVIENAQAD-DIPESNQASEFlldeeqlqqDIEvlgvekvRQLVALFKTSSAEQLEELSAAR 903
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|.
gi 446108595  849 VGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSG 889
Cdd:TIGR02956 904 AVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTG 944
sCache_4 pfam09984
Single cache domain 4; Members of this family of domains are found in various BarA-like signal ...
31-177 1.33e-61

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: 205.17  E-value: 1.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   31 VHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQL 110
Cdd:pfam09984   1 INRYYELEDQLIDRGTSIIEPLAIASEYGLTTRNRESLRRLISALHRKNSPIVRSIAIFDANNQLFVTSNYHRDFESLRL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446108595  111 GSNVPFPRQLTVTRDGDIMILRTPIISESySPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEI 177
Cdd:pfam09984  81 PEGAPIPTLTTVEHSGDSLILRTPIISEG-LSLPGLPATAESAQRPLGYIAIELNLDSARLQQYREI 146
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
409-518 8.84e-56

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: 187.70  E-value: 8.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVI 488
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 446108595 489 TQKLVNEMGGDISFHSQPNRGSTFWFHINL 518
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
404-516 2.35e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 130.08  E-value: 2.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   404 GDPLRLQQIITNLVGNAIKFT-ENGNIDIlvekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASiSRRHGGT 482
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITV-----TLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 446108595   483 GLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHI 516
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITL 108
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
178-512 1.48e-34

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 139.00  E-value: 1.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 178 FISSVMMLFCIGIALIFG---WRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEgfMLGELDM--LKNGINSMAMSLaayhe 252
Cdd:NF040691 185 LVRGTLLLGGLALVVLLGliaWLVTRQVVAPVRSAARTAERFAAGDLSERMP--VKGEDDLarLARSFNQMADSL----- 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 253 emQHNIDQatsdlretLEQMeiqnveldlakkraqeaARIKSEFLANMSHELRTPLngvigfTRLTLKTELTPTQRDHLN 332
Cdd:NF040691 258 --QRQIRQ--------LEEL-----------------SRLQQRFVSDVSHELRTPL------TTIRMAADVIHDSRDDFD 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 333 -TIERSAnNLL--------AIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIkSDVPDNVI 403
Cdd:NF040691 305 pATARSA-ELLhteldrfeSLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDA-PGTPVVAE 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 404 GDPLRLQQIITNLVGNAIKFTENGNIDILVekrALSNTKVQIEVqiRDTGIGIPERDQSRLFQAFRQADASISRRHGGTG 483
Cdd:NF040691 383 VDPRRVERVLRNLVVNAIEHGEGKPVVVTV---AQDDTAVAVTV--RDHGVGLKPGEVALVFDRFWRADPARARTTGGTG 457
                        330       340
                 ....*....|....*....|....*....
gi 446108595 484 LGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:NF040691 458 LGLAIALEDARLHGGWLEAWGRPGQGSQF 486
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
190-506 5.43e-25

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 109.53  E-value: 5.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 190 IALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAmslaayheemqhnidqatsdlrETL 269
Cdd:NF012163 176 LAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQDFNQLA----------------------STL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 270 EQMEiqnveldlakkraqeaaRIKSEFLANMSHELRTPLngvigftrLTLKTELTPTQ-------RDHLNTIERSANNLL 342
Cdd:NF012163 234 EKNE-----------------QMRRDFMADISHELRTPL--------AVLRAELEAIQdgirkftPESLDSLQAEVGTLT 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 343 AIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLEltlnIKSDVPDN--VIGDPLRLQQIITNLVGNA 420
Cdd:NF012163 289 KLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE----LEVSLPDSslVFGDRDRLMQLFNNLLENS 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 421 IKFTEN-GNIDILVEKRALSntkVQIEVQirDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGD 499
Cdd:NF012163 365 LRYTDSgGSLHISASQRPKE---VTLTVA--DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGT 439

                 ....*..
gi 446108595 500 ISFHSQP 506
Cdd:NF012163 440 LHAAHSP 446
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
156-516 1.74e-16

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: 81.96  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 156 MLGYI----ALE---LDLKSVrlqQYKEIFISSV------MMLFCIG-IALIFGWRLMRDVTGPIRNMVNTVDRIRRGQL 221
Cdd:NF012226  27 FLGYFiynyAIEvgwITLSSL---QEDWTEFHFVdwiwlfTVILCGSvISLIIGMKLAQRFIVPINFLADAAKKISQGDL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 222 DSRVEgfmlgeldmlKNGINSMAMSlaayheEMQHNIDQATSDLRETLEQMEIQNveldlakkraqeaarikseflANMS 301
Cdd:NF012226 104 SARAE----------DSQIHSAEIS------ELMHNFNDMAQKLESSVKNAQVWN---------------------AAIA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 302 HELRTPLNGVIGFTRLTLKTELTPTQ---RDHLNTIErsanNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTL 378
Cdd:NF012226 147 HELRTPITILQGRLQGILDGVFEPDPalfKSLLNQVE----GLSHLVEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKM 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 379 LAHSSHDKGLELTLNIKSDVpdnVIGDPLRLQQIITNLVGNAIKFTENGNIDIlvekralSNTKVQIE--VQIRDTGIGI 456
Cdd:NF012226 223 FEDRLEQAQLTIVLNLTATP---VFCDRRRIEQVLIALIDNAIRYANAGKLKI-------SSSVIQDDwiLQIEDEGPGI 292
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 457 PERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFhSQPNRGSTFWFHI 516
Cdd:NF012226 293 AEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFTIKL 351
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-918 0e+00

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1760.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   1 MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHS 80
Cdd:PRK11107   1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  81 DIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYI 160
Cdd:PRK11107  81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSQNMLGYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 161 ALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI 240
Cdd:PRK11107 161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 241 NSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLK 320
Cdd:PRK11107 241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 321 TELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPD 400
Cdd:PRK11107 321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 401 NVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHG 480
Cdd:PRK11107 401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSETP 560
Cdd:PRK11107 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 561 LEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTPT 640
Cdd:PRK11107 561 LEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLSKPLSHT 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 641 RLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQ 720
Cdd:PRK11107 641 RLLPALLEPCHHKQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQ 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 721 MPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSGISSRVVTPEVN 800
Cdd:PRK11107 721 MPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPP 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 801 EIVVNPNATLDWQLALRQAAGKTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQ 880
Cdd:PRK11107 801 EPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQ 880
                        890       900       910
                 ....*....|....*....|....*....|....*...
gi 446108595 881 LIEQQLRSGTKEEDLEPELLELLDEMDNVAREASKILG 918
Cdd:PRK11107 881 LIEQQLRSGTSVEDLEPELLELLDEMENVARAAKKVLS 918
BarA5 COG4999
Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction ...
1-889 0e+00

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


Pssm-ID: 444023 [Multi-domain]  Cd Length: 921  Bit Score: 1029.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   1 MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHS 80
Cdd:COG4999    3 MTLRRRRRIILLLLLLLLILLLLLLFFFFFVYRYQLLQQQLSASIIIIIAAAAASSEYLMNKRRREQLLLLLLRRHHRHS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  81 DIVRAISVYDENNRLFVTSNFHLDPSSMQLGsnvPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSqNMLGYI 160
Cdd:COG4999   83 IIISAIDDNNNLNNLSNNNNNNLNLLLLQLP---PPSPPLLLLTRSDLILLLIPPISIIYEDESSEPSDNTAA-NPLGYI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 161 ALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI 240
Cdd:COG4999  159 AIELDLSSDRLQQYQEQFVATLLLLLLLLLALLFAYRLMRDVTVPITNMVNVVDRIRRRRLDSRVEGGMLGELLLLKNGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 241 NSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLK 320
Cdd:COG4999  239 NNMAMSLAAYHEEMQQNIDQATSDLRETLEQLEIQNVELDLAKKRAQEAARAKSEFLANMSHELRTPLNGVIGFTRQTLK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 321 TELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPD 400
Cdd:COG4999  319 TTLTPTQTDYLQTIERSANNLLNIINDILDFSKLEAGKLLLELIPFPFRDTLDEVVVLLALLAHEKGLELTLLLDNDVPE 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 401 NVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHG 480
Cdd:COG4999  399 DVIGDPLRIQQILQNLLGNAIKFTETGNIDIIVELRTQRQNSVELQVQVRDTGIGISERQQAQLFQAFFQADASISRRRG 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNP-NIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSET 559
Cdd:COG4999  479 GTGGGLVITQKLVKEMGGEIGFISRLSQGSTFWFTFFLLLNLaPALSDPLPLDRLQGKRLLYVEPNPAAAQATLDLLSQT 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 560 PLEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTP 639
Cdd:COG4999  559 PLEVTYSPTLEQLPEAHYDILLIGLPVTYRNTLADLTDKLAQALRMADCVILALPSTAQVLAEQLKAAGARACLSKPLSA 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 640 TRLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDI 719
Cdd:COG4999  639 TRLLPLLLDECLFELPLPAATPEAPLPPLVVAVVDDNANNLLLIALLLELVVQVVVCCSSGEAAAAAAAQQLDDILIMDI 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 720 QMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSgiSSRVVTPEV 799
Cdd:COG4999  719 QMPMMDGIAAEEIIRQLPHNNTTPIVAVAAAAAAGREELLLAGGMDDYLAKPIEEELLLLLLLRYQPGP--HTVPSPPPV 796
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 800 NEIVVNPNATLDWQLALRQAAGK--TDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKN 877
Cdd:COG4999  797 PPSLAPLVLLQASQLSLDAAAALqqALDALLLLLELLLLLLLELLEVLILRQEIDLLGALDLLHGLHSSLLCSGLLRLKG 876
                        890
                 ....*....|..
gi 446108595 878 LCQLIEQQLRSG 889
Cdd:COG4999  877 LLSLQLQLEPEE 888
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
171-889 5.07e-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: 312.87  E-value: 5.07e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  171 LQQYKEIFISSVMMLFCIGIALIfgWRLM-RDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI--------- 240
Cdd:TIGR02956 326 LSVAQFGLLITGMLGLVILVFIM--WRVVyRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIeafrdtaah 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  241 --------NSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVI 312
Cdd:TIGR02956 404 nlklqadeRQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGIL 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  313 GFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTL 392
Cdd:TIGR02956 484 GTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRL 563
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  393 NIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVekRALSNTKVQIEVQirDTGIGIPERDQSRLFQAFRQAD 472
Cdd:TIGR02956 564 NIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRV--SLNDDSSLLFEVE--DTGCGIAEEEQATLFDAFTQAD 639
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  473 AsiSRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHInldlnpniiiegPSTQClagkrlayvEPNSAAAQCT 552
Cdd:TIGR02956 640 G--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTL------------PLTRG---------KPAEDSATLT 696
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  553 LDilsetplevvysptfsALPPAHydmmllgiavtfrepltmqherlakavsmtdflmlalpchaqvnaeklkqdgigac 632
Cdd:TIGR02956 697 VI----------------DLPPQR-------------------------------------------------------- 704
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  633 llkpltptrllpaltefchhkqntllpvtdesklamtVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPF 712
Cdd:TIGR02956 705 -------------------------------------VLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAF 747
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  713 DLILMDIQMPDMDGIracELIHQL----PHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGS 788
Cdd:TIGR02956 748 DLALLDINLPDGDGV---TLLQQLraiyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGG 824
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  789 GISSR----VVTPEVNEIVVNPNATLDwQLALRQAAGKT---------DLA-------RDMLQMLLDFLPEVRNKVEEQL 848
Cdd:TIGR02956 825 KSNTEapvlSASPSFDSASVIENAQAD-DIPESNQASEFlldeeqlqqDIEvlgvekvRQLVALFKTSSAEQLEELSAAR 903
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|.
gi 446108595  849 VGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSG 889
Cdd:TIGR02956 904 AVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTG 944
PRK15347 PRK15347
two component system sensor kinase;
97-889 1.89e-82

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 285.38  E-value: 1.89e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  97 VTSNFHL-----DPSSMQLGSNVPFPRQLTV---TRDGDIMILRTP---IISESYSPDESPS--------SDAKN---SQ 154
Cdd:PRK15347 180 PGGGWHVsvavaDKQGVLVGFTVKLNDLISYnhpVLDDDINLWLDQngeLLPFSTIPLSSNQlqkilnqlENVKLhdgWQ 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 155 NMLGYIALELDLKSVRLQQ---YKEIFIS-------------SVMMLFCIgiALIFGWRLMRDVTGPIRNMVNTVDRIRR 218
Cdd:PRK15347 260 QIPDYLVLRTQLKGPGWQQvtlYPRRNLAnealkpalqqlpfALLILVLL--TSVLFLLLRRYLAKPLWRFVDIINKTGP 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 219 GQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATsdlretleqmeiqnVELDLAKKRAQEAARIKSEFLA 298
Cdd:PRK15347 338 AALEPRLPENRLDELGSIAKAYNQLLDTLNEQYDTLENKVAERT--------------QALAEAKQRAEQANKRKSEHLT 403
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 299 NMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLIL---ESIPFPLrstLDEV 375
Cdd:PRK15347 404 TISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLsleETALLPL---LDQA 480
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 376 VTLLAHSSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRalsNTKVQIEVQirDTGIG 455
Cdd:PRK15347 481 MLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRH---EQQLCFTVE--DTGCG 555
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 456 IPERDQSRLFQAFRQADASIsrrhGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINL-DLNPNIIIEGP--STQ 532
Cdd:PRK15347 556 IDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLnEYAPPEPLKGElsAPL 631
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 533 CLAGKRLAY-VEPNSAAAQCTLDilsetplevvySPTFSALPPAHYDMMllgiavtFREPLTMQHERLAKAvsmtdflml 611
Cdd:PRK15347 632 ALHRQLSAWgITCQPGHQNPALL-----------DPELAYLPGRLYDLL-------QQIIQGAPNEPVINL--------- 684
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 612 alpchaqvnaeklkqdgigacllkPLTPTRllpaltefchhkqntllpvtdesklaMTVMAVDDNPANLKLIGALLEDMV 691
Cdd:PRK15347 685 ------------------------PLQPWQ--------------------------LQILLVDDVETNRDIIGMMLVELG 714
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 692 QHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQT--PVIAVTAHAMAGQKEKLLGAGMSDYLA 769
Cdd:PRK15347 715 QQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPdcMIVALTANAAPEEIHRCKKAGMNHYLT 794
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 770 KPIEEERLHNLL---LRYKPGSGIssrvvtpevnEIVVNpNATLDWQLALRQaagkTDLARDMLQMLLDFLPEVRNKVee 846
Cdd:PRK15347 795 KPVTLAQLARALelaAEYQLLRGI----------ELSPQ-DSSCSPLLDTDD----MALNSKLYQSLLLLLAQIEQAV-- 857
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|...
gi 446108595 847 qlvgENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSG 889
Cdd:PRK15347 858 ----ENQEVLSQLLHTLKGCAGQAGLTELQCAVIDLENALETG 896
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
184-518 6.92e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 254.06  E-value: 6.92e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 184 MLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATS 263
Cdd:COG0642    1 LLLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 264 DLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLtLKTELTPTQRDHLNTIERSANNLLA 343
Cdd:COG0642   81 LLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLEL-LLEELDEEQREYLETILRSADRLLR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 344 IINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPdNVIGDPLRLQQIITNLVGNAIKF 423
Cdd:COG0642  160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 424 TENGNiDILVEkraLSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADAsiSRRHGGTGLGLVITQKLVNEMGGDISFH 503
Cdd:COG0642  239 TPEGG-TVTVS---VRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVE 312
                        330
                 ....*....|....*
gi 446108595 504 SQPNRGSTFWFHINL 518
Cdd:COG0642  313 SEPGKGTTFTVTLPL 327
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
286-784 3.44e-70

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 250.66  E-value: 3.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 286 AQEAARIKSEFLANMSHELRTPLNGVIGFTRLtLKTELTPTQRDHL-NTIERSANNLLAIINDVLDFSKLEAGKLILESI 364
Cdd:PRK10841 440 AEQASQSKSMFLATVSHELRTPLYGIIGNLDL-LQTKELPKGVDRLvTAMNNSSSLLLKIISDILDFSKIESEQLKIEPR 518
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 365 PFPLRstldEVVTllaHSSHD-------KGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRa 437
Cdd:PRK10841 519 EFSPR----EVIN---HITANylplvvkKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVD- 590
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 438 lsntKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHIN 517
Cdd:PRK10841 591 ----GDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIP 666
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 518 L---DLNPNIIIEGpstqcLAGKRLAYVEPNSAAAQCTLDILSETPLEVVYsptFSALPPAHYDMMLlgiavtfrepltm 594
Cdd:PRK10841 667 LygaQYPQKKGVEG-----LQGKRCWLAVRNASLEQFLETLLQRSGIQVQR---YEGQEPTPEDVLI------------- 725
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 595 qherlakavsmTDF-LMLALPCHAQVN-----AEKLKQDGIGACLLKPLTPTRLLPALTEFCHHKQN-----TLLPVTDE 663
Cdd:PRK10841 726 -----------TDDpVQKKWQGRAVITfcrrhIGIPLEIAPGEWVHSTATPHELPALLARIYRIELEsddsaNALPSTDK 794
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 664 SKLA---MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqq 740
Cdd:PRK10841 795 AVSDnddMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGL-- 872
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 446108595 741 QTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRY 784
Cdd:PRK10841 873 TLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVY 916
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
278-516 8.29e-70

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 231.33  E-value: 8.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 278 ELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTE--LTPTQRDHLNTIERSANNLLAIINDVLDFSKLE 355
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 356 AGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPdNVIGDPLRLQQIITNLVGNAIKFT-ENGNIDIlve 434
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSpPGGTITI--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 435 krALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADAsiSRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWF 514
Cdd:COG2205  157 --SARREGDGVRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTV 232

                 ..
gi 446108595 515 HI 516
Cdd:COG2205  233 TL 234
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
156-516 7.04e-68

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 231.75  E-value: 7.04e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 156 MLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDM 235
Cdd:COG5002   30 LLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 236 LKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEaaRIKSEFLANMSHELRTPLNGVIGFT 315
Cdd:COG5002  110 LLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLE--QMRREFVANVSHELRTPLTSIRGYL 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 316 RLTL--KTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLN 393
Cdd:COG5002  188 ELLLdgAADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELD 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 394 IKSDVPdNVIGDPLRLQQIITNLVGNAIKFT-ENGNIDIlvekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQAD 472
Cdd:COG5002  268 LPEDPL-LVLGDPDRLEQVLTNLLDNAIKYTpEGGTITV-----SLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVD 341
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446108595 473 ASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHI 516
Cdd:COG5002  342 KSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
283-890 1.36e-67

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 241.00  E-value: 1.36e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 283 KKRAQE----AARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGK 358
Cdd:PRK11091 269 RKRYQDalekASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRK 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 359 LILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVekRAL 438
Cdd:PRK11091 349 LQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRV--RYE 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 439 SNTKVQIEVQirDTGIGIPERDQSRLFQAFRQADASISRRHG-GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFwfhin 517
Cdd:PRK11091 427 EGDMLTFEVE--DSGIGIPEDELDKIFAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCF----- 499
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 518 ldlnpniiiegpstqclagkrlayvepnsaaaqcTLDIlsetplevvysptfsalppahydmmllgiavtfrepltmqhe 597
Cdd:PRK11091 500 ----------------------------------TLTI------------------------------------------ 503
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 598 rlakavsmtdflmlALPCHAQVNAEKLKQDgigacllkpltpTRLLPALtefchhkqNTLLpvtdesklamtvmaVDDNP 677
Cdd:PRK11091 504 --------------HAPAVAEEVEDAFDED------------DMPLPAL--------NILL--------------VEDIE 535
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 678 ANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIR-ACELIHQLPHQQQTPVIAVTAHAMAGQK 756
Cdd:PRK11091 536 LNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDiARELRERYPREDLPPLVALTANVLKDKK 615
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 757 EkLLGAGMSDYLAKPIEEERLHNLLLRYkpgsgiSSRVVTPEVNEIVVNPNATLDWQLALrqaagktdlarDMLQMLLDF 836
Cdd:PRK11091 616 E-YLDAGMDDVLSKPLSVPALTAMIKKF------WDTQDDEESTVTTEESSKANEALLDI-----------PMLEQYVEL 677
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 837 ----------------LPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMknlcQLIEQQLRSGT 890
Cdd:PRK11091 678 vgpklitdslavfekmMPGYLSVLDSNLTARDQKGIVEEAHKIKGAAGSVGLRHL----QQLAQQIQSPD 743
sCache_4 pfam09984
Single cache domain 4; Members of this family of domains are found in various BarA-like signal ...
31-177 1.33e-61

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: 205.17  E-value: 1.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   31 VHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQL 110
Cdd:pfam09984   1 INRYYELEDQLIDRGTSIIEPLAIASEYGLTTRNRESLRRLISALHRKNSPIVRSIAIFDANNQLFVTSNYHRDFESLRL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446108595  111 GSNVPFPRQLTVTRDGDIMILRTPIISESySPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEI 177
Cdd:pfam09984  81 PEGAPIPTLTTVEHSGDSLILRTPIISEG-LSLPGLPATAESAQRPLGYIAIELNLDSARLQQYREI 146
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
409-518 8.84e-56

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: 187.70  E-value: 8.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVI 488
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 446108595 489 TQKLVNEMGGDISFHSQPNRGSTFWFHINL 518
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
170-564 4.69e-51

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 194.35  E-value: 4.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 170 RLQQYKEIFISSVMMLFCIGI-ALIF-GWRLM-RDVTGPIRNMVNTVDRIRRGQLDSRV-EGFMLGELDMLKNGINSMAM 245
Cdd:PRK11466 321 HLEKASARGQYSLLLLGMVSLcALILiLWRVVyRSVTRPLAEQTQALQRLLDGDIDSPFpETAGVRELDTIGRLMDAFRS 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 246 SLAAYHEEMQHNIDQATSDLRETLEQMeiqnVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELTP 325
Cdd:PRK11466 401 NVHALNRHREQLAAQVKARTAELQELV----IEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALN 476
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 326 TQRDHLNTIERSANNLLAIINDVLDFSKLEAG--KLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVI 403
Cdd:PRK11466 477 AQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALM 556
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 404 GDPLRLQQIITNLVGNAIKFTENGNIdilVEKRALSNTKVQIEVQirDTGIGIPERDQSRLFQAFRQADAsisrRHGGTG 483
Cdd:PRK11466 557 GDPRRIRQVITNLLSNALRFTDEGSI---VLRSRTDGEQWLVEVE--DSGCGIDPAKLAEIFQPFVQVSG----KRGGTG 627
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 484 LGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQC-LAGKRLAYVEPNSAAAQCTLDILSETPLE 562
Cdd:PRK11466 628 LGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAVrLDGLRLLLIEDNPLTQRITAEMLNTSGAQ 707

                 ..
gi 446108595 563 VV 564
Cdd:PRK11466 708 VV 709
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
4-516 2.77e-49

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 182.68  E-value: 2.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   4 YSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIV 83
Cdd:COG4251    7 LLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  84 RAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALE 163
Cdd:COG4251   87 LELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 164 LDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSM 243
Cdd:COG4251  167 ILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 244 AMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDlakkraqeaariksEFLANMSHELRTPLNGVIGFTRL---TLK 320
Cdd:COG4251  247 LLILVLELLELRLELEELEEELEERTAELERSNEELE--------------QFAYVASHDLREPLRKISGFSQLleeDYG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 321 TELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILEsiPFPLRSTLDEVVTLLAHSSHDKGLELTLnikSDVPD 400
Cdd:COG4251  313 DKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQELEFE--PVDLNELLEEVLEDLEPRIEERGAEIEV---GPLPT 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 401 nVIGDPLRLQQIITNLVGNAIKFT---ENGNIDILVEKRalsNTKVQIEVqiRDTGIGIPERDQSRLFQAFRQADASisR 477
Cdd:COG4251  388 -VRGDPTLLRQVFQNLISNAIKYSrpgEPPRIEIGAERE---GGEWVFSV--RDNGIGIDPEYAEKIFEIFQRLHSR--D 459
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 446108595 478 RHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHI 516
Cdd:COG4251  460 EYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTL 498
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
670-781 2.78e-42

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: 149.54  E-value: 2.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPH-QQQTPVIAVT 748
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGgGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446108595 749 AHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLL 781
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
177-518 2.45e-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: 157.43  E-value: 2.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 177 IFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQH 256
Cdd:COG5000    8 LLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 257 ------NIDQATSD----------------------------------------------LRETLEQMEIQNVELDLAKK 284
Cdd:COG5000   88 rrryleTILENLPAgvivldadgritlanpaaerllgipleeligkpleellpeldlaelLREALERGWQEEIELTRDGR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 285 --------------------------RAQEAARIKsEFLANMSHELRTPLNGVIGFT-RLTLK-----TELTPTQRDHLN 332
Cdd:COG5000  168 rtllvrasplrddgyvivfdditellRAERLAAWG-ELARRIAHEIKNPLTPIQLSAeRLRRKladklEEDREDLERALD 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 333 TIERSANNLLAIINDVLDFSKLEAGKLIlesiPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDnVIGDPLRLQQI 412
Cdd:COG5000  247 TIIRQVDRLKRIVDEFLDFARLPEPQLE----PVDLNELLREVLALYEPALKEKDIRLELDLDPDLPE-VLADRDQLEQV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 413 ITNLVGNAIKFTE-NGNIDIlvekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFrqadasISRRHGGTGLGLVITQK 491
Cdd:COG5000  322 LINLLKNAIEAIEeGGEIEV-----STRREDGRVRIEVSDNGPGIPEEVLERIFEPF------FTTKPKGTGLGLAIVKK 390
                        410       420
                 ....*....|....*....|....*..
gi 446108595 492 LVNEMGGDISFHSQPNRGSTFWFHINL 518
Cdd:COG5000  391 IVEEHGGTIELESRPGGGTTFTIRLPL 417
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
263-522 6.26e-41

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: 157.83  E-value: 6.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 263 SDLRETLEQMeiqnveldlakkRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLtLKTELTPTQRDHLNTIERSANNLL 342
Cdd:COG5809  252 TERKKLEELL------------RKSEKLSVVGELAAGIAHEIRNPLTSLKGFIQL-LKDTIDEEQKTYLDIMLSELDRIE 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 343 AIINDVLDFSKLEAGKLIlesiPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDnVIGDPLRLQQIITNLVGNAIK 422
Cdd:COG5809  319 SIISEFLVLAKPQAIKYE----PKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIE 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 423 FTENGNiDILVEKRALSNTKVQIEVQirDTGIGIPERDQSRLFQAFrqadasISRRHGGTGLGLVITQKLVNEMGGDISF 502
Cdd:COG5809  394 AMPEGG-NITIETKAEDDDKVVISVT--DEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITV 464
                        250       260
                 ....*....|....*....|
gi 446108595 503 HSQPNRGSTFWFHINLDLNP 522
Cdd:COG5809  465 ESEVGKGTTFSITLPIKLSE 484
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
291-516 1.92e-39

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: 149.28  E-value: 1.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  291 RIKSEFLANMSHELRTPLNGVIGF--TRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPL 368
Cdd:TIGR02966 112 QMRRDFVANVSHELRTPLTVLRGYleTLADGPDEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDM 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  369 RSTLDEVVTLLAHSSHDKGLELTLNIKSDVPdnVIGDPLRLQQIITNLVGNAIKFT-ENGNIDILVEKRalsNTKVQIEV 447
Cdd:TIGR02966 192 PALLDHLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTpEGGTITVRWRRD---GGGAEFSV 266
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446108595  448 QirDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHI 516
Cdd:TIGR02966 267 T--DTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
668-784 1.18e-38

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: 139.99  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAV 747
Cdd:COG0784    6 KRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIAL 85
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRY 784
Cdd:COG0784   86 TAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
273-512 3.40e-37

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 143.45  E-value: 3.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 273 EIQNVELDLAKKRAQEAARiksEFLANMSHELRTPLNGVIGFTRLtLKTELT-PTQRDHLNTIERSANNLLAIINDVLDF 351
Cdd:COG3852  118 ERKRLERELRRAEKLAAVG---ELAAGLAHEIRNPLTGIRGAAQL-LERELPdDELREYTQLIIEEADRLNNLVDRLLSF 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 352 SKLEAGKLIlesiPFPLRSTLDEVVTLLaHSSHDKGLELTLNIKSDVPDnVIGDPLRLQQIITNLVGNAIK-FTENGNID 430
Cdd:COG3852  194 SRPRPPERE----PVNLHEVLERVLELL-RAEAPKNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEaMPEGGTIT 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 431 ILVEKRALSNTKVQ-----IEVQIRDTGIGIPERDQSRLFQAFrqadasISRRHGGTGLGLVITQKLVNEMGGDISFHSQ 505
Cdd:COG3852  268 IRTRVERQVTLGGLrprlyVRIEVIDNGPGIPEEILDRIFEPF------FTTKEKGTGLGLAIVQKIVEQHGGTIEVESE 341

                 ....*..
gi 446108595 506 PNRGSTF 512
Cdd:COG3852  342 PGKGTTF 348
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
156-516 3.79e-37

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 143.40  E-value: 3.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 156 MLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDM 235
Cdd:COG4191   10 LLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 236 LKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEqmeiqnvELDLAKKRAQEAARIKS--EFLANMSHELRTPLNGVIG 313
Cdd:COG4191   90 LEALLLLLLAALDAEENAELEELERDITELERAEE-------ELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 314 FT---RLTLKTELTPTQ-RDHLNTIERSANNLLAIINDVLDFSKLEAgkliLESIPFPLRSTLDEVVTLLAHSSHDKGLE 389
Cdd:COG4191  163 NAellRRRLEDEPDPEElREALERILEGAERAAEIVRSLRAFSRRDE----EEREPVDLNELIDEALELLRPRLKARGIE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 390 LTLNIKSDVPdNVIGDPLRLQQIITNLVGNAI---KFTENGNIDILVEKRALsntkvQIEVQIRDTGIGIPERDQSRLFQ 466
Cdd:COG4191  239 VELDLPPDLP-PVLGDPGQLEQVLLNLLINAIdamEEGEGGRITISTRREGD-----YVVISVRDNGPGIPPEVLERIFE 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446108595 467 AF---RQADasisrrhGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHI 516
Cdd:COG4191  313 PFfttKPVG-------KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
404-516 2.35e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 130.08  E-value: 2.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   404 GDPLRLQQIITNLVGNAIKFT-ENGNIDIlvekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASiSRRHGGT 482
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITV-----TLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 446108595   483 GLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHI 516
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITL 108
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
178-512 1.48e-34

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 139.00  E-value: 1.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 178 FISSVMMLFCIGIALIFG---WRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEgfMLGELDM--LKNGINSMAMSLaayhe 252
Cdd:NF040691 185 LVRGTLLLGGLALVVLLGliaWLVTRQVVAPVRSAARTAERFAAGDLSERMP--VKGEDDLarLARSFNQMADSL----- 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 253 emQHNIDQatsdlretLEQMeiqnveldlakkraqeaARIKSEFLANMSHELRTPLngvigfTRLTLKTELTPTQRDHLN 332
Cdd:NF040691 258 --QRQIRQ--------LEEL-----------------SRLQQRFVSDVSHELRTPL------TTIRMAADVIHDSRDDFD 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 333 -TIERSAnNLL--------AIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIkSDVPDNVI 403
Cdd:NF040691 305 pATARSA-ELLhteldrfeSLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDA-PGTPVVAE 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 404 GDPLRLQQIITNLVGNAIKFTENGNIDILVekrALSNTKVQIEVqiRDTGIGIPERDQSRLFQAFRQADASISRRHGGTG 483
Cdd:NF040691 383 VDPRRVERVLRNLVVNAIEHGEGKPVVVTV---AQDDTAVAVTV--RDHGVGLKPGEVALVFDRFWRADPARARTTGGTG 457
                        330       340
                 ....*....|....*....|....*....
gi 446108595 484 LGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:NF040691 458 LGLAIALEDARLHGGWLEAWGRPGQGSQF 486
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
260-772 1.71e-34

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 142.95  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  260 QATSDLRETLEQMEIQnveldlaKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQR-DHLNTIERSA 338
Cdd:PRK09959  686 QDITETRDLIHALEVE-------RNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATG 758
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  339 NNLLAIINDVLDFSKLEAGKlilesipFPLRSTLDEVVTLLAHSSHDKGL-----ELTLNIKSDVPDN--VIGDPLRLQQ 411
Cdd:PRK09959  759 QSLLGLIGEILDVDKIESGN-------YQLQPQWVDIPTLVQNTCHSFGAiaaskSIALSCSSTFPDHylVKIDPQAFKQ 831
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  412 IITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADAsiSRRHGGTGLGLVITQK 491
Cdd:PRK09959  832 VLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSA--GRQQTGSGLGLMICKE 909
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  492 LVNEMGGDISFHSQPNRGSTFWFHInldlnpniiiegpstqclagkrlayvepnsaaaqctldilsetPLEVVysptfsa 571
Cdd:PRK09959  910 LIKNMQGDLSLESHPGIGTTFTITI-------------------------------------------PVEIS------- 939
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  572 lppahydmmllgiavtfrepltmqherlakavsmtdflmlalpchAQVNAEKLKQDGigacllkpltptrllpaltefch 651
Cdd:PRK09959  940 ---------------------------------------------QQVATVEAKAEQ----------------------- 951
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  652 hkqntllPVTDESKLamTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracE 731
Cdd:PRK09959  952 -------PITLPEKL--SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGF---E 1019
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 446108595  732 LIHQLPHQQQT-PVIAVTAHAMAGQKEKLLGAGMSDYLAKPI 772
Cdd:PRK09959 1020 LTRKLREQNSSlPIWGLTANAQANEREKGLSCGMNLCLFKPL 1061
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
667-784 6.17e-34

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 128.49  E-value: 6.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 667 AMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIA 746
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKPIEEERLH---NLLLRY 784
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEELLarvDLVARY 121
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
670-781 8.05e-34

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: 125.34  E-value: 8.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqqQTPVIAVTA 749
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDP--TTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 446108595  750 HAMAGQKEKLLGAGMSDYLAKPIEEERLHNLL 781
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
5-514 2.07e-32

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: 131.74  E-value: 2.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595    5 SLRARMMILILAPTVLIGLLLSIFFvvhrYNDLQRQLE----DAGASIIEPLAVSTEYGMSL-QNRESIGQLISVLHRRH 79
Cdd:TIGR01386   3 SLTLRLALLFAAVTALVFALSGFML----YSSLERHFEerdrEELQGKLEQVRRFLRDPADLdEDIKRLQEKIDDLLVGH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   80 SDIvrAISVYDENNRLFVTSNFHldpssmqlgSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGY 159
Cdd:TIGR01386  79 SDL--ALSILNPDGRLLFERAQG---------AALVPAVAANDALLELDQADAKMTHYRSILRSVAALPGGKGRKPVQIT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  160 IALELDLKSVRLQQYKEIFISSVMMLFcIGIALIfGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRvegfmlgeLDMlkng 239
Cdd:TIGR01386 148 VALDINAHTHLLDALRKWLILIAVLLV-LLTALL-GWWITRLGLEPLRRLSAVAARISPESLDQR--------LDP---- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  240 insmamslaayheemqhnidqatSDLRETLEQMEIqnvELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTL 319
Cdd:TIGR01386 214 -----------------------SRAPAELRELAQ---SFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVAL 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  320 KTEltPTQRDHLNTIERSA---NNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKS 396
Cdd:TIGR01386 268 SQP--RTGEEYREVLESNLeelERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEG 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  397 DVPdnviGDPLRLQQIITNLVGNAIKFT-ENGNIDILVEKRAlsntkVQIEVQIRDTGIGIPERDQSRLFQAFRQADASI 475
Cdd:TIGR01386 346 LVR----GDPQMFRRAISNLLSNALRHTpDGGTITVRIERRS-----DEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPAR 416
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446108595  476 SRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRgSTFWF 514
Cdd:TIGR01386 417 SNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFIL 454
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
404-519 1.17e-31

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: 119.40  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  404 GDPLRLQQIITNLVGNAIKFT-ENGNIDILVEKralsntKVQIEVQIRDTGIGIPERDQSRLFQAFRQADasiSRRHGGT 482
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSE------GGELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446108595  483 GLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLD 519
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
667-781 3.47e-31

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 122.20  E-value: 3.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 667 AMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIA 746
Cdd:COG3437    6 APTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIF 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLL 781
Cdd:COG3437   86 LTALADPEDRERALEAGADDYLTKPFDPEELLARV 120
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
669-778 7.63e-31

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: 117.26  E-value: 7.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVT 748
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 446108595 749 AHAMAGQKEKLLGAGMSDYLAKPIEEERLH 778
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPIDTREFL 110
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
240-512 5.36e-28

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 117.66  E-value: 5.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 240 INSMAMSLAAY-HEEMQHNIDqatsdLRETLEQMEIQNveldlakkraqeaarIKSEFLANMSHELRTPLNGVIGFTRLT 318
Cdd:COG5806  167 IQLLAMLIAVYlIENLIENIL-----LRKELQRAEKLE---------------VVSELAASIAHEVRNPLTVVRGFIQLL 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 319 LKTELTPTQRDH-----LNTIERsANnllAIINDVLDFSKLEAGKLIlesiPFPLRSTLDEVVTLLAHSSHDKGLELTLN 393
Cdd:COG5806  227 QEPELSDEKRKQyiriaLEELDR-AE---AIITDYLTFAKPQPEKLE----KIDVSEELEHVIDVLSPYANMNNVEIQTE 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 394 IKSDVpdNVIGDPLRLQQIITNLVGNAIKFTENG---NIDILVEKRalsntKVQIEvqIRDTGIGIPERDQSRLFQAFrq 470
Cdd:COG5806  299 LEPGL--YIEGDRQKLQQCLINIIKNGIEAMPNGgtlTIDVSIDKN-----KVIIS--IKDTGVGMTKEQLERLGEPY-- 367
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446108595 471 adasISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:COG5806  368 ----FSTKEKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTF 405
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
670-772 1.18e-27

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: 107.60  E-value: 1.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTA 749
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                         90       100
                 ....*....|....*....|...
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPI 772
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
PRK09303 PRK09303
histidine kinase;
252-514 1.34e-26

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 112.74  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 252 EEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPL--------------NGVIGFTRL 317
Cdd:PRK09303 110 GENLQPSEIDSGRYSQELLQLSDELFVLRQENETLLEQLKFKDRVLAMLAHDLRTPLtaaslaletlelgqIDEDTELKP 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 318 TLKTELTPTQRDHLNTIERsannllaIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSD 397
Cdd:PRK09303 190 ALIEQLQDQARRQLEEIER-------LITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSD 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 398 VPdNVIGDPLRLQQIITNLVGNAIKFT-ENGNIDILVEKRalSNTKVQieVQIRDTGIGIPERDQSRLFQ-AFR-QADAS 474
Cdd:PRK09303 263 LP-SVYADQERIRQVLLNLLDNAIKYTpEGGTITLSMLHR--TTQKVQ--VSICDTGPGIPEEEQERIFEdRVRlPRDEG 337
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446108595 475 ISrrhgGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWF 514
Cdd:PRK09303 338 TE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHF 373
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
668-805 4.09e-26

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: 106.96  E-value: 4.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqqQTPVIAV 747
Cdd:COG0745    2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPS--DIPIIML 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKPIEEE----RLHNLLLRYKPGSGISSRVVTPEVNEIVVN 805
Cdd:COG0745   80 TARDDEEDRVRGLEAGADDYLTKPFDPEellaRIRALLRRRAAEVLRVGDLLDLAAREVTRD 141
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
282-512 9.63e-26

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 113.14  E-value: 9.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 282 AKKRAQE----AARIKS--EFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLE 355
Cdd:PRK11360 373 ERKRLQRrvarQERLAAlgELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPR 452
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 356 AGKLIlesiPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIgDPLRLQQIITNLVGNAIK-FTENGNIDILVE 434
Cdd:PRK11360 453 ESQWQ----PVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWA-DPELLKQVLLNILINAVQaISARGKIRIRTW 527
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446108595 435 KralsNTKVQIEVQIRDTGIGIPERDQSRLFQAFrqadasISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:PRK11360 528 Q----YSDGQVAVSIEDNGCGIDPELLKKIFDPF------FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTF 595
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
670-781 2.93e-25

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 101.00  E-value: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTA 749
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEEERLHNLL 781
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
190-506 5.43e-25

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 109.53  E-value: 5.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 190 IALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAmslaayheemqhnidqatsdlrETL 269
Cdd:NF012163 176 LAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQDFNQLA----------------------STL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 270 EQMEiqnveldlakkraqeaaRIKSEFLANMSHELRTPLngvigftrLTLKTELTPTQ-------RDHLNTIERSANNLL 342
Cdd:NF012163 234 EKNE-----------------QMRRDFMADISHELRTPL--------AVLRAELEAIQdgirkftPESLDSLQAEVGTLT 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 343 AIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLEltlnIKSDVPDN--VIGDPLRLQQIITNLVGNA 420
Cdd:NF012163 289 KLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE----LEVSLPDSslVFGDRDRLMQLFNNLLENS 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 421 IKFTEN-GNIDILVEKRALSntkVQIEVQirDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGD 499
Cdd:NF012163 365 LRYTDSgGSLHISASQRPKE---VTLTVA--DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGT 439

                 ....*..
gi 446108595 500 ISFHSQP 506
Cdd:NF012163 440 LHAAHSP 446
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
673-771 1.85e-24

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: 98.45  E-value: 1.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 673 VDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVTAHAM 752
Cdd:cd00156    3 VDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE--LPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 446108595 753 AGQKEKLLGAGMSDYLAKP 771
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
668-780 2.64e-24

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: 98.67  E-value: 2.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMV-QHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIA 746
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKPIEEE----RLHNL 780
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPFDPVellaRVRNL 118
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
246-604 4.12e-24

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 109.00  E-value: 4.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 246 SLAAYHEEMQHnIDQATSDLRETLEQMEIQNvELDLAKKRAQEAARIKS--EFLANMSHELRTPLNGVIGFTRLTL-KTE 322
Cdd:PRK13837 403 GLRPPAGELQL-LELALDCLAHAIERRRLET-ERDALERRLEHARRLEAvgTLASGIAHNFNNILGAILGYAEMALnKLA 480
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 323 LTPTQRDHLNTIERSANNLLAIINDVLDFSKleagKLILESIPFPLRSTLDEVVTLLAhSSHDKGLELTLNIKSDvPDNV 402
Cdd:PRK13837 481 RHSRAARYIDEIISAGARARLIIDQILAFGR----KGERNTKPFDLSELVTEIAPLLR-VSLPPGVELDFDQDQE-PAVV 554
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 403 IGDPLRLQQIITNLVGNAIK-FTENGNIDILVEKRALSNTKVQIE--------VQIR--DTGIGIPERDQSRLFQAFrqa 471
Cdd:PRK13837 555 EGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKLRAPKVLSHgvlppgryVLLRvsDTGAGIDEAVLPHIFEPF--- 631
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 472 dasISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTF--WFHIN--LDLNPNIIIEGPSTQCLAGKRLAYVEPNSA 547
Cdd:PRK13837 632 ---FTTRAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFdvYLPPSskVPVAPQAFFGPGPLPRGRGETVLLVEPDDA 708
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446108595 548 AAQCTLDILSETPLEVVYSPTFSAL------PPAHYDMMLLGIAVTFREPLTMQHERLAKAVS 604
Cdd:PRK13837 709 TLERYEEKLAALGYEPVGFSTLAAAiawiskGPERFDLVLVDDRLLDEEQAAAALHAAAPTLP 771
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
668-783 2.22e-23

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 103.89  E-value: 2.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqqQTPVIAV 747
Cdd:COG2204    3 ARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDP--DLPVILL 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLR 783
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVER 116
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
299-516 2.75e-23

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 104.54  E-value: 2.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 299 NMSHELRTPLNGVIGFTRLtLKTELTPTQRDH-LNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVT 377
Cdd:PRK11100 262 TLTHELKSPLAAIRGAAEL-LQEDPPPEDRARfTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 378 LLAHSSHDKGLELTLNIksdVPDNVIGDPLRLQQIITNLVGNAIKFT-ENGNIDILVEKRAlsntkVQIEVQIRDTGIGI 456
Cdd:PRK11100 341 AREAQAAAKGITLRLRP---DDARVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVDG-----EQVALSVEDQGPGI 412
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446108595 457 PERDQSRLFQAFrqadASISRRHGG---TGLGLVITQKLVNEMGGDISFHSQPNRG--STFWFHI 516
Cdd:PRK11100 413 PDYALPRIFERF----YSLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGvlATLTLPR 473
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
669-772 1.33e-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: 1.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVT 748
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                         90       100
                 ....*....|....*....|....
gi 446108595 749 AHAMAGQKEKLLGAGMSDYLAKPI 772
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKPI 104
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
280-512 3.58e-22

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: 101.35  E-value: 3.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 280 DLAKKRAQEAARIKSEFL-------ANMSHELRTPLNGVIGFTRLtLKTELTpTQRDHLNTIERSANNLLAIINDVLDFS 352
Cdd:COG5805  267 DITEKKEAEELMARSEKLsiagqlaAGIAHEIRNPLTSIKGFLQL-LQPGIE-DKEEYFDIMLSELDRIESIISEFLALA 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 353 KLEAGKLILESIpfplRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPdNVIGDPLRLQQIITNLVGNAIKFTEN-GNIDI 431
Cdd:COG5805  345 KPQAVNKEKENI----NELIQDVVTLLETEAILHNIQIRLELLDEDP-FIYCDENQIKQVFINLIKNAIEAMPNgGTITI 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 432 LVEkraLSNTKVQIEVQirDTGIGIPERDQSRLFQAFrqadasISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGST 511
Cdd:COG5805  420 HTE---EEDNSVIIRVI--DEGIGIPEERLKKLGEPF------FTTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTT 488

                 .
gi 446108595 512 F 512
Cdd:COG5805  489 F 489
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
668-785 4.85e-22

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 92.73  E-value: 4.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDM--VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVI 745
Cdd:COG4565    4 IRVLIVEDDPMVAELLRRYLERLpgFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDVDVI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446108595 746 AVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYK 785
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYL 121
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
170-501 9.96e-22

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 99.32  E-value: 9.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 170 RLQQYKEIFISSVMMLFcigiALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLaa 249
Cdd:PRK10549 160 KQQRRTSWLIVALSTLL----AALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTL-- 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 250 yheemqhnidqatsdlrETLEQMeiqnveldlakKRAqeaarikseFLANMSHELRTPLNgvigftrlTLKTELTPTQR- 328
Cdd:PRK10549 234 -----------------EKNEQM-----------RRD---------FMADISHELRTPLA--------VLRGELEAIQDg 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 329 ------DHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLniksDVPDN- 401
Cdd:PRK10549 269 vrkftpESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQL----SLPDSa 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 402 -VIGDPLRLQQIITNLVGNAIKFT-ENGNIDILVEKRALSNTkvqieVQIRDTGIGIPERDQSRLFQAFRQADASISRRH 479
Cdd:PRK10549 345 tVFGDPDRLMQLFNNLLENSLRYTdSGGSLHISAEQRDKTLR-----LTFADSAPGVSDEQLQKLFERFYRTEGSRNRAS 419
                        330       340
                 ....*....|....*....|..
gi 446108595 480 GGTGLGLVITQKLVNEMGGDIS 501
Cdd:PRK10549 420 GGSGLGLAICLNIVEAHNGRII 441
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
280-514 1.33e-21

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 98.54  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 280 DLAKKRAQEAARikSEFLANMSHELRTPLNGVIGFTRLTLKTELT-PTQRDHLNTIERSANNLLAIINDVLDFSKLEAGK 358
Cdd:PRK11006 193 DVTQMHQLEGAR--RNFFANVSHELRTPLTVLQGYLEMMQDQPLEgALREKALHTMREQTQRMEGLVKQLLTLSKIEAAP 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 359 LI-LES---IPFPLRSTLDEVVTLlAHSSHdkglELTLNIKSDVpdNVIGDPLRLQQIITNLVGNAIKFTENG-NIDIlv 433
Cdd:PRK11006 271 TIdLNEkvdVPMMLRVLEREAQTL-SQGKH----TITFEVDNSL--KVFGNEDQLRSAISNLVYNAVNHTPEGtHITV-- 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 434 ekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFW 513
Cdd:PRK11006 342 ---RWQRVPQGAEFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFS 418

                 .
gi 446108595 514 F 514
Cdd:PRK11006 419 F 419
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
62-889 5.86e-21

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


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 98.96  E-value: 5.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  62 LQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYS 141
Cdd:COG2198    2 ALLLLALLLLLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 142 PDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQL 221
Cdd:COG2198   82 LLLLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 222 DSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMS 301
Cdd:COG2198  162 LLALLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAEL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 302 HELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAH 381
Cdd:COG2198  242 AALLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 382 SSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQ 461
Cdd:COG2198  322 LLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLL 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 462 SRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWF--------------HINLDLNPNIIIE 527
Cdd:COG2198  402 LLLSLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLllllgllllallllLLLLLLLLLLLLL 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 528 GPSTQCLAGKRLAYVEPNSAAAQCTLDILSETPLEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTD 607
Cdd:COG2198  482 LLLLLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALL 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 608 FLMLALPCHAQVNAEKLKQDGIGACLLKPLTPTRLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALL 687
Cdd:COG2198  562 LGLGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLL 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 688 EDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDY 767
Cdd:COG2198  642 LLLLLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAA 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 768 LAKPIEEERLHNLLLRYKPgSGISSRVVTPEVNEIVVNPNATLDWQlALRQAAGKTDLARDMLQMLLDFLPEVRNKVEEQ 847
Cdd:COG2198  722 LLAALLLLLLLLLLLLLLL-LLLLLAAAAAAAASPAAPALPVLDLE-ALRRLGGDPELLRELLELFLEELPELLAELRQA 799
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|..
gi 446108595 848 LVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSG 889
Cdd:COG2198  800 LAAGDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARAG 841
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
68-529 6.66e-21

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 96.88  E-value: 6.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  68 IGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPS 147
Cdd:COG3850    9 LALLRLLLALLALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLLLLLAA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 148 SDAKNSQNMLGYIALELDLKSVRLQQYKEIfISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEG 227
Cdd:COG3850   89 LLSLLLLLLLLLLLLLLLLLLLLAAAINRK-LALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 228 FMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQAtsdlretleqmeiqnveldlakkRAQEAARIKSEFLANMSHELRTP 307
Cdd:COG3850  168 SGRDELGTLARAFNRMADELQELYAELEEEEELE-----------------------AELELLALLDELLLLAALLLLLA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 308 LNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKG 387
Cdd:COG3850  225 LLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 388 LELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQA 467
Cdd:COG3850  305 LLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGAALAAAAAAAGLARALAQAGADAAE 384
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446108595 468 FRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGP 529
Cdd:COG3850  385 ALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIAGGEAIARGEALAARGLAAAAA 446
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
405-512 2.53e-20

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: 87.16  E-value: 2.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 405 DPLRLQQIITNLVGNAIKFTENGN-IDILVEKRALSntkvQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTG 483
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGrIRCILEKFRLN----RFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTG 76
                         90       100
                 ....*....|....*....|....*....
gi 446108595 484 LGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:cd16925   77 LGLSIVKEFVELHGGTVTVSDAPGGGALF 105
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
673-771 3.13e-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: 86.31  E-value: 3.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 673 VDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqqQTPVIAVTAHAM 752
Cdd:cd17574    3 VEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGS--DIPIIMLTAKDE 80
                         90
                 ....*....|....*....
gi 446108595 753 AGQKEKLLGAGMSDYLAKP 771
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
668-785 3.18e-20

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 90.65  E-value: 3.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDM--VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQTP-V 744
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEKYpdLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGF---ELARQLRELDPPPpI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446108595 745 IAVTAH---AMAGQKeklLGAgmSDYLAKPIEEERLHNLLLRYK 785
Cdd:COG3279   79 IFTTAYdeyALEAFE---VNA--VDYLLKPIDEERLAKALEKAK 117
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
293-357 3.23e-20

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 84.96  E-value: 3.23e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446108595  293 KSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAG 357
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
293-357 3.33e-20

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 84.93  E-value: 3.33e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446108595   293 KSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAG 357
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
669-771 3.68e-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: 86.37  E-value: 3.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDM--VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIA 746
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEagFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE--LDPDTKIII 78
                         90       100
                 ....*....|....*....|....*
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:COG4753   79 LSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
393-512 4.31e-19

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: 84.10  E-value: 4.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 393 NIKSDVPDNVI---GDPLRLQQIITNLVGNAIKFTENGNIDILvekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFR 469
Cdd:cd16947    2 QVEINIPDRPIyanANTEALQRILKNLISNAIKYGSDGKFLGM----TLREDEKHVYIDIWDKGKGISETEKDHVFERLY 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446108595 470 QADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:cd16947   78 TLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVF 120
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-514 6.31e-19

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 82.76  E-value: 6.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFT---ENGNIDILVEKRALSNTkvqIEVqiRDTGIGIPERDQSRLFQAFRQADASisRRHGGTGLG 485
Cdd:cd16921    1 LGQVLTNLLGNAIKFRrprRPPRIEVGAEDVGEEWT---FYV--RDNGIGIDPEYAEKVFGIFQRLHSR--EEYEGTGVG 73
                         90       100
                 ....*....|....*....|....*....
gi 446108595 486 LVITQKLVNEMGGDISFHSQPNRGSTFWF 514
Cdd:cd16921   74 LAIVRKIIERHGGRIWLESEPGEGTTFYF 102
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
405-518 6.49e-19

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 82.90  E-value: 6.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 405 DPLRLQQIITNLVGNAIKFTENGNIdilVEKRAlSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGL 484
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGGK---LRIRA-AQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446108595 485 GLVITQKLVNEMGGDISFHSQPNRGstFWFHINL 518
Cdd:cd16946   77 GLAICHNIALAHGGTISAEHSPLGG--LRLVLTL 108
PRK10490 PRK10490
sensor protein KdpD; Provisional
281-524 1.10e-18

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 91.64  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 281 LAKKRAQEAARIKSE-------FLANMSHELRTPLNGVIGFTR---LTLKTELTP--TQ----RDH-LNTIeRSANNLLa 343
Cdd:PRK10490 645 LTLTASEEQARLASEreqlrnaLLAALSHDLRTPLTVLFGQAEiltLDLASEGSPhaRQaseiRQQvLNTT-RLVNNLL- 722
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 344 iindvlDFSKLEAGKlilesipFPLRS---TLDEVVtllahSSHDKGLELTLN---IKSDVPDNVI---GDPLRLQQIIT 414
Cdd:PRK10490 723 ------DMARIQSGG-------FNLRKewlTLEEVV-----GSALQMLEPGLSghpINLSLPEPLTlihVDGPLFERVLI 784
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 415 NLVGNAIKFTENG---NIDILVEKRalsntkvQIEVQIRDTGIGIPERDQSRLFQAFRQAD--ASISrrhgGTGLGLVIT 489
Cdd:PRK10490 785 NLLENAVKYAGAQaeiGIDAHVEGE-------RLQLDVWDNGPGIPPGQEQLIFDKFARGNkeSAIP----GVGLGLAIC 853
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446108595 490 QKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNI 524
Cdd:PRK10490 854 RAIVEVHGGTIWAENRPEGGACFRVTLPLETPPEL 888
envZ PRK09467
osmolarity sensor protein; Provisional
297-501 1.86e-18

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 89.20  E-value: 1.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 297 LANMSHELRTPLngvigfTRLTLKTELTPTQRDHL-----NTIERSanNllAIINDVLDFSKLEAgKLILESIPfpLRST 371
Cdd:PRK09467 233 MAGVSHDLRTPL------TRIRLATEMMSEEDGYLaesinKDIEEC--N--AIIEQFIDYLRTGQ-EMPMEMAD--LNAL 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 372 LDEVVtlLAHSSHDKGLELTLNiksDVPDNVIGDPLRLQQIITNLVGNAIKFtenGNIDILVEkraLSNTKVQIEVQIRD 451
Cdd:PRK09467 300 LGEVI--AAESGYEREIETALQ---PGPIEVPMNPIAIKRALANLVVNAARY---GNGWIKVS---SGTEGKRAWFQVED 368
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446108595 452 TGIGIPERDQSRLFQAFRQADasISRRHGGTGLGLVITQKLVNEMGGDIS 501
Cdd:PRK09467 369 DGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKVE 416
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
159-512 4.33e-18

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 88.29  E-value: 4.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 159 YIALELDLKSVRLQQYKEIFIS-----SVMMLFCIGIALIFGWRLMRDVTGPIRNmvntvdrIRRGQLDSRVEGFMLG-E 232
Cdd:PRK09835 168 LIALSIDFHLHYINDLKNKLIMtasviSLLIVFIVLLAVHKGHAPIRSVSRQIQN-------ITSKDLDVRLDPQTVPiE 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 233 LDMLKNGINSMamslaayheemqhnidqatsdlretLEQMEiqnvelDLAKKRAQeaarikseFLANMSHELRTPLNGVI 312
Cdd:PRK09835 241 LEQLVLSFNHM-------------------------IERIE------DVFTRQSN--------FSADIAHEIRTPITNLI 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 313 GFTRLTLKTELTPTQ-RDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELT 391
Cdd:PRK09835 282 TQTEIALSQSRSQKElEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELR 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 392 LNIKsdvPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILvekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQA 471
Cdd:PRK09835 362 FVGD---PCQVAGDPLMLRRAISNLLSNALRYTPAGEAITV----RCQEVDHQVQLVVENPGTPIAPEHLPRLFDRFYRV 434
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446108595 472 DASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPnRGSTF 512
Cdd:PRK09835 435 DPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRF 474
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
667-777 1.45e-17

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 81.93  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 667 AMTVMAVDDNPANLKLIGALLEDM-VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlphQQQTPVI 745
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAgYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISE---ERPAPVI 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446108595 746 AVTAHAMAGQKEKLLGAGMSDYLAKPIEEERL 777
Cdd:COG3707   80 LLTAYSDPELIERALEAGVSAYLVKPLDPEDL 111
PRK10604 PRK10604
sensor protein RstB; Provisional
299-522 1.10e-16

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 83.50  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 299 NMSHELRTPLngVIGFTRLTLKTELTPTQRdhlNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTL 378
Cdd:PRK10604 218 GIAHELRTPL--VRLRYRLEMSDNLSAAES---QALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLAD 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 379 LAHSSHDKGLELTLNIKSDVpdnVIGDPLRLQQIITNLVGNAIKFTEnGNIDIlvekrALSNTKVQIEVQIRDTGIGIPE 458
Cdd:PRK10604 293 IQAVTPEKTVRLDTPHQGDY---GALDMRLMERVLDNLLNNALRYAH-SRVRV-----SLLLDGNQACLIVEDDGPGIPP 363
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446108595 459 RDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFH--INLDLNP 522
Cdd:PRK10604 364 EERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSwpVWHNLPQ 429
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
156-516 1.74e-16

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: 81.96  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 156 MLGYI----ALE---LDLKSVrlqQYKEIFISSV------MMLFCIG-IALIFGWRLMRDVTGPIRNMVNTVDRIRRGQL 221
Cdd:NF012226  27 FLGYFiynyAIEvgwITLSSL---QEDWTEFHFVdwiwlfTVILCGSvISLIIGMKLAQRFIVPINFLADAAKKISQGDL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 222 DSRVEgfmlgeldmlKNGINSMAMSlaayheEMQHNIDQATSDLRETLEQMEIQNveldlakkraqeaarikseflANMS 301
Cdd:NF012226 104 SARAE----------DSQIHSAEIS------ELMHNFNDMAQKLESSVKNAQVWN---------------------AAIA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 302 HELRTPLNGVIGFTRLTLKTELTPTQ---RDHLNTIErsanNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTL 378
Cdd:NF012226 147 HELRTPITILQGRLQGILDGVFEPDPalfKSLLNQVE----GLSHLVEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKM 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 379 LAHSSHDKGLELTLNIKSDVpdnVIGDPLRLQQIITNLVGNAIKFTENGNIDIlvekralSNTKVQIE--VQIRDTGIGI 456
Cdd:NF012226 223 FEDRLEQAQLTIVLNLTATP---VFCDRRRIEQVLIALIDNAIRYANAGKLKI-------SSSVIQDDwiLQIEDEGPGI 292
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 457 PERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFhSQPNRGSTFWFHI 516
Cdd:NF012226 293 AEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFTIKL 351
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-513 1.78e-16

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: 76.29  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 402 VIGDPLRLQQIITNLVGNAIKFT-ENGNIDILVEKRALSNtkvqieVQIRDTGIGIPERDQSRLFQAFRQADasiSRRHG 480
Cdd:cd16940    7 VQGDALLLFLLLRNLVDNAVRYSpQGSRVEIKLSADDGAV------IRVEDNGPGIDEEELEALFERFYRSD---GQNYG 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446108595 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFW 513
Cdd:cd16940   78 GSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAW 110
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
670-783 2.27e-16

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 75.84  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDM---VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLphQQQTPVIA 746
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEelgFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL--YPDIKIII 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446108595 747 VTAH--------AMAgqkeklLGAgmSDYLAKPIEEERLHNLLLR 783
Cdd:cd17536   79 LSGYddfeyaqkAIR------LGV--VDYLLKPVDEEELEEALEK 115
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
670-779 4.48e-16

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: 75.24  E-value: 4.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDM--VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAV 747
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpdIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIVL 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKPIEEERLHN 779
Cdd:cd17535   79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIE 110
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
669-777 9.89e-16

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 74.26  E-value: 9.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQL---PHQQQTPVI 745
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGI---ELIKELrklPAYKFTPIL 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446108595 746 AVTAHAMAGQKEKLLGAGMSDYLAKPIEEERL 777
Cdd:cd17562   79 MLTTESSDEKKQEGKAAGATGWLVKPFDPEQL 110
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
668-778 1.99e-15

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 73.21  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDM-VQHVELCDSGHQAVERAKQMPFDLILMDIQMP-DMDGIRACELIHQlphQQQTPVI 745
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLgYEVVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE---KFDIPVI 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446108595 746 AVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLH 778
Cdd:cd17534   78 FLTAYSDEETLERAKETNPYGYLVKPFNERELK 110
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
670-771 4.08e-15

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: 71.81  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQTPVIAVTA 749
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGL---EVIRRLREWSAVPVIVLSA 77
                         90       100
                 ....*....|....*....|..
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd17620   78 RDEESDKIAALDAGADDYLTKP 99
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
291-353 7.83e-15

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: 69.93  E-value: 7.83e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446108595 291 RIKSEFLANMSHELRTPLNGVIGFTRLTLKTEL-TPTQRDHLNTIERSANNLLAIINDVLDFSK 353
Cdd:cd00082    2 QAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
670-783 1.57e-14

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: 70.73  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVE--RAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqqqTPVIAV 747
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSmlRENKDEFDLVITDVHMPDMDGFEFLELIRLEMD---LPVIMM 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLR 783
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQH 113
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
406-512 2.01e-14

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: 70.14  E-value: 2.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 406 PLRLQQIITNLVGNAIK-FTENGNIDIlveKRALSNTKVQIEVqiRDTGIGIPERDQSRLFQAFrqadaSISRRHG-GTG 483
Cdd:cd16943    1 PSQLNQVLLNLLVNAAQaMEGRGRITI---RTWAHVDQVLIEV--EDTGSGIDPEILGRIFDPF-----FTTKPVGeGTG 70
                         90       100
                 ....*....|....*....|....*....
gi 446108595 484 LGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:cd16943   71 LGLSLSYRIIQKHGGTIRVASVPGGGTRF 99
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-508 2.41e-14

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: 69.74  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFTENGNIDILVEKR-------ALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFrqadasISRRHGG 481
Cdd:cd16918    1 LIQVFLNLVRNAAQALAGSGGEIILRTRtqrqvtlGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPM------VSGRENG 74
                         90       100
                 ....*....|....*....|....*..
gi 446108595 482 TGLGLVITQKLVNEMGGDISFHSQPNR 508
Cdd:cd16918   75 TGLGLAIAQNIVSQHGGVIECDSQPGH 101
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
821-888 2.62e-14

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: 69.20  E-value: 2.62e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446108595   821 GKTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRS 888
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDA 68
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-516 2.70e-14

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 69.92  E-value: 2.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFT-ENGNIDI---LVEKRAlsntkvqiEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGL 484
Cdd:cd16952    1 LRSAFSNLVSNAVKYTpPSDTITVrwsQEESGA--------RLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGL 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446108595 485 GLVITQKLVNEMGGDISFHSQPNRGSTFWFHI 516
Cdd:cd16952   73 GLAIVKHVMSRHDARLLIASELGKGSRFTCLF 104
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
668-777 3.01e-14

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: 70.00  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQHV--ELCDsGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLphQQQTPVI 745
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVvgEAAN-GEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKI--DPNAKVI 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446108595 746 AVTAhamAGQKEKL---LGAGMSDYLAKPIEEERL 777
Cdd:cd17542   78 MCSA---MGQEEMVkeaIKAGAKDFIVKPFQPERV 109
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
298-512 3.10e-14

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 75.98  E-value: 3.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 298 ANMSHELRTPLNGVIGFTrlTLKTELTPT---QRDHLNTIERSANNLLAIINDVLDFSKleAGKLILEsiPFPLRSTLDE 374
Cdd:PRK10364 242 AGVAHEIRNPLSSIKGLA--KYFAERAPAggeAHQLAQVMAKEADRLNRVVSELLELVK--PTHLALQ--AVDLNDLINH 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 375 VVTLLAHSSHDKGLELTLNIKSDVPDnVIGDPLRLQQIITNLVGNAIK-FTENGNIDIlvekrALSNTKVQIEVQIRDTG 453
Cdd:PRK10364 316 SLQLVSQDANSREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAIQaIGQHGVISV-----TASESGAGVKISVTDSG 389
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446108595 454 IGIPERDQSRLFqafrqaDASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:PRK10364 390 KGIAADQLEAIF------TPYFTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATF 442
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
671-772 3.86e-14

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


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 69.61  E-value: 3.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 671 MAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTAH 750
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                         90       100
                 ....*....|....*....|....
gi 446108595 751 amAGQKEKLLG--AGMSDYLAKPI 772
Cdd:cd19937   81 --GEEFDKVLGleLGADDYITKPF 102
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
670-771 5.61e-14

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: 68.56  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQ---QQTPVIA 746
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGY---SLLGKLRKNadfDTIPVIF 77
                         90       100
                 ....*....|....*....|....*
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd19927   78 LTAKGMTSDRIKGYNAGCDGYLSKP 102
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
670-783 6.23e-14

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 75.07  E-value: 6.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLphQQQTPVIAVTA 749
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL--NPAIPVLIMTA 85
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLR 783
Cdd:PRK10365  86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
280-518 6.66e-14

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


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 75.94  E-value: 6.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  280 DLAKKRAQEAARIK--SEFLANMS----HELRTPLNGVigftRLTLKT-ELTPTQRDHLNTIERS---ANNLLAIINDVL 349
Cdd:TIGR03785 466 DLSRSFAQMVARLRqyTHYLENMSsrlsHELRTPVAVV----RSSLENlELQALEQEKQKYLERAregTERLSMILNNMS 541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  350 DFSKLEAGKLILESIPFPLRSTLDEVVTllAHSSHDKGLELTLNI-KSDVPDNviGDPLRLQQIITNLVGNAIKFT-ENG 427
Cdd:TIGR03785 542 EATRLEQAIQSAEVEDFDLSEVLSGCMQ--GYQMTYPPQRFELNIpETPLVMR--GSPELIAQMLDKLVDNAREFSpEDG 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  428 NIDIlvekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPn 507
Cdd:TIGR03785 618 LIEV-----GLSQNKSHALLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQ- 691
                         250
                  ....*....|.
gi 446108595  508 RGSTFWFHINL 518
Cdd:TIGR03785 692 QNDGVVFRISL 702
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-514 7.83e-14

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: 68.19  E-value: 7.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFTENGNidilVEKRALS-----NTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASisrrhgGTG 483
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGG----CERRELTirtspADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSE------GLG 70
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446108595 484 LGLVITQKLVNEMGGDISFHSQPNRGSTFWF 514
Cdd:cd16920   71 MGLSICRSIIEAHGGRLSVESPAGGGATFQF 101
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
669-785 7.88e-14

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: 68.81  E-value: 7.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPanlkLIGALLEDMVQHVE------LCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQ-QQ 741
Cdd:cd19925    2 NVLIVEDDP----MVAEIHRAYVEQVPgftvigTAGTGEEALKLLKERQPDLILLDIYLPDGNGL---DLLRELRAAgHD 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446108595 742 TPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYK 785
Cdd:cd19925   75 VDVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERYR 118
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
384-521 8.35e-14

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 74.11  E-value: 8.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 384 HDKGLELTLNIKSDVPDNVIGDPLrLQQIITNLVGNAI-----KFTENGNIDILVEKralSNTKVQIEVqiRDTGIGIPE 458
Cdd:COG3290  258 RERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIeavekLPEEERRVELSIRD---DGDELVIEV--EDSGPGIPE 331
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446108595 459 RDQSRLFQafrqaDASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLN 521
Cdd:COG3290  332 ELLEKIFE-----RGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
673-779 1.21e-13

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: 68.35  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 673 VDDNPANLKLIGALLEDMVQ-HVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTAHA 751
Cdd:cd17552    7 IDDEEDIREVVQACLEKLAGwEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLTAKA 86
                         90       100
                 ....*....|....*....|....*...
gi 446108595 752 MAGQKEKLLGAGMSDYLAKPIEEERLHN 779
Cdd:cd17552   87 QPSDRQRFASLGVAGVIAKPFDPLTLAE 114
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
296-511 1.43e-13

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 73.08  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 296 FLANMSHELRTPLNGVigftRLTLK-------TELTP-TQR-DHL-NTIE------RSANNLLAIINDVLDFskleagkl 359
Cdd:PRK10755 140 FTADVAHELRTPLAGI----RLHLEllekqhhIDVAPlIARlDQMmHTVEqllqlaRAGQSFSSGHYQTVKL-------- 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 360 iLESIPFPLRSTLDEVVTLLAHSshdkgLELTLnikSDVPDNVIGDPLRLQQIITNLVGNAIKFT-ENGNIDILvekraL 438
Cdd:PRK10755 208 -LEDVILPSQDELSEMLEQRQQT-----LLLPE---SAADITVQGDATLLRLLLRNLVENAHRYSpEGSTITIK-----L 273
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446108595 439 SNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADasisRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGST 511
Cdd:PRK10755 274 SQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHGQFFLQNRQERSGT 342
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
297-500 1.68e-13

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 73.81  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 297 LANMSHELRTPLngvigfTRLTLKTELTptQRDH-----LNTIERSANNLLAIINDVLDFSKLEAgKLILESIPFPLRST 371
Cdd:PRK09470 247 LSDISHELRTPL------TRLQLATALL--RRRQgeskeLERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSL 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 372 LDEVVTLLAHSSHDKGLELTLnikSDVPDN--VIGDPLRLQQIITNLVGNAIKFTeNGNIDIlvekrALSNTKVQIEVQI 449
Cdd:PRK09470 318 WSEVLEDAKFEAEQMGKSLTV---SAPPGPwpINGNPNALASALENIVRNALRYS-HTKIEV-----AFSVDKDGLTITV 388
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446108595 450 RDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDI 500
Cdd:PRK09470 389 DDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWV 439
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
182-509 1.94e-13

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 74.34  E-value: 1.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 182 VMMLFCIGIALIFGWRL-MRDVTGPIRNMVNTVDRIRRGQLDsrvegfmlgeLDMLKNG---INSMAMSLAAYHEEMQhn 257
Cdd:COG4192  330 AIALLSLLLAVLINYFYvRRRLVKRLNALSDAMAAIAAGDLD----------VPIPVDGndeIGRIARLLRVFRDQAI-- 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 258 idQATSDLREtleqmEIQNVELDLAKKRAQEAARIKSEFLA-------NMSHELRTPLNG---VIGFTRLTLKTELTPTQ 327
Cdd:COG4192  398 --EKTQELET-----EIEERKRIEKNLRQTQDELIQAAKMAvvgqtmtSLAHELNQPLNAmsmYLFSAKKALEQENYAQL 470
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 328 RDHLNTIERSANNLLAIINDVLDFSKLEAGKLIlesiPFPLRSTLDEVVTLLAhsSHDKGLELTLNIKSDVpdNVIGDPL 407
Cdd:COG4192  471 PTSLDKIEGLIERMDKIIKSLRQFSRKSDTPLQ----PVDLRQVIEQAWELVE--SRAKPQQITLHIPDDL--MVQGDQV 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 408 RLQQIITNLVGNAIK-FTENGNIDILVekraLSNTKvQIEVQIRDTGIGIPERDqsRLFQAFrqadasISRRHGGTGLGL 486
Cdd:COG4192  543 LLEQVLVNLLVNALDaVATQPQISVDL----LSNAE-NLRVAISDNGNGWPLVD--KLFTPF------TTTKEVGLGLGL 609
                        330       340
                 ....*....|....*....|...
gi 446108595 487 VITQKLVNEMGGDISFHSQPNRG 509
Cdd:COG4192  610 SICRSIMQQFGGDLYLASTLERG 632
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-501 2.09e-13

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: 66.97  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFTengNIDILVekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVI 488
Cdd:cd16949    1 LARALENVLRNALRYS---PSKILL---DISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAI 74
                         90
                 ....*....|...
gi 446108595 489 TQKLVNEMGGDIS 501
Cdd:cd16949   75 AERAIEQHGGKIK 87
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
668-771 2.12e-13

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 67.80  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDmVQHVELCD---SGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlphQQQTPV 744
Cdd:cd17541    1 IRVLIVDDSAVMRKLLSRILES-DPDIEVVGtarDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMA---ERPTPV 76
                         90       100
                 ....*....|....*....|....*....
gi 446108595 745 IAVTAHAMAGQKE--KLLGAGMSDYLAKP 771
Cdd:cd17541   77 VMVSSLTEEGAEItlEALELGAVDFIAKP 105
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
6-500 3.79e-13

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 73.22  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   6 LRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRA 85
Cdd:COG2770   40 LLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  86 ISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELD 165
Cdd:COG2770  120 LLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLL 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 166 LKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAM 245
Cdd:COG2770  200 LVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMAD 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 246 SLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELTP 325
Cdd:COG2770  280 SLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAAL 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 326 TQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIGD 405
Cdd:COG2770  360 LLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALE 439
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 406 PLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLG 485
Cdd:COG2770  440 LAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLL 519
                        490
                 ....*....|....*
gi 446108595 486 LVITQKLVNEMGGDI 500
Cdd:COG2770  520 LLEAEALEVAEELLE 534
pleD PRK09581
response regulator PleD; Reviewed
668-774 5.47e-13

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 72.24  E-value: 5.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MT--VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVI 745
Cdd:PRK09581   1 MTarILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVV 80
                         90       100
                 ....*....|....*....|....*....
gi 446108595 746 AVTAHAMAGQKEKLLGAGMSDYLAKPIEE 774
Cdd:PRK09581  81 MVTALDDPEDRVRGLEAGADDFLTKPIND 109
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
673-777 7.23e-13

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 65.98  E-value: 7.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 673 VDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqqQTPVIAVTAHA- 751
Cdd:cd17550    4 VDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYP--DLPVIMISGHGt 81
                         90       100
                 ....*....|....*....|....*...
gi 446108595 752 --MAGQKEKLlgaGMSDYLAKPIEEERL 777
Cdd:cd17550   82 ieTAVKATKL---GAYDFIEKPLSLDRL 106
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
822-889 9.10e-13

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: 64.71  E-value: 9.10e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446108595 822 KTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSG 889
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELEDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDAL 68
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
668-781 1.04e-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: 65.44  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDM-VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGI---RACELIHQLPHqqqTP 743
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELgFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLellKTIRADGALSH---LP 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446108595 744 VIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLL 781
Cdd:cd19923   78 VLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-512 1.20e-12

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: 65.00  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 412 IITNLVGNAIKFT-ENGNIDILVEKralsnTKVQIEVQIRDTGIGIPERDQSRLFQAF------RQADASisrrhggTGL 484
Cdd:cd16948    9 IIGQIVSNALKYSkQGGKIEIYSET-----NEQGVVLSIKDFGIGIPEEDLPRVFDKGftgengRNFQES-------TGM 76
                         90       100
                 ....*....|....*....|....*...
gi 446108595 485 GLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:cd16948   77 GLYLVKKLCDKLGHKIDVESEVGEGTTF 104
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-512 1.47e-12

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


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 64.72  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFT-ENGNIDIlveKRALSNTKVQIEvqIRDTGIGIPERDQSRLFQAFRQADasISRRHGGTGLGLV 487
Cdd:cd16923    1 LQRVFSNLLSNAIKYSpENTRIYI---TSFLTDDVVNIM--FKNPSSHPLDFKLEKLFERFYRGD--NSRNTEGAGLGLS 73
                         90       100
                 ....*....|....*....|....*
gi 446108595 488 ITQKLVNEMGGDISFHSQpNRGSTF 512
Cdd:cd16923   74 IAKAIIELHGGSASAEYD-DNHDLF 97
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
668-784 1.60e-12

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: 64.87  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNP-ANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIA 746
Cdd:cd17593    1 MKVLICDDSSmARKQLARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPV--EQLETKVIV 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRY 784
Cdd:cd17593   79 VSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
670-778 1.75e-12

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: 64.91  E-value: 1.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPAnlklIGALLEDMVQH----VELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVI 745
Cdd:cd17572    1 VLLVEDSPS----LAALYQEYLSDegykVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQE--RSLPTSVI 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446108595 746 AVTAHA---MAGQKEKLlgaGMSDYLAKPIEEERLH 778
Cdd:cd17572   75 VITAHGsvdIAVEAMRL---GAYDFLEKPFDADRLR 107
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
671-783 2.13e-12

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: 64.55  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 671 MAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQ-QTPVIAVTA 749
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGL---EVLKSLREEGiETPVLLLTA 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEeerLHNLLLR 783
Cdd:cd17625   78 LDAVEDRVKGLDLGADDYLPKPFS---LAELLAR 108
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
384-516 2.32e-12

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 70.71  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 384 HDKGLELTLNIKSDVPDNviGDPLRLQQIIT---NLVGN---AIKFTENGNIDILVEKRalsNTKVQIEVQirDTGIGIP 457
Cdd:PRK11086 408 RELGITLIISEDSQLPDS--GDEDQVHELITilgNLIENaleAVGGEEGGEISVSLHYR---NGWLHCEVS--DDGPGIA 480
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446108595 458 ERDQSRLFqafrqaDASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHI 516
Cdd:PRK11086 481 PDEIDAIF------DKGYSTKGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
673-786 4.06e-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: 4.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 673 VDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVTAHAM 752
Cdd:COG4567   10 VDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE--RDPDARIVVLTGYAS 87
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446108595 753 AGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKP 786
Cdd:COG4567   88 IATAVEAIKLGADDYLAKPADADDLLAALERAEG 121
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
668-749 4.44e-12

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: 63.39  E-value: 4.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIhqLPHQQQTPVIAV 747
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKI--REKKPDLPVIIC 78

                 ..
gi 446108595 748 TA 749
Cdd:cd17554   79 TA 80
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
670-771 4.58e-12

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: 63.23  E-value: 4.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPanlKLIGALLEDMVQH---VELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIA 746
Cdd:cd19935    1 ILVVEDEK---KLAEYLKKGLTEEgyaVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLM 75
                         90       100
                 ....*....|....*....|....*
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd19935   76 LTARDSVEDRVKGLDLGADDYLVKP 100
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
668-722 5.59e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.43  E-value: 5.59e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 446108595   668 MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMP 722
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
669-776 7.69e-12

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: 62.89  E-value: 7.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPAnlklIGALLEDMVQ----HVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLphQQQTPV 744
Cdd:COG5803    4 KILIVDDQAG----IRMLLKEVLKkegyEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEI--DPDIPV 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446108595 745 IAVTAHAMAGQKEKLLGAGMSDYLAKP--IEEER 776
Cdd:COG5803   78 IMMTAYGELDMVEEAKELGAKGYFTKPfdIDELR 111
glnL PRK11073
nitrogen regulation protein NR(II);
287-506 7.81e-12

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 67.80  E-value: 7.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 287 QEAARiksEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLeaGKLILESIpf 366
Cdd:PRK11073 127 QVAAR---DLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLLGPQRP--GTHVTESI-- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 367 plRSTLDEVVTLLAhsshdkgLELTLNIK------SDVPDnVIGDPLRLQQIITNLVGNAIKF--TENGNIdILVEKRAL 438
Cdd:PRK11073 200 --HKVAERVVQLVS-------LELPDNVRlirdydPSLPE-LAHDPDQIEQVLLNIVRNALQAlgPEGGTI-TLRTRTAF 268
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446108595 439 SNT------KVQIEVQIRDTGIGIPERDQSRLFQAFrqadasISRRHGGTGLGLVITQKLVNEMGGDISFHSQP 506
Cdd:PRK11073 269 QLTlhgeryRLAARIDIEDNGPGIPPHLQDTLFYPM------VSGREGGTGLGLSIARNLIDQHSGKIEFTSWP 336
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
665-783 9.76e-12

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 68.34  E-value: 9.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 665 KLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIhqLPHQQQTPV 744
Cdd:PRK11361   2 TAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEM--RSHETRTPV 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446108595 745 IAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLhNLLLR 783
Cdd:PRK11361  80 ILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL-NLIVQ 117
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
405-506 1.13e-11

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: 62.09  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 405 DPLRLQQIITNLVGNAIKFT-ENGNIDILVEKRAlsntkVQIEVQIRDTGIGIPERDQSRLFQAFrqadASISRRHGG-- 481
Cdd:cd16945    1 DPFLLRQAINNLLDNAIDFSpEGGLIALQLEADT-----EGIELLVFDEGSGIPDYALNRVFERF----YSLPRPHSGqk 71
                         90       100
                 ....*....|....*....|....*.
gi 446108595 482 -TGLGLVITQKLVNEMGGDISFHSQP 506
Cdd:cd16945   72 sTGLGLAFVQEVAQLHGGRITLRNRP 97
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
48-516 1.59e-11

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 67.35  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  48 IIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGD 127
Cdd:COG2972   27 LSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLILLLLLLLLLLLILLLSLLLLLALI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 128 IMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIR 207
Cdd:COG2972  107 LLLALLLLLSILLLILGLLLIILLLLSLLGWTLVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIK 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 208 NMVNTVDRIRRGQLdSRVEGFMLGELDMLKNGINSMAMSLAAYHEEmqhnidqatsdlretLEQMEIQNVELDLAKKRAQ 287
Cdd:COG2972  187 RLKKAMKKVEKGDL-VRLEVSGNDEIGILARSFNEMVERIKELIEE---------------VYELELEKKEAELKALQAQ 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 288 eaarIKSEFLANMshelrtplngvigftrltlkteltptqrdhLNTIersanNLLAIIND-------VLDFSKLeagkli 360
Cdd:COG2972  251 ----INPHFLFNT------------------------------LNSI-----RWLAELEDpeeaeemLEALSKL------ 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 361 lesipfpLRSTL---DEVVTL---LAH---------SSHDKGLELTLNIKSDVPDNVIgdPLRLQQIitnLVGNAIKF-- 423
Cdd:COG2972  286 -------LRYSLskgDELVTLeeeLELiksyleiqkLRFGDRLEVEIEIDEELLDLLI--PKLILQP---LVENAIEHgi 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 424 ---TENGNIDILVEKRalsNTKVQIEVqiRDTGIGIPERDQSRLFQAFrqadasiSRRHGGTGLGLVITQ---KLVNEMG 497
Cdd:COG2972  354 epkEGGGTIRISIRKE---GDRLVITV--EDNGVGMPEEKLEKLLEEL-------SSKGEGRGIGLRNVRerlKLYYGEE 421
                        490
                 ....*....|....*....
gi 446108595 498 GDISFHSQPNRGSTFWFHI 516
Cdd:COG2972  422 YGLEIESEPGEGTTVTIRI 440
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
670-771 1.79e-11

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: 61.62  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTA 749
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                         90       100
                 ....*....|....*....|....
gi 446108595 750 HA--MAGQKEKLLGAgmSDYLAKP 771
Cdd:cd17602   81 KDglVDRIRAKMAGA--SGYLTKP 102
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
669-774 2.54e-11

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: 61.45  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLED----MVQhvelCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQ-QTP 743
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDsgfqVLQ----AADGRQGLELFRSEQPDLVLCDLRMPEMDGL---EVLKQITKESpDTP 74
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446108595 744 VIAVTAHAMAGQKEKLLGAGMSDYLAKPIEE 774
Cdd:cd17555   75 VIVVSGAGVMSDAVEALRLGAWDYLTKPIED 105
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
668-777 2.85e-11

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 61.28  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPanlkLIGALLEDMVQH-----VELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACElihQLPHQQQT 742
Cdd:cd19932    1 VRVLIAEDEA----LIRMDLREMLEEagyevVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAK---IITSENIA 73
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446108595 743 PVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERL 777
Cdd:cd19932   74 PIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
828-889 3.02e-11

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: 60.06  E-value: 3.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446108595  828 DMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSG 889
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREG 62
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
670-785 4.36e-11

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: 61.01  E-value: 4.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDM--VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQTP-VIA 746
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHpdIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGL---ELAKKLSKLAKPPlIVF 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446108595 747 VTAHAMAGQKEKLLGAgmSDYLAKPIEEERLHNLLLRYK 785
Cdd:cd17532   78 VTAYDEYAVEAFELNA--VDYLLKPFSEERLAEALAKLR 114
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-515 6.06e-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: 6.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFTengniDILVEKRALSNTKvQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVI 488
Cdd:cd16939    1 MARALDNLLRNALRYA-----HRTVRIALLVSGG-RLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                         90       100
                 ....*....|....*....|....*..
gi 446108595 489 TQKLVNEMGGDISFHSQPNRGSTFWFH 515
Cdd:cd16939   75 VHRVALWHGGHVECDDSELGGACFRLT 101
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
670-777 6.23e-11

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: 60.19  E-value: 6.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVTA 749
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTA 78
                         90       100
                 ....*....|....*....|....*...
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEEERL 777
Cdd:cd17624   79 RDGVDDRVAGLDAGADDYLVKPFALEEL 106
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
281-523 9.64e-11

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 65.72  E-value: 9.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 281 LAKKRAQEAARI-------KSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSK 353
Cdd:PRK10618 431 LVNKKLQQAQREyeknqqaRKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNM 510
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 354 LEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILV 433
Cdd:PRK10618 511 LETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEV 590
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 434 EKRAlsNTKVQIEVQIRDTGIGIPERDQSRLFQAFrQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFW 513
Cdd:PRK10618 591 DQDE--SSPDRLTIRILDTGAGVSIKELDNLHFPF-LNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYS 667
                        250
                 ....*....|
gi 446108595 514 FHINLDLNPN 523
Cdd:PRK10618 668 IHLKMLAADP 677
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
670-777 1.74e-10

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: 59.25  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLeDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVta 749
Cdd:cd17539    1 VLLVDDRPSSAERIAAML-SSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAV-- 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446108595 750 hAMAGQKEKLLGA---GMSDYLAKPIEEERL 777
Cdd:cd17539   78 -ADPGDRGRLIRAleiGVNDYLVRPIDPNEL 107
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
669-783 2.77e-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: 58.52  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQL-PHQQQTPVIAV 747
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGL---EVLRRLrADGPDVPVLFL 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKP--IEE--ERLHNLLLR 783
Cdd:cd17615   78 TAKDSVEDRIAGLTAGGDDYVTKPfsLEEvvARLRALLRR 117
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
670-783 2.93e-10

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: 58.55  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLphQQQTPVIAVTA 749
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA--GNDLPILVLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEEE----RLHNLLLR 783
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKPFALEellaRVRALLRR 116
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-500 4.27e-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: 57.46  E-value: 4.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFtenGNIDIlveKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADasISRRHGGTGLGLVI 488
Cdd:cd16950    1 LKRVLSNLVDNALRY---GGGWV---EVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGD--NARGTSGTGLGLAI 72
                         90
                 ....*....|..
gi 446108595 489 TQKLVNEMGGDI 500
Cdd:cd16950   73 VQRISDAHGGSL 84
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
670-771 5.37e-10

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: 57.39  E-value: 5.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQM---------PFDLILMDIQMPDMDGIRACELIHQLPHQQ 740
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlskELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446108595 741 QTPVIAVTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
669-771 5.38e-10

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: 57.64  E-value: 5.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVT 748
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                         90       100
                 ....*....|....*....|...
gi 446108595 749 AHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd17618   82 ARGEEEDKVRGLEAGADDYITKP 104
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
670-777 5.78e-10

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 57.42  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQ-QTPVIAVT 748
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGY---EVLRTLRLAKvKTPILILS 77
                         90       100
                 ....*....|....*....|....*....
gi 446108595 749 AHAMAGQKEKLLGAGMSDYLAKPIEEERL 777
Cdd:cd17616   78 GLADIEDKVKGLGFGADDYMTKPFHKDEL 106
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
669-777 6.98e-10

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: 59.34  E-value: 6.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQT-PVIAV 747
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGL---ELQEELAARGSPlPVIFL 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446108595 748 TAHA---MAGQKEKllgAGMSDYLAKPIEEERL 777
Cdd:COG4566   78 TGHGdvpMAVRAMK---AGAVDFLEKPFDDQAL 107
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
668-733 7.01e-10

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 57.98  E-value: 7.01e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDM--VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELI 733
Cdd:COG2197    2 IRVLIVDDHPLVREGLRALLEAEpdIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
670-781 9.07e-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: 57.02  E-value: 9.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVER--AKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVI-A 746
Cdd:cd19933    3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLlaSAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLIvA 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLL 781
Cdd:cd19933   83 LTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PRK10337 PRK10337
sensor protein QseC; Provisional
296-509 1.02e-09

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 61.97  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 296 FLANMSHELRTPLngvigfTRLTLKTELT------PTQRDH----LNT-IERsANNLlaiINDVLDFSKLEAGKLILESI 364
Cdd:PRK10337 240 FTSDAAHELRSPL------AALKVQTEVAqlsdddPQARKKallqLHAgIDR-ATRL---VDQLLTLSRLDSLDNLQDVA 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 365 PFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDvpdNVI--GDPLRLQQIITNLVGNAIKFTENGN-IDILVEKRALsnt 441
Cdd:PRK10337 310 EIPLEDLLQSAVMDIYHTAQQAGIDVRLTLNAH---PVIrtGQPLLLSLLVRNLLDNAIRYSPQGSvVDVTLNARNF--- 383
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446108595 442 kvqievQIRDTGIGIPERDQSRLFQAF-RQADASISrrhgGTGLGLVITQKLVNEMGGDISFHSQPNRG 509
Cdd:PRK10337 384 ------TVRDNGPGVTPEALARIGERFyRPPGQEAT----GSGLGLSIVRRIAKLHGMNVSFGNAPEGG 442
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-514 1.28e-09

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: 56.31  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNA---IKFTENGNIDIlvekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQadasiSRRHG-GTGL 484
Cdd:cd16976    1 IQQVLMNLLQNAldaMGKVENPRIRI-----AARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFT-----TKPVGkGTGL 70
                         90       100       110
                 ....*....|....*....|....*....|
gi 446108595 485 GLVITQKLVNEMGGDISFHSQPNRGSTFWF 514
Cdd:cd16976   71 GLSISYGIVEEHGGRLSVANEEGAGARFTF 100
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
669-771 1.30e-09

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 56.36  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQ-MPFDLILMDIQMPDMDGIracELIHQLPH-QQQTPVIA 746
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQgKDIDIVVTDIVMPEMDGI---ELAREARKiDPDVKILF 77
                         90       100
                 ....*....|....*....|....*
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd18160   78 ISGGAAAAPELLSDAVGDNATLKKP 102
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
669-777 1.49e-09

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 56.45  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQ-QTPVIAV 747
Cdd:cd17537    2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGL---ELQDELLARGsNIPIIFI 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446108595 748 TAHA---MAGQKEKllgAGMSDYLAKPIEEERL 777
Cdd:cd17537   79 TGHGdvpMAVEAMK---AGAVDFLEKPFRDQVL 108
fixJ PRK09390
response regulator FixJ; Provisional
669-777 1.56e-09

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 58.48  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQT-PVIAV 747
Cdd:PRK09390   5 VVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGI---ELLRRLKARGSPlPVIVM 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446108595 748 TAHA---MAGQKEKLlgaGMSDYLAKPIEEERL 777
Cdd:PRK09390  82 TGHGdvpLAVEAMKL---GAVDFIEKPFEDERL 111
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
670-771 1.67e-09

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: 56.01  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVTA 749
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQ--RLPQTPVAVITA 78
                         90       100
                 ....*....|....*....|..
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd19926   79 YGSLDTAIEALKAGAFDFLTKP 100
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
669-727 2.43e-09

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: 55.87  E-value: 2.43e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGI 727
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGA 60
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
667-777 2.57e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 60.16  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 667 AMTVMAVDDNPANLKLIGALLE---DMvqhvELCDS---GHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQL-Phq 739
Cdd:PRK00742   3 KIRVLVVDDSAFMRRLISEILNsdpDI----EVVGTapdGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLrP-- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446108595 740 qqTPVIAVTAHAMAGQKEKL--LGAGMSDYLAKPIEEERL 777
Cdd:PRK00742  77 --TPVVMVSSLTERGAEITLraLELGAVDFVTKPFLGISL 114
PRK15115 PRK15115
response regulator GlrR; Provisional
664-778 3.43e-09

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 60.24  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 664 SKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQ-T 742
Cdd:PRK15115   2 SRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGM---QLFAEIQKVQPgM 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446108595 743 PVIAVTAH-----AMAGQKEkllgaGMSDYLAKPIEEERLH 778
Cdd:PRK15115  79 PVIILTAHgsipdAVAATQQ-----GVFSFLTKPVDRDALY 114
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-512 6.61e-09

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: 54.22  E-value: 6.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 412 IITNLVGNAIKF---TENGNIDILVEKRAlSNTKVQIEVqiRDTGIGIPERDQSRLFQAfrqadASISRRHGGTGLGLVI 488
Cdd:cd16915    4 IVGNLIDNALDAlaaTGAPNKQVEVFLRD-EGDDLVIEV--RDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLAL 75
                         90       100
                 ....*....|....*....|....
gi 446108595 489 TQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:cd16915   76 VRQSVERLGGSITVESEPGGGTTF 99
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
670-780 6.66e-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: 54.83  E-value: 6.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMP-FDLILMDIQMPDMDGiraCELIHQLPHQ---QQTPVI 745
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDG---FELVREIRKKysrDQLAII 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446108595 746 AVTAHAMAGQKEKLLGAGMSDYLAKPIEEERL-----HNL 780
Cdd:cd17544   80 GISASGDNALSARFIKAGANDFLTKPFLPEEFycrvtQNL 119
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
670-777 6.89e-09

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: 54.40  E-value: 6.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlphQQQTPVIAVTA 749
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA---ESGVPIVMLTA 79
                         90       100
                 ....*....|....*....|....*...
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEEERL 777
Cdd:cd17626   80 KSDTVDVVLGLESGADDYVAKPFKPKEL 107
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
405-519 7.25e-09

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: 54.08  E-value: 7.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 405 DPLRLQQIITNLVGNAIKFTENGNID-ILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFrqadasISRRHGGTG 483
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEGRPSDvGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPY------VTTRPKGTG 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446108595 484 LGLVITQKLVNEMGGDISFHSQPNRGStfWFHINLD 519
Cdd:cd16944   75 LGLAIVKKIMEEHGGRISLSNREAGGA--CIRIILP 108
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
670-777 7.97e-09

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: 54.80  E-value: 7.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqqQTPVIAVTA 749
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDP--DLPVILITG 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446108595 750 H---AMAGQKeklLGAGMSDYLAKPIEEERL 777
Cdd:cd17549   79 HgdvPMAVEA---MRAGAYDFLEKPFDPERL 106
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
669-771 9.04e-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: 9.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPAnlklIGALLEDMVQH----VELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPhqqQTPV 744
Cdd:cd19938    1 RILIVEDEPK----LAQLLIDYLRAagyaPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPI 73
                         90       100
                 ....*....|....*....|....*....
gi 446108595 745 IAVTAHamAGQKEKLLG--AGMSDYLAKP 771
Cdd:cd19938   74 IMVTAR--VEEIDRLLGleLGADDYICKP 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
670-783 1.19e-08

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 53.83  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQT-PVIAVT 748
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGL---SVLRRWRSEGRAtPVLILT 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446108595 749 AHAMAGQKEKLLGAGMSDYLAKP--IEE--ERLHNLLLR 783
Cdd:cd19934   78 ARDSWQDKVEGLDAGADDYLTKPfhIEEllARLRALIRR 116
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
670-771 1.22e-08

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: 53.85  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQTPVIAVTA 749
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGL---DVLKELRKTSQVPVLMLTA 77
                         90       100
                 ....*....|....*....|....
gi 446108595 750 HamAGQKEKLLG--AGMSDYLAKP 771
Cdd:cd17623   78 R--GDDIDRILGleLGADDYLPKP 99
PRK10610 PRK10610
chemotaxis protein CheY;
668-781 2.21e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 53.44  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDM-VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIA 746
Cdd:PRK10610   6 LKFLVVDDFSTMRRIVRNLLKELgFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLM 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446108595 747 VTAHAmagQKEKLLG---AGMSDYLAKPIE----EERLHNLL 781
Cdd:PRK10610  86 VTAEA---KKENIIAaaqAGASGYVVKPFTaatlEEKLNKIF 124
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
398-511 2.30e-08

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: 53.62  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 398 VPDNVIGDPLRLQQIITNLVGNAIKFTENG-----------------NIDILVEKRALSNTKVQIEVQIRDTGIGIPERD 460
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGgnitfrvfleggsedrsDRDWGPWRPSMSDESVEIRFEVEINDSGSPSIE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446108595 461 QSRLFQafrqadaSISRRHG----GTGLGLVITQKLVNEMGGDISfhSQPNRGST 511
Cdd:cd16938   81 SASMRN-------SLNRRYNlselGEHLSFSICKQLVQLMGGNIW--IVPGSGLG 126
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
404-520 2.82e-08

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: 52.66  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 404 GDPLRLQQIITNLVGNAIKFT--ENGNIDILVEKR----ALSNTKVQIEVQIRDTGIGIPERDQSRLFQafrqadasisR 477
Cdd:cd16932    2 GDQIRLQQVLADFLLNAVRFTpsPGGWVEIKVSPTkkqiGDGVHVIHLEFRITHPGQGLPEELVQEMFE----------E 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446108595 478 RHGGT--GLGLVITQKLVNEMGGDISFHSQPNRGStfwFHINLDL 520
Cdd:cd16932   72 NQWTTqeGLGLSISRKLVKLMNGDVRYLREAGRSY---FLITLEL 113
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
670-782 2.97e-08

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 52.71  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTA 749
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEEE----RLHNLLL 782
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKyllsRIKYILV 117
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
656-786 3.14e-08

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 55.46  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 656 TLLPVTDESKlamTVMAVDDNPanlKLiGALLEDMVQ----HVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACE 731
Cdd:PRK10710   2 TELPIDENTP---RILIVEDEP---KL-GQLLIDYLQaasyATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCR 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446108595 732 LIHQLphqQQTPVIAVTAHAMagQKEKLLG--AGMSDYLAKPIEEE----RLHNLLLRYKP 786
Cdd:PRK10710  75 EIRRF---SDIPIVMVTAKIE--EIDRLLGleIGADDYICKPYSPRevvaRVKTILRRCKP 130
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
682-774 3.69e-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: 52.66  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 682 LIGAL-----LEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVTAHAMAGQK 756
Cdd:cd19930   10 VRGALaalleLEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE--ELPDTKVLIVTTFGRPGYF 87
                         90       100
                 ....*....|....*....|
gi 446108595 757 EKLLGAGMSDYLAK--PIEE 774
Cdd:cd19930   88 RRALAAGVDGYVLKdrPIEE 107
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
694-771 5.01e-08

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 51.89  E-value: 5.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446108595 694 VELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd19919   27 VTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ--RHPDLPVIIMTAHSDLDSAVSAYQGGAFEYLPKP 102
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
670-777 1.34e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 53.27  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQmPFDLILMDIQMPDMDGIracELIHQLPHQQQTPVIAVTA 749
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGI---DTLKELRQTHQTPVIMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 446108595 750 HamAGQKEKLLG--AGMSDYLAKPIEEERL 777
Cdd:PRK10955  80 R--GSELDRVLGleLGADDYLPKPFNDREL 107
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
670-772 1.89e-07

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: 50.44  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVE-----------RAKQMPFDLILMDIQMPDMDGIRACELIHQLPH 738
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEflgledeedssNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446108595 739 QQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPI 772
Cdd:cd17581   81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
670-781 2.00e-07

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 50.45  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACElihQLPHQQQTPVIAVTA 749
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCR---DLRPKYQGPILLLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEEE----RLHNLL 781
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVKPVEPAvllaRLRALL 115
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
668-771 2.36e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 53.73  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPanlkLIGALLEDMVQHV---ELCDS---GHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQL-Phqq 740
Cdd:PRK12555   1 MRIGIVNDSP----LAVEALRRALARDpdhEVVWVatdGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAErP--- 73
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446108595 741 qTPVIAVTAHAMAGQKEKL--LGAGMSDYLAKP 771
Cdd:PRK12555  74 -CPILIVTSLTERNASRVFeaMGAGALDAVDTP 105
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
668-771 2.54e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 52.66  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLK-LIGAL-LEDMVqhVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPhqQQTPVI 745
Cdd:PRK11083   4 PTILLVEDEQAIADtLVYALqSEGFT--VEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFH--PALPVI 79
                         90       100
                 ....*....|....*....|....*...
gi 446108595 746 AVTAHamAGQKEKLLG--AGMSDYLAKP 771
Cdd:PRK11083  80 FLTAR--SDEVDRLVGleIGADDYVAKP 105
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
405-514 3.09e-07

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


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 49.38  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 405 DPLRLQQIITNLVGNAIKFT-ENGNIDILVEkralsNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASisRRHGG-T 482
Cdd:cd16975    1 DTLLLSRALINIISNACQYApEGGTVSISIY-----DEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTS--RRSGGhY 73
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446108595 483 GLGLVITQKLVNEMGGDISFhSQPNRGS---TFWF 514
Cdd:cd16975   74 GMGLYIAKNLVEKHGGSLII-ENSQKGGaevTVKI 107
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
670-773 3.10e-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: 49.68  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQqqtPVIAVTA 749
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHV---PILMLTA 78
                         90       100
                 ....*....|....*....|....*.
gi 446108595 750 HamAGQKEKLLG--AGMSDYLAKPIE 773
Cdd:cd19939   79 R--TEEMDRVLGleMGADDYLCKPFS 102
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
263-509 3.81e-07

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


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 53.75  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  263 SDLRETLEQMEIQNVELDLAKKRAQEAARiksEFLANMSHELRTPLNgVIGFTRLTLK----TELTPTQRDHLNTIERSA 338
Cdd:TIGR02938 249 SNLREEQERARLSALQALMAEEERLEAIR---ETLSAAIHRLQGPMN-LISAAISVLQrrgdDAGNPASAAMLQQALSAG 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  339 NNLLAIINDVLDFSKLEAGKlilesiPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPdNVIGDPLRLQQIITNLVG 418
Cdd:TIGR02938 325 REHMEALRQVIPQSPQEIVV------PVNLNQILRDVITLSTPRLLAAGIVVDWQPAATLP-AILGRELQLRSLFKALVD 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  419 NAIkftENGNIDiLVEKRALS-NTKVQ---IEVQIRDTGIGIPERDQSRLFQAFRQADASiSRRHGGTGLGLVitQKLVN 494
Cdd:TIGR02938 398 NAI---EAMNIK-GWKRRELSiTTALNgdlIVVSILDSGPGIPQDLRYKVFEPFFTTKGG-SRKHIGMGLSVA--QEIVA 470
                         250
                  ....*....|....*
gi 446108595  495 EMGGDISFHSQPNRG 509
Cdd:TIGR02938 471 DHGGIIDLDDDYSEG 485
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
1-290 5.05e-07

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 53.49  E-value: 5.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   1 MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHS 80
Cdd:COG0840    5 LLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  81 DIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYI 160
Cdd:COG0840   85 LLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 161 ALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI 240
Cdd:COG0840  165 ALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAF 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446108595 241 NSMAMSLAayheEMQHNIDQATSDLRETLEQMEIQNVELdlaKKRAQEAA 290
Cdd:COG0840  245 NRMIENLR----ELVGQVRESAEQVASASEELAASAEEL---AAGAEEQA 287
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
673-781 1.09e-06

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: 48.57  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 673 VDDNPANLKLI-GALLEDMVQH-VELCDSGHQAVE------RAKQMPF-DLILMDIQMPDMDGIRACELIHQLPHQQQTP 743
Cdd:cd17557    5 VEDNPGDAELIqEAFKEAGVPNeLHVVRDGEEALDflrgegEYADAPRpDLILLDLNMPRMDGFEVLREIKADPDLRRIP 84
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446108595 744 VIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLL 781
Cdd:cd17557   85 VVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAI 122
PRK15479 PRK15479
transcriptional regulator TctD;
714-783 1.11e-06

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 50.49  E-value: 1.11e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446108595 714 LILMDIQMPDMDGIracELIHQLPHQQQT-PVIAVTAHAMAGQKEKLLGAGMSDYLAKPIE----EERLHNLLLR 783
Cdd:PRK15479  47 LAVLDINMPGMDGL---EVLQRLRKRGQTlPVLLLTARSAVADRVKGLNVGADDYLPKPFEleelDARLRALLRR 118
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
667-844 1.58e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 50.03  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 667 AMTVMAVDDNPANLKLIGALL--EDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDG------IRACELihqlph 738
Cdd:PRK10651   6 PATILLIDDHPMLRTGVKQLIsmAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGletldkLREKSL------ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 739 qqQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGsgisSRVVTPEVNEIVVnpnATL--DWQLAL 816
Cdd:PRK10651  80 --SGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAG----EMVLSEALTPVLA---ASLraNRATTE 150
                        170       180
                 ....*....|....*....|....*...
gi 446108595 817 RQAAGKTDLARDMLQMLLDFLPevrNKV 844
Cdd:PRK10651 151 RDVNQLTPRERDILKLIAQGLP---NKM 175
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-518 1.59e-06

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 47.57  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 409 LQQIITNLVGNAIKFTENGNIDILVekrALSNTKVQIEVQIRDTGIGIPERDQSRLFQAF---RQADASISRRhggTGLG 485
Cdd:cd16953    1 LGQVLRNLIGNAISFSPPDTGRITV---SAMPTGKMVTISVEDEGPGIPQEKLESIFDRFyteRPANEAFGQH---SGLG 74
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446108595 486 LVITQKLVNEMGGDI--SFHSQPNRGSTFWFHINL 518
Cdd:cd16953   75 LSISRQIIEAHGGISvaENHNQPGQVIGARFTVQL 109
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
670-771 1.76e-06

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: 47.34  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMP-FDLILMDIQMPDMdgIRACELIHQ-LPHQQQTPVIAV 747
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPGG--MNGSQLAEEaRRRRPDLKVLLT 78
                         90       100
                 ....*....|....*....|....
gi 446108595 748 TAHAMAGQKEKLLGAGMsDYLAKP 771
Cdd:cd18161   79 SGYAENAIEGGDLAPGV-DVLSKP 101
HAMP pfam00672
HAMP domain;
197-247 2.05e-06

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 45.69  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446108595  197 RLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSL 247
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
372-512 2.17e-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: 48.01  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 372 LDEVVTLLAHSSHDKGLELTLNIKSDVpdNVIGDPLRLQQIITNLVGNAIKFTeNGNIDIlvekrALSNTKVQIEVQIRD 451
Cdd:cd16954    3 LDSLCSALNKVYQRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWC-LEFVEV-----TARQTDGGLHLIVDD 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446108595 452 TGIGIPERDQSRLFQAFRQADasisRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTF 512
Cdd:cd16954   75 DGPGVPESQRSKIFQRGQRLD----EQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
PRK11517 PRK11517
DNA-binding response regulator HprR;
668-771 2.57e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 49.51  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGiraCELIHQLPHQQQTPVIAV 747
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDG---WQILQTLRTAKQTPVICL 77
                         90       100
                 ....*....|....*....|....
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:PRK11517  78 TARDSVDDRVRGLDSGANDYLVKP 101
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
670-785 2.67e-06

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 47.00  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQTPVIAVTA 749
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGL---SLTRELREQSEVGIILVTG 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKPIEeerLHNLLLRYK 785
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKPFN---PRELLVRAK 112
PRK10693 PRK10693
two-component system response regulator RssB;
696-772 2.72e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 50.37  E-value: 2.72e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446108595 696 LCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACEliHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPI 772
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVE--HLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPV 76
ompR PRK09468
osmolarity response regulator; Provisional
670-771 3.56e-06

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 49.20  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPAnlklIGALLEDMvqhveLCDSGHQ--AVERAKQM-------PFDLILMDIQMPDMDGIRACELIHQlpHQQ 740
Cdd:PRK09468   8 ILVVDDDMR----LRALLERY-----LTEQGFQvrSAANAEQMdrlltreSFHLMVLDLMLPGEDGLSICRRLRS--QNN 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446108595 741 QTPVIAVTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:PRK09468  77 PTPIIMLTAKGEEVDRIVGLEIGADDYLPKP 107
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
445-514 3.69e-06

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: 46.60  E-value: 3.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446108595 445 IEVQIRDTGIGIPERDQSRLFQAFrqadaSISRRHG-GTGLGLVITQKLVNEMGGDISFHSQPNRGSTF--WF 514
Cdd:cd16919   48 VCLEVSDTGSGMPAEVLRRAFEPF-----FTTKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVriYL 115
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
668-785 5.26e-06

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: 46.67  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQ-HVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQT---- 742
Cdd:cd17530    1 LRVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGI---EFLRHLAESHSNaavi 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446108595 743 ------PVIAVTAHAMAGQkeklLGAGMSDYLAKPIEEERLHNLLLRYK 785
Cdd:cd17530   78 lmsgldGGILESAETLAGA----NGLNLLGTLSKPFSPEELTELLTKYT 122
PRK09483 PRK09483
response regulator; Provisional
668-770 5.92e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 48.18  E-value: 5.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDM--VQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIhqLPHQQQTPVI 745
Cdd:PRK09483   2 INVLLVDDHELVRAGIRRILEDIkgIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKI--LRYTPDVKII 79
                         90       100
                 ....*....|....*....|....*
gi 446108595 746 AVTAHAMAGQKEKLLGAGMSDYLAK 770
Cdd:PRK09483  80 MLTVHTENPLPAKVMQAGAAGYLSK 104
PRK10816 PRK10816
two-component system response regulator PhoP;
668-796 6.36e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 48.20  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNpanlkligALLEDMVQhVELCDSGHQ--AVERAKQMPF-------DLILMDIQMPDMDGIracELIHQL-P 737
Cdd:PRK10816   1 MRVLVVEDN--------ALLRHHLK-VQLQDAGHQvdAAEDAKEADYylnehlpDIAIVDLGLPDEDGL---SLIRRWrS 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446108595 738 HQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKP--IEE--ERLHNLLLRykpGSGISSRVVT 796
Cdd:PRK10816  69 NDVSLPILVLTARESWQDKVEVLSAGADDYVTKPfhIEEvmARMQALMRR---NSGLASQVIS 128
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
670-771 7.22e-06

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 45.47  E-value: 7.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPF--DLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAV 747
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
4-519 1.02e-05

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 49.13  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595   4 YSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIV 83
Cdd:COG3920   20 AALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLAAAALA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595  84 RAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALE 163
Cdd:COG3920  100 LALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAALLL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 164 LDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSM 243
Cdd:COG3920  180 LLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 244 AMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLakkRAQEAA-RIKseflaNMshelrtpLNGVIGFTRLTLKTE 322
Cdd:COG3920  260 LLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKEL---LLRELHhRVK-----NN-------LQVVSSLLRLQARRA 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 323 LTPTQRDHLNTIER--SAnnlLAIINDVLdfskLEAGKLilESIPfpLRSTLDEVVTLLAHSSHDKGLELTLNiksdvpd 400
Cdd:COG3920  325 DDPEAREALEESQNriQA---LALVHELL----YQSEDW--EGVD--LRDYLRELLEPLRDSYGGRGIRIELD------- 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 401 nviGDPLRLQQ--------IITNLVGNAIKF----TENGNIDILVEKRAlsntkVQIEVQIRDTGIGIPErdqsrlfqaf 468
Cdd:COG3920  387 ---GPDVELPAdaavplglILNELVTNALKHaflsGEGGRIRVSWRRED-----GRLRLTVSDNGVGLPE---------- 448
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446108595 469 rqaDASISRRhggTGLGLVITQKLVNEMGGDISFHSQPnrGSTFWFHINLD 519
Cdd:COG3920  449 ---DVDPPAR---KGLGLRLIRALVRQLGGTLELDRPE--GTRVRITFPLA 491
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
670-771 1.03e-05

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: 45.49  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHqqqTPVIAVTA 749
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSN---VPIIMLTA 77
                         90       100
                 ....*....|....*....|....
gi 446108595 750 HamAGQKEKLLG--AGMSDYLAKP 771
Cdd:cd17614   78 K--DSEVDKVLGleLGADDYVTKP 99
pleD PRK09581
response regulator PleD; Reviewed
669-777 1.13e-05

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 48.74  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQmPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVT 748
Cdd:PRK09581 157 RILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAET-NYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLV 235
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446108595 749 AhamAGQKEKLLGA---GMSDYLAKPIEEERL 777
Cdd:PRK09581 236 D---EDDDPRLVKAlelGVNDYLMRPIDKNEL 264
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
693-771 1.38e-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: 45.13  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 693 HVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVT-----AHAMAGQKeklLGAgmSDY 767
Cdd:cd17563   26 EVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRA--LQPDARIVVLTgyasiATAVEAIK---LGA--DDY 98

                 ....
gi 446108595 768 LAKP 771
Cdd:cd17563   99 LAKP 102
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
673-771 1.52e-05

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: 44.36  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 673 VDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQTPVIAVTAHam 752
Cdd:cd19936    4 VDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGM---ELLQRLRQKSTLPVIFLTSK-- 78
                         90       100
                 ....*....|....*....|.
gi 446108595 753 AGQKEKLLG--AGMSDYLAKP 771
Cdd:cd19936   79 DDEIDEVFGlrMGADDYITKP 99
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
200-249 1.75e-05

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 43.01  E-value: 1.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 446108595   200 RDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAA 249
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEE 50
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
704-771 1.82e-05

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 47.11  E-value: 1.82e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446108595 704 VERAKQMPfDLILMDIQMPDMDGIracELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:PRK10529  39 LEAATRKP-DLIILDLGLPDGDGI---EFIRDLRQWSAIPVIVLSARSEESDKIAALDAGADDYLSKP 102
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
669-770 4.76e-05

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: 43.94  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALL---EDMVQHveLCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVI 745
Cdd:cd17575    2 MVLLVDDQAIIGEAVRRALadeEDIDFH--YCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPII 79
                         90       100
                 ....*....|....*....|....*
gi 446108595 746 AVTAHAMAGQKEKLLGAGMSDYLAK 770
Cdd:cd17575   80 VLSTKEEPEVKSEAFALGANDYLVK 104
orf27 CHL00148
Ycf27; Reviewed
668-783 5.32e-05

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 45.86  E-value: 5.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACElihQLPHQQQTPVIAV 747
Cdd:CHL00148   7 EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQ---EIRKESDVPIIML 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKPIE----EERLHNLLLR 783
Cdd:CHL00148  84 TALGDVSDRITGLELGADDYVVKPFSpkelEARIRSVLRR 123
PRK09191 PRK09191
two-component response regulator; Provisional
666-749 6.82e-05

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 45.61  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 666 LAMTVMAVDDNPanlkLIGALLEDMVQhvelcDSGHQ----------AVERAKQMPFDLILMDIQMPD-MDGIRAcelIH 734
Cdd:PRK09191 136 VATRVLIIEDEP----IIAMDLEQLVE-----SLGHRvtgiartraeAVALAKKTRPGLILADIQLADgSSGIDA---VN 203
                         90
                 ....*....|....*
gi 446108595 735 QLPHQQQTPVIAVTA 749
Cdd:PRK09191 204 DILKTFDVPVIFITA 218
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
203-247 7.53e-05

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


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 40.89  E-value: 7.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446108595 203 TGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSL 247
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
668-749 7.69e-05

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 44.89  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNP-ANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQTPVIA 746
Cdd:PRK09958   1 MNAIIIDDHPlAIAAIRNLLIKNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGI---QVLETLRKRQYSGIII 77

                 ...
gi 446108595 747 VTA 749
Cdd:PRK09958  78 IVS 80
PRK11697 PRK11697
two-component system response regulator BtsR;
668-783 8.44e-05

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 45.22  E-value: 8.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDmVQHVELCDSGHQAVERAKQM----PfDLILMDIQMPDMDGIracELIHQLPHQQQTP 743
Cdd:PRK11697   2 IKVLIVDDEPLAREELRELLQE-EGDIEIVGECSNAIEAIGAIhrlkP-DVVFLDIQMPRISGL---ELVGMLDPEHMPY 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446108595 744 VIAVTAH---AMAGQKEKLLgagmsDYLAKPIEEERLHNLLLR 783
Cdd:PRK11697  77 IVFVTAFdeyAIKAFEEHAF-----DYLLKPIDPARLAKTLAR 114
PLN03029 PLN03029
type-a response regulator protein; Provisional
658-780 1.59e-04

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 44.25  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 658 LPVTDESKLAmtVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVE--------------------RAKQMPFDLILM 717
Cdd:PLN03029   1 MGITTESQFH--VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKflglheddrsnpdtpsvspnSHQEVEVNLIIT 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446108595 718 DIQMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNL 780
Cdd:PLN03029  79 DYCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRL 141
PRK10336 PRK10336
two-component system response regulator QseB;
668-783 1.69e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.12  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNpanlKLIG----ALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQ-QQT 742
Cdd:PRK10336   1 MRILLIEDD----MLIGdgikTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGR---DILREWREKgQRE 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446108595 743 PVIAVTAHAMAGQKEKLLGAGMSDYLAKP---IE-EERLHNLLLR 783
Cdd:PRK10336  74 PVLILTARDALAERVEGLRLGADDYLCKPfalIEvAARLEALMRR 118
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
670-771 2.02e-04

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 41.41  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACElihQLPHQQQTPVIAVTA 749
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCR---QLRARSNVPVIMVTA 77
                         90       100
                 ....*....|....*....|..
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd17621   78 KDSEIDKVVGLELGADDYVTKP 99
dpiA PRK10046
two-component response regulator DpiA; Provisional
714-785 2.56e-04

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 43.47  E-value: 2.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446108595 714 LILMDIQMPDMDGIracELIHQLpHQQQTP--VIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYK 785
Cdd:PRK10046  53 LILLDNYLPDGRGI---NLLHEL-VQAHYPgdVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFR 122
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
668-771 2.96e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 43.37  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGiraCELIHQLPHQQQ-TPVIA 746
Cdd:PRK09836   1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNG---WDIVRMLRSANKgMPILL 77
                         90       100
                 ....*....|....*....|....*
gi 446108595 747 VTAHAMAGQKEKLLGAGMSDYLAKP 771
Cdd:PRK09836  78 LTALGTIEHRVKGLELGADDYLVKP 102
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
669-785 3.74e-04

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 40.89  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQTPVIAVT 748
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGL---DLLRTIRARSDVPIIIIS 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446108595 749 AHAMAgQKEKLLG--AGMSDYLAKPIEeerLHNLLLRYK 785
Cdd:cd17594   78 GDRRD-EIDRVVGleLGADDYLAKPFG---LRELLARVR 112
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
670-777 4.14e-04

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: 40.79  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLE--DMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAV 747
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIEldPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALRE--EGVSARIVIL 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 446108595 748 TAHAMAGQKEKLLGAGMSDYLAKPIEEERL 777
Cdd:cd19931   79 TVSDAEDDVVTALRAGADGYLLKDMEPEDL 108
PRK10643 PRK10643
two-component system response regulator PmrA;
712-778 6.04e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 42.33  E-value: 6.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446108595 712 FDLILMDIQMPDMDGIracELIHQLPHQQQT-PVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLH 778
Cdd:PRK10643  45 YSLVVLDLGLPDEDGL---HLLRRWRQKKYTlPVLILTARDTLEDRVAGLDVGADDYLVKPFALEELH 109
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
670-772 8.55e-04

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: 39.94  E-value: 8.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDM-VQHVELCDSGHQAVERAKQMPFDLILMDIQMPdmDGIRACELIHQLPHQQQTP----V 744
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLgVTRIDTASSGEEALRMCENKTYDIVLCDYNLG--KGKNGQQLLEELRHKKLISpstvF 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446108595 745 IAVTAHAmagQKEKLLGAGMS---DYLAKPI 772
Cdd:cd17589   79 IMVTGES---SRAMVLSALELepdDYLLKPF 106
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
297-506 9.70e-04

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 42.70  E-value: 9.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 297 LANMSHELRTPLnGVIGFTRLTLKT--ELTPTQRD--HLNTIERSANNllaiINDVLDFSKLEAGKLILESIPFPLRSTL 372
Cdd:PRK10815 270 LTDLTHSLKTPL-AVLQSTLRSLRSgkQMSVEQAEpiMLEQISRISQQ----IGYYLHRASMRSEHNLLSRELHSVAPLL 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 373 DEVVTLLAHSSHDKGLELTLNIKSDVpdNVIGDPLRLQQIITNLVGNAIKFTENgnidiLVEKRAL-SNTKVQIEVQirD 451
Cdd:PRK10815 345 DNLTSALNKVYQRKGVNITLDISPEI--TFVGEKNDFMEVMGNVLDNACKYCLE-----FVEISARqTDEHLHIVVE--D 415
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446108595 452 TGIGIPERDQSRLFQAFRQADasisRRHGGTGLGLVITQKLVNEMGGDISFHSQP 506
Cdd:PRK10815 416 DGPGIPESKRELIFDRGQRAD----TLRPGQGLGLSVAREITEQYEGKISAGDSP 466
PRK10766 PRK10766
two-component system response regulator TorR;
666-785 9.87e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 41.56  E-value: 9.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 666 LAMTVMAVDDNPanlkLIGALLEDMVQH----VELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIracELIHQLPHQQQ 741
Cdd:PRK10766   1 MSYHILVVEDEP----VTRARLQGYFEQegytVSEAASGAGMREIMQNQHVDLILLDINLPGEDGL---MLTRELRSRST 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446108595 742 TPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEeerLHNLLLRYK 785
Cdd:PRK10766  74 VGIILVTGRTDSIDRIVGLEMGADDYVTKPLE---LRELLVRVK 114
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
699-786 1.02e-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: 39.84  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 699 SGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLphQQQTPVIAVTAHAMAG--QKEKLLGAGMsdYLAKPIEEER 776
Cdd:cd17553   32 NGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVI--DENIRVIIMTAYGELDmiQESKELGALT--HFAKPFDIDE 107
                         90
                 ....*....|
gi 446108595 777 LHNLLLRYKP 786
Cdd:cd17553  108 IRDAVKKYLP 117
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
416-516 1.08e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 39.33  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 416 LVGNAIK--FT---ENGNIDILVEKRalsNTKVQIEVQirDTGIGIPErdqSRLFQAFRQADASISrrhgGTGLGLV-IT 489
Cdd:cd16957    9 LVENAIRhaFPkrkENNEVRVVVKKD---QHKVHVSVS--DNGQGIPE---ERLDLLGKTTVTSEK----GTGTALEnLN 76
                         90       100
                 ....*....|....*....|....*....
gi 446108595 490 QKLVNEMGGDISFH--SQPNRGSTFWFHI 516
Cdd:cd16957   77 RRLIGLFGSEACLHieSEVHGGTEVWFVI 105
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
670-771 1.33e-03

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: 39.19  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 670 VMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQlphQQQTPVIAVTA 749
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFISS 77
                         90       100
                 ....*....|....*....|..
gi 446108595 750 HAMAGQKEKLLGAGMSDYLAKP 771
Cdd:cd18159   78 RDDNMDQVMAINMGGDDYITKP 99
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
408-518 1.47e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 39.51  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 408 RLQQIITNLVGNAIK----FTENGNIDILVEkraLSNTKVQIEVqiRDTGIGIPERDqsrlfqafrqADASISRRHGGtG 483
Cdd:COG2172   34 DLVLAVSEAVTNAVRhaygGDPDGPVEVELE---LDPDGLEIEV--RDEGPGFDPED----------LPDPYSTLAEG-G 97
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446108595 484 LGLVITQKLVNEMGgdisFHSQPNrGSTFWFHINL 518
Cdd:COG2172   98 RGLFLIRRLMDEVE----YESDPG-GTTVRLVKRL 127
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
707-773 1.83e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 41.78  E-value: 1.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446108595 707 AKQMPfDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIE 773
Cdd:PRK10923  44 ASKTP-DVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFD 107
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
411-511 4.06e-03

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 40.99  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 411 QIITNLVGNAIKFTENGNIDIlvekRALSNTKVQIEVQIRDTGIGIP---ERDQsrlfqafrqadasisrrHggtgLGLV 487
Cdd:PRK10935 474 QIIREATLNAIKHANASEIAV----SCVTNPDGEHTVSIRDDGIGIGelkEPEG-----------------H----YGLN 528
                         90       100
                 ....*....|....*....|....
gi 446108595 488 ITQKLVNEMGGDISFHSQPNRGST 511
Cdd:PRK10935 529 IMQERAERLGGTLTISQPPGGGTT 552
PRK14084 PRK14084
DNA-binding response regulator;
668-777 5.85e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 39.35  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 668 MTVMAVDDNPANLKLIGALLE--DMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQtpVI 745
Cdd:PRK14084   1 MKALIVDDEPLARNELTYLLNeiGGFEEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPA--II 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446108595 746 AVTAHAMAGQKEKLLGAgmSDYLAKPIEEERL 777
Cdd:PRK14084  79 FATAHDQFAVKAFELNA--TDYILKPFEQKRI 108
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
147-198 6.49e-03

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 39.74  E-value: 6.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446108595 147 SSDAKNSQNMLGyialeldlksVRLQQykeIFISSVMMLFCIGIALIFGWRL 198
Cdd:cd18578  118 STDASDVRGLVG----------DRLGL---ILQAIVTLVAGLIIAFVYGWKL 156
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
669-750 7.38e-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: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 669 TVMAVDDNPanlkLIGALLEDMVQhvelcDSGHQ----------AVERAKQMPFDLILMDIQMPD-MDGIRACELIhQLP 737
Cdd:cd17540    2 RVLIIEDEP----LIAMDLEQIVE-----DLGHQvvgiartrdeAVALARRERPDLILADIQLADgSSGIDAVNEI-LTT 71
                         90
                 ....*....|...
gi 446108595 738 HqqQTPVIAVTAH 750
Cdd:cd17540   72 H--DVPVIFVTAY 82
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
712-773 8.60e-03

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 37.02  E-value: 8.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446108595 712 FDLILMDIQMPDMDGIRACELIHQlpHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIE 773
Cdd:cd17573   43 YDLVLVSDKLPDGNGLSIVSRIKE--KHPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFD 102
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
404-511 9.06e-03

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


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 36.96  E-value: 9.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446108595 404 GDPLRLQQIITNLVGNAIKFTENGniDILVEKRAlSNTKVQIEVQIRDTGIGIPERDQSRLFQaFRQAdasisrrhGGTG 483
Cdd:cd16934   21 VRQAEIATAVTELARNLLKHAGGG--QVLLEVVA-EGGRVALEILAVDQGPGIADVDEALRDG-FSTG--------GGLG 88
                         90       100
                 ....*....|....*....|....*...
gi 446108595 484 LGLVITQKLVNEMggdiSFHSQPNRGST 511
Cdd:cd16934   89 LGLGGVRRLADEF----DLHSAPGRGTV 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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