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Conserved domains on  [gi|742417147|ref|WP_038896261|]
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MULTISPECIES: TMAO reductase system sensor histidine kinase/response regulator TorS [Vibrio]

Protein Classification

ATP-binding protein( domain architecture ID 1002581)

ATP-binding protein similar to the ATPase domains of hybrid sensor kinases that regulate diverse biological functions through distinct molecular mechanisms

CATH:  3.30.565.10
EC:  2.7.13.3
Gene Ontology:  GO:0000155|GO:0005524
PubMed:  10966457
SCOP:  4001957

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
TMAO_torS super family cl37193
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
7-984 0e+00

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]


The actual alignment was detected with superfamily member TIGR02956:

Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 1005.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147    7 SIGRKLLLSFIAMAMLVMISALIGVSGFSLVAKTERNVVDSAIPAMLEARQVSELSTRIISSVQMLSNAQNEQERKEAGR 86
Cdd:TIGR02956   1 SIGRKLLLAFSVMAALLLLSVVIGVLGLSLVAKTERTVTQSALPAMIEARQLSELSNQIIFSVQLLSNVDDERQRQAIGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   87 VLFEQLESLLTHIKELGSESFDSKLLEALENNVQNVIDNLAELGVTVERKLWLTKEIDTRVEEMRLLSEELEQLTRTQVQ 166
Cdd:TIGR02956  81 KLTLQSETLLHSLKALGELPFNEDLLARLEVLVKDIIDTLAQLGLSVGERITLQAQLQQLSRELSEAAQEISELSQSQVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  167 NTSTIAVANVTHIYDLLDANKKAQAFQALDALVEVDLDLTERLHELHLLAFKMLNQIEEARTLTNVDRIQQIQTAFEDNL 246
Cdd:TIGR02956 161 NASTIALANVSGIYDLIESGKNDQVYQALDDLIEVDLDLAERLNELRLLALRVLNTIDDTKTSQDLAHINQLDEEFNRLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  247 KIMKRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQLMQKTLELFSELNGTVNKLVDDSNKTTRIAVE 326
Cdd:TIGR02956 241 MILSRRVQSIEDPTRSNQLKDLLVTLNKTPKLFKLLRQLSQILQKQQRLQQANLEQFTQLNTTVSQLVNAQNQRTEAAVS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  327 KLTSTLKFAQWSLTVISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAIITARNT 406
Cdd:TIGR02956 321 DLLMTLSVAQFGLLITGMLGLVILVFIMWRVVYRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIEAFRDT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  407 AQALKVVAEGEAQAKRELEEHKEHLEELIEQRTSQLKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMN 486
Cdd:TIGR02956 401 AAHNLKLQADERQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  487 GVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLL 566
Cdd:TIGR02956 481 GILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQ 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  567 FSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLNPedETQVLFEVSDTGIGIAKKDQKTLFDAFTQA 646
Cdd:TIGR02956 561 LRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLND--DSSLLFEVEDTGCGIAEEEQATLFDAFTQA 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  647 EgGMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESEPVETVSIASARCKIRAKVLVVEDNPVNRVV 726
Cdd:TIGR02956 639 D-GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMV 717
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  727 AEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIErnkpsdKALNPTPMVAVSAHVFAEE 806
Cdd:TIGR02956 718 AQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIY------GAKNEVKFIAFSAHVFNED 791
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  807 VESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQSGECLAQdEIITTSDNDTVSVTTDLTAEEPAMVIINPNVIQ 886
Cdd:TIGR02956 792 VAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEAPVLSASP-SFDSASVIENAQADDIPESNQASEFLLDEEQLQ 870
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  887 SDMKILGKEKMLHIIDLFRQTSADVLSQMESSAQNGESRAVKDLAHKLKGSAGSLGLTALMNTCQSIEIASESLEAYTML 966
Cdd:TIGR02956 871 QDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALELSD 950
                         970
                  ....*....|....*...
gi 742417147  967 RADLKGQVSDSVIALDEL 984
Cdd:TIGR02956 951 IDEIKQAWQASKTALDQW 968
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
7-984 0e+00

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: 1005.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147    7 SIGRKLLLSFIAMAMLVMISALIGVSGFSLVAKTERNVVDSAIPAMLEARQVSELSTRIISSVQMLSNAQNEQERKEAGR 86
Cdd:TIGR02956   1 SIGRKLLLAFSVMAALLLLSVVIGVLGLSLVAKTERTVTQSALPAMIEARQLSELSNQIIFSVQLLSNVDDERQRQAIGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   87 VLFEQLESLLTHIKELGSESFDSKLLEALENNVQNVIDNLAELGVTVERKLWLTKEIDTRVEEMRLLSEELEQLTRTQVQ 166
Cdd:TIGR02956  81 KLTLQSETLLHSLKALGELPFNEDLLARLEVLVKDIIDTLAQLGLSVGERITLQAQLQQLSRELSEAAQEISELSQSQVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  167 NTSTIAVANVTHIYDLLDANKKAQAFQALDALVEVDLDLTERLHELHLLAFKMLNQIEEARTLTNVDRIQQIQTAFEDNL 246
Cdd:TIGR02956 161 NASTIALANVSGIYDLIESGKNDQVYQALDDLIEVDLDLAERLNELRLLALRVLNTIDDTKTSQDLAHINQLDEEFNRLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  247 KIMKRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQLMQKTLELFSELNGTVNKLVDDSNKTTRIAVE 326
Cdd:TIGR02956 241 MILSRRVQSIEDPTRSNQLKDLLVTLNKTPKLFKLLRQLSQILQKQQRLQQANLEQFTQLNTTVSQLVNAQNQRTEAAVS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  327 KLTSTLKFAQWSLTVISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAIITARNT 406
Cdd:TIGR02956 321 DLLMTLSVAQFGLLITGMLGLVILVFIMWRVVYRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIEAFRDT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  407 AQALKVVAEGEAQAKRELEEHKEHLEELIEQRTSQLKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMN 486
Cdd:TIGR02956 401 AAHNLKLQADERQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  487 GVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLL 566
Cdd:TIGR02956 481 GILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQ 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  567 FSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLNPedETQVLFEVSDTGIGIAKKDQKTLFDAFTQA 646
Cdd:TIGR02956 561 LRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLND--DSSLLFEVEDTGCGIAEEEQATLFDAFTQA 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  647 EgGMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESEPVETVSIASARCKIRAKVLVVEDNPVNRVV 726
Cdd:TIGR02956 639 D-GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMV 717
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  727 AEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIErnkpsdKALNPTPMVAVSAHVFAEE 806
Cdd:TIGR02956 718 AQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIY------GAKNEVKFIAFSAHVFNED 791
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  807 VESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQSGECLAQdEIITTSDNDTVSVTTDLTAEEPAMVIINPNVIQ 886
Cdd:TIGR02956 792 VAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEAPVLSASP-SFDSASVIENAQADDIPESNQASEFLLDEEQLQ 870
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  887 SDMKILGKEKMLHIIDLFRQTSADVLSQMESSAQNGESRAVKDLAHKLKGSAGSLGLTALMNTCQSIEIASESLEAYTML 966
Cdd:TIGR02956 871 QDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALELSD 950
                         970
                  ....*....|....*...
gi 742417147  967 RADLKGQVSDSVIALDEL 984
Cdd:TIGR02956 951 IDEIKQAWQASKTALDQW 968
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
5-986 6.01e-142

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 447.04  E-value: 6.01e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   5 TASIGRKLLLSFIAMAMLVMISALIGVSGFSLVAKTERNVVDSAIPAMLEARQVSELSTRIISSVQMLSNAQNEQERKEA 84
Cdd:PRK11466   2 NLTLTRRLWMGFALMALLTLTSTLVGWYNLRFISQVEKDNTQALIPTMNMARQLSEASAWELFAAQNLTSADNEKMWQAQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  85 GRVLFEQLESLLTHIKELGSESFDsklLEALENNVQNVIDNLAELGVTVERKLWLTKEIDTRVEEMRLLSEELEQLTRTQ 164
Cdd:PRK11466  82 GRMLTAQSLKINALLQALREQGFD---TTAIEQQEQEISRSLRQQGELVGQRLQLRQQQQQLSQQIVAAADEIARLAQGQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 165 VQNTSTIAVANVTHIYDLLDANKKAQAFQALDALVEVDLDLTERLHELHLLAFK---MLNQIEEARTLTNVDRIQQiqtA 241
Cdd:PRK11466 159 ANNAATSAGATQAGIYDLIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSALRvqqMVMNLGLEQIQKNAPTLEK---Q 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 242 FEDNLKIMKRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQLMQKTLELFSELNGTVNKLVDDSNKTT 321
Cdd:PRK11466 236 LNNAVKILQRRQIRIEDPGVRAQVATTLTTVSQYSDLLALYQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 322 RIAVEKLTSTLKFAQWSLTVISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVEL-EVKGKDELAHMGQAI 400
Cdd:PRK11466 316 QHGLAHLEKASARGQYSLLLLGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFpETAGVRELDTIGRLM 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 401 ITARNTAQALKvvaegeaqakreleehkehleELIEQRTSQLKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHE 480
Cdd:PRK11466 396 DAFRSNVHALN---------------------RHREQLAAQVKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHE 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 481 IRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAG--HLEIRSLGFDLHQMVEDTFQLMNG 558
Cdd:PRK11466 455 IRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSG 534
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 559 KAQEKKLLFSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLnpeDETQVLFEVSDTGIGIAKKDQKT 638
Cdd:PRK11466 535 RVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRT---DGEQWLVEVEDSGCGIDPAKLAE 611
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 639 LFDAFTQAEGgmnQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESEPVETVSIASARCKIRAKVLVVE 718
Cdd:PRK11466 612 IFQPFVQVSG---KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAVRLDGLRLLLIE 688
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 719 DNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHD-FDIALVDINLPDCNGADLIHRLKRIernKPSDKalnptpMVA 797
Cdd:PRK11466 689 DNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEpFAAALVDFDLPDYDGITLARQLAQQ---YPSLV------LIG 759
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 798 VSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQlllpqsgeclaqdeiittsDNDTVsvttdltaeepam 877
Cdd:PRK11466 760 FSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQV-------------------NNDQP------------- 807
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 878 viINPNVIQSDMKILGKEKMLHIIDLFRQTSADVLSQMESSAQNGESRAVKDLAHKLKGSAGSLGLTALMNTCQSIEIAS 957
Cdd:PRK11466 808 --LDVSQLNEDAALMGTEKIHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQACAQLEQQP 885
                        970       980
                 ....*....|....*....|....*....
gi 742417147 958 ESleaytmlRADLKGQVSDSVIALDELMA 986
Cdd:PRK11466 886 LS-------APLPHEEITRSVAALEAWLA 907
TorS_sensor_domain cd16172
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide ...
55-315 3.38e-113

sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide (TMAO) reductase (Tor) pathway, which consists TorT, a periplasmic binding protein that binds TMAO; TorS, a sensor histidine kinase that forms a complex with TorT, and TorR, the response regulator. The Tor pathway is involved in regulating a cellular response to trimethylamine-N-oxide (TMAO), a terminal electron receptor in anaerobic respiration. TorS consists of a periplasmic sensor domain, as well as a HAMP domain, a histidine kinase domain, and a receiver domain.


Pssm-ID: 293930 [Multi-domain]  Cd Length: 261  Bit Score: 349.19  E-value: 3.38e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  55 ARQVSELSTRIISSVQMLSNAQNEQERKEAGRVLFEQLESLLTHIKELGSESFDSKLLEALENNVQNVIDNLAELGVTVE 134
Cdd:cd16172    1 ARQLSELSSRIIASAQLLANADSEAERQQQGRQLTAQLEALLRLLKALGQDSFDSFLLSRLEQTVQEIIDNLAQLGELVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 135 RKLWLTKEIDTRVEEMRLLSEELEQLTRTQVQNTSTIAVANVTHIYDLLDANKKAQAFQALDALVEVDLDLTERLHELHL 214
Cdd:cd16172   81 QRLQLRQQFQQLFERLRAAAGELAQLARTQVANASTIAVANVSGLYDLIEQNDKEAAYQALDRLIEVDLDLLERMHELRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 215 LAFKMLNQIEEARTLTNVDRIQQIQTAFEDNLKIMKRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQ 294
Cdd:cd16172  161 LALQLGNLINELRTASDIARLAELRQQFNANLAILQRRVQAVEDPGRRAQMAQLLSDLEQGQGLFALRRQLLALEQRLQA 240
                        250       260
                 ....*....|....*....|.
gi 742417147 295 LMQKTLELFSELNGTVNKLVD 315
Cdd:cd16172  241 LMQNNLVLFTQLNQTVNALVD 261
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
362-693 7.38e-73

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 244.05  E-value: 7.38e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 362 VIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAIITARNTAQALKVVAEGEAQAKRELEEHKEHLEELIEQRTSQ 441
Cdd:COG0642    2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 442 LKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSgLNPIQKRYAEIINRSGKTLLAI 521
Cdd:COG0642   82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 522 LNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVgRYWKGDVIRINQVLNNLVGNAIKFT 601
Cdd:COG0642  161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDL-PTVRGDPDRLRQVLLNLLSNAIKYT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 602 EQGEiDIYVSLNPEDEtQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMnQTGGTGLGLAISRRIIQAMGGCLEVDSDEG 681
Cdd:COG0642  240 PEGG-TVTVSVRREGD-RVRISVEDTGPGIPPEDLERIFEPFFRTDPSR-RGGGTGLGLAIVKRIVELHGGTIEVESEPG 316
                        330
                 ....*....|..
gi 742417147 682 HGSRFWFSIPLE 693
Cdd:COG0642  317 KGTTFTVTLPLA 328
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
581-693 8.93e-37

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 133.93  E-value: 8.93e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   581 GDVIRINQVLNNLVGNAIKFTEQGeIDIYVSLNPEDEtQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQTGGTGLGL 660
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVTLERDGD-HVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGTGLGL 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 742417147   661 AISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLE 693
Cdd:smart00387  79 SIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
581-694 2.47e-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: 118.62  E-value: 2.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  581 GDVIRINQVLNNLVGNAIKFTEQGEiDIYVSLNPEDEtqVLFEVSDTGIGIAKKDQKTLFDAFTQAEggMNQTGGTGLGL 660
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGGE--LTLTVEDNGIGIPPEDLPRIFEPFSTAD--KRGGGGTGLGL 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 742417147  661 AISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEE 694
Cdd:pfam02518  76 SIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
377-700 6.77e-24

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 106.65  E-value: 6.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 377 AQGNLAVELEVKGKDELAHMGQAIitarntaqalkvvaegeaqakreleehkehleeliEQRTSQLKQANRRLneevlnh 456
Cdd:NF040691 227 AAGDLSERMPVKGEDDLARLARSF-----------------------------------NQMADSLQRQIRQL------- 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 457 akarkqaEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDS--GLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAG 534
Cdd:NF040691 265 -------EELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAG 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 535 HLEIRSLGFDL----HQMVEDTFQLMNGKAQEKKL-LFSYHIESDVgrywkgDVIRINQVLNNLVGNAIKFTEQGEIDIY 609
Cdd:NF040691 338 AAELDVEPVDLrplvRRVVDALRQLAERAGVELRVdAPGTPVVAEV------DPRRVERVLRNLVVNAIEHGEGKPVVVT 411
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 610 VSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQT-GGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWF 688
Cdd:NF040691 412 VA---QDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTtGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRL 488
                        330
                 ....*....|..
gi 742417147 689 SIPLEESEPVET 700
Cdd:NF040691 489 TLPRVAGDRLTT 500
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
454-677 5.13e-19

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 91.04  E-value: 5.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 454 LNH-AKARKQAEQASRAksaFLATMSHEIRTPMnGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIE 532
Cdd:NF012163 226 FNQlASTLEKNEQMRRD---FMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSD 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 533 AGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYwkGDVIRINQVLNNLVGNAIKFTEQ-GEIDIYVS 611
Cdd:NF012163 302 EGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSSLVF--GDRDRLMQLFNNLLENSLRYTDSgGSLHISAS 379
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742417147 612 LNPEdetQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQ-TGGTGLGLAISRRIIQAMGGCLEVD 677
Cdd:NF012163 380 QRPK---EVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRaSGGSGLGLAISLNIVQAHGGTLHAA 443
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
7-984 0e+00

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: 1005.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147    7 SIGRKLLLSFIAMAMLVMISALIGVSGFSLVAKTERNVVDSAIPAMLEARQVSELSTRIISSVQMLSNAQNEQERKEAGR 86
Cdd:TIGR02956   1 SIGRKLLLAFSVMAALLLLSVVIGVLGLSLVAKTERTVTQSALPAMIEARQLSELSNQIIFSVQLLSNVDDERQRQAIGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   87 VLFEQLESLLTHIKELGSESFDSKLLEALENNVQNVIDNLAELGVTVERKLWLTKEIDTRVEEMRLLSEELEQLTRTQVQ 166
Cdd:TIGR02956  81 KLTLQSETLLHSLKALGELPFNEDLLARLEVLVKDIIDTLAQLGLSVGERITLQAQLQQLSRELSEAAQEISELSQSQVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  167 NTSTIAVANVTHIYDLLDANKKAQAFQALDALVEVDLDLTERLHELHLLAFKMLNQIEEARTLTNVDRIQQIQTAFEDNL 246
Cdd:TIGR02956 161 NASTIALANVSGIYDLIESGKNDQVYQALDDLIEVDLDLAERLNELRLLALRVLNTIDDTKTSQDLAHINQLDEEFNRLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  247 KIMKRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQLMQKTLELFSELNGTVNKLVDDSNKTTRIAVE 326
Cdd:TIGR02956 241 MILSRRVQSIEDPTRSNQLKDLLVTLNKTPKLFKLLRQLSQILQKQQRLQQANLEQFTQLNTTVSQLVNAQNQRTEAAVS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  327 KLTSTLKFAQWSLTVISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAIITARNT 406
Cdd:TIGR02956 321 DLLMTLSVAQFGLLITGMLGLVILVFIMWRVVYRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIEAFRDT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  407 AQALKVVAEGEAQAKRELEEHKEHLEELIEQRTSQLKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMN 486
Cdd:TIGR02956 401 AAHNLKLQADERQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  487 GVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLL 566
Cdd:TIGR02956 481 GILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQ 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  567 FSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLNPedETQVLFEVSDTGIGIAKKDQKTLFDAFTQA 646
Cdd:TIGR02956 561 LRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLND--DSSLLFEVEDTGCGIAEEEQATLFDAFTQA 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  647 EgGMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESEPVETVSIASARCKIRAKVLVVEDNPVNRVV 726
Cdd:TIGR02956 639 D-GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMV 717
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  727 AEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIErnkpsdKALNPTPMVAVSAHVFAEE 806
Cdd:TIGR02956 718 AQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIY------GAKNEVKFIAFSAHVFNED 791
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  807 VESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQSGECLAQdEIITTSDNDTVSVTTDLTAEEPAMVIINPNVIQ 886
Cdd:TIGR02956 792 VAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEAPVLSASP-SFDSASVIENAQADDIPESNQASEFLLDEEQLQ 870
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  887 SDMKILGKEKMLHIIDLFRQTSADVLSQMESSAQNGESRAVKDLAHKLKGSAGSLGLTALMNTCQSIEIASESLEAYTML 966
Cdd:TIGR02956 871 QDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALELSD 950
                         970
                  ....*....|....*...
gi 742417147  967 RADLKGQVSDSVIALDEL 984
Cdd:TIGR02956 951 IDEIKQAWQASKTALDQW 968
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
5-986 6.01e-142

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 447.04  E-value: 6.01e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   5 TASIGRKLLLSFIAMAMLVMISALIGVSGFSLVAKTERNVVDSAIPAMLEARQVSELSTRIISSVQMLSNAQNEQERKEA 84
Cdd:PRK11466   2 NLTLTRRLWMGFALMALLTLTSTLVGWYNLRFISQVEKDNTQALIPTMNMARQLSEASAWELFAAQNLTSADNEKMWQAQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  85 GRVLFEQLESLLTHIKELGSESFDsklLEALENNVQNVIDNLAELGVTVERKLWLTKEIDTRVEEMRLLSEELEQLTRTQ 164
Cdd:PRK11466  82 GRMLTAQSLKINALLQALREQGFD---TTAIEQQEQEISRSLRQQGELVGQRLQLRQQQQQLSQQIVAAADEIARLAQGQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 165 VQNTSTIAVANVTHIYDLLDANKKAQAFQALDALVEVDLDLTERLHELHLLAFK---MLNQIEEARTLTNVDRIQQiqtA 241
Cdd:PRK11466 159 ANNAATSAGATQAGIYDLIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSALRvqqMVMNLGLEQIQKNAPTLEK---Q 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 242 FEDNLKIMKRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQLMQKTLELFSELNGTVNKLVDDSNKTT 321
Cdd:PRK11466 236 LNNAVKILQRRQIRIEDPGVRAQVATTLTTVSQYSDLLALYQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 322 RIAVEKLTSTLKFAQWSLTVISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVEL-EVKGKDELAHMGQAI 400
Cdd:PRK11466 316 QHGLAHLEKASARGQYSLLLLGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFpETAGVRELDTIGRLM 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 401 ITARNTAQALKvvaegeaqakreleehkehleELIEQRTSQLKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHE 480
Cdd:PRK11466 396 DAFRSNVHALN---------------------RHREQLAAQVKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHE 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 481 IRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAG--HLEIRSLGFDLHQMVEDTFQLMNG 558
Cdd:PRK11466 455 IRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSG 534
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 559 KAQEKKLLFSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLnpeDETQVLFEVSDTGIGIAKKDQKT 638
Cdd:PRK11466 535 RVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRT---DGEQWLVEVEDSGCGIDPAKLAE 611
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 639 LFDAFTQAEGgmnQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESEPVETVSIASARCKIRAKVLVVE 718
Cdd:PRK11466 612 IFQPFVQVSG---KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAVRLDGLRLLLIE 688
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 719 DNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHD-FDIALVDINLPDCNGADLIHRLKRIernKPSDKalnptpMVA 797
Cdd:PRK11466 689 DNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEpFAAALVDFDLPDYDGITLARQLAQQ---YPSLV------LIG 759
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 798 VSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQlllpqsgeclaqdeiittsDNDTVsvttdltaeepam 877
Cdd:PRK11466 760 FSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQV-------------------NNDQP------------- 807
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 878 viINPNVIQSDMKILGKEKMLHIIDLFRQTSADVLSQMESSAQNGESRAVKDLAHKLKGSAGSLGLTALMNTCQSIEIAS 957
Cdd:PRK11466 808 --LDVSQLNEDAALMGTEKIHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQACAQLEQQP 885
                        970       980
                 ....*....|....*....|....*....
gi 742417147 958 ESleaytmlRADLKGQVSDSVIALDELMA 986
Cdd:PRK11466 886 LS-------APLPHEEITRSVAALEAWLA 907
TorS_sensor_domain cd16172
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide ...
55-315 3.38e-113

sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide (TMAO) reductase (Tor) pathway, which consists TorT, a periplasmic binding protein that binds TMAO; TorS, a sensor histidine kinase that forms a complex with TorT, and TorR, the response regulator. The Tor pathway is involved in regulating a cellular response to trimethylamine-N-oxide (TMAO), a terminal electron receptor in anaerobic respiration. TorS consists of a periplasmic sensor domain, as well as a HAMP domain, a histidine kinase domain, and a receiver domain.


Pssm-ID: 293930 [Multi-domain]  Cd Length: 261  Bit Score: 349.19  E-value: 3.38e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  55 ARQVSELSTRIISSVQMLSNAQNEQERKEAGRVLFEQLESLLTHIKELGSESFDSKLLEALENNVQNVIDNLAELGVTVE 134
Cdd:cd16172    1 ARQLSELSSRIIASAQLLANADSEAERQQQGRQLTAQLEALLRLLKALGQDSFDSFLLSRLEQTVQEIIDNLAQLGELVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 135 RKLWLTKEIDTRVEEMRLLSEELEQLTRTQVQNTSTIAVANVTHIYDLLDANKKAQAFQALDALVEVDLDLTERLHELHL 214
Cdd:cd16172   81 QRLQLRQQFQQLFERLRAAAGELAQLARTQVANASTIAVANVSGLYDLIEQNDKEAAYQALDRLIEVDLDLLERMHELRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 215 LAFKMLNQIEEARTLTNVDRIQQIQTAFEDNLKIMKRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQ 294
Cdd:cd16172  161 LALQLGNLINELRTASDIARLAELRQQFNANLAILQRRVQAVEDPGRRAQMAQLLSDLEQGQGLFALRRQLLALEQRLQA 240
                        250       260
                 ....*....|....*....|.
gi 742417147 295 LMQKTLELFSELNGTVNKLVD 315
Cdd:cd16172  241 LMQNNLVLFTQLNQTVNALVD 261
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
459-954 8.34e-92

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 312.55  E-value: 8.34e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 459 ARKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEI 538
Cdd:PRK11107 282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVL 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 539 RSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLNPEDET 618
Cdd:PRK11107 362 ENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNT 441
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 619 QVL--FEVSDTGIGIAKKDQKTLFDAFTQAEGGMN-QTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEES 695
Cdd:PRK11107 442 KVQleVQIRDTGIGISERQQSQLFQAFRQADASISrRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLN 521
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 696 ---------------------EP---------------------------------------------------VETVSI 703
Cdd:PRK11107 522 pnpiidglptdclagkrllyvEPnsaaaqatldilsetplevtysptlsqlpeahydilllglpvtfrepltmlHERLAK 601
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 704 ASARC----------------------------------------------------------KIRAKVLVVEDNPVNRV 725
Cdd:PRK11107 602 AKSMTdflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesRLPLTVMAVDDNPANLK 681
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 726 VAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNG---ADLIHRLKrIERNkpsdkalnpTPMVAVSAHV 802
Cdd:PRK11107 682 LIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGiraCELIRQLP-HNQN---------TPIIAVTAHA 751
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 803 FAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGkqlllPQSGECLAQDEIITTSDNDTVSVTTDLTaeepamviinp 882
Cdd:PRK11107 752 MAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPG-----PKFTSRVVAPEPPEPVHFPNATLDWQLA----------- 815
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742417147 883 nVIQSDMKI-LGKE--KMLhiIDLFRQTSADVLSQMESSAQNGesraVKDLAHKLKGSAGSLGLTALMNTCQSIE 954
Cdd:PRK11107 816 -LRQAAGKPdLARDmlQML--LDFLPEVRNKVEEALAGEDPEG----LLDLIHKLHGSCSYSGVPRLKKLCQLIE 883
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
460-954 1.09e-86

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 295.31  E-value: 1.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 460 RKQA----EQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGH 535
Cdd:PRK11091 269 RKRYqdalEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRK 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 536 LEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLNPE 615
Cdd:PRK11091 349 LQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEG 428
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 616 DEtqVLFEVSDTGIGIAKKDQKTLFDAFTQAEG--GMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLE 693
Cdd:PRK11091 429 DM--LTFEVEDSGIGIPEDELDKIFAMYYQVKDshGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAP 506
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 694 ESEPVETVSIASARCKIRA-KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGAD 772
Cdd:PRK11091 507 AVAEEVEDAFDEDDMPLPAlNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLD 586
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 773 LIHRLKRIErnkPSDKAlnpTPMVAVSAHVFAEEVEsYLAAGFDGYLPKPMEKEALSALIQDMLDgkqlllPQSGECLAQ 852
Cdd:PRK11091 587 IARELRERY---PREDL---PPLVALTANVLKDKKE-YLDAGMDDVLSKPLSVPALTAMIKKFWD------TQDDEESTV 653
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 853 DEIITTSDNDTvsvttdltaeepamvIINPNVIQSDMKILGKEKMLHIIDLFRQTSADVLSQMESSAQNGESRAVKDLAH 932
Cdd:PRK11091 654 TTEESSKANEA---------------LLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAH 718
                        490       500
                 ....*....|....*....|..
gi 742417147 933 KLKGSAGSLGLTALMNTCQSIE 954
Cdd:PRK11091 719 KIKGAAGSVGLRHLQQLAQQIQ 740
PRK15347 PRK15347
two component system sensor kinase;
448-967 2.37e-78

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 274.98  E-value: 2.37e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 448 RLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLD 527
Cdd:PRK15347 376 KVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLD 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 528 YSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEID 607
Cdd:PRK15347 456 FSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIR 535
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 608 IYVSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMnqtGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFW 687
Cdd:PRK15347 536 LRVK---RHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS---QGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFS 609
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 688 FSIPLEESEPVETVS---IA-------------------------------------------------SARCKI----- 710
Cdd:PRK15347 610 LVLPLNEYAPPEPLKgelSAplalhrqlsawgitcqpghqnpalldpelaylpgrlydllqqiiqgapnEPVINLplqpw 689
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNKPSDkal 790
Cdd:PRK15347 690 QLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPD--- 766
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 791 npTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIqDMLDGKQL-----LLPQSGEClaqDEIITTSDNDtvs 865
Cdd:PRK15347 767 --CMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL-ELAAEYQLlrgieLSPQDSSC---SPLLDTDDMA--- 837
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 866 vttdltaeepamviinpnviqsdmkilgkekmlhIIDLFRQTSADVLSQMESSAQNGEsrAVKDLAHKLKGSAGSLGLTA 945
Cdd:PRK15347 838 ----------------------------------LNSKLYQSLLLLLAQIEQAVENQE--VLSQLLHTLKGCAGQAGLTE 881
                        570       580
                 ....*....|....*....|....*..
gi 742417147 946 LMNTCQSIEIASE-----SLEAYTMLR 967
Cdd:PRK15347 882 LQCAVIDLENALEtgeilSLEELTDLR 908
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
362-693 7.38e-73

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 244.05  E-value: 7.38e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 362 VIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAIITARNTAQALKVVAEGEAQAKRELEEHKEHLEELIEQRTSQ 441
Cdd:COG0642    2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 442 LKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSgLNPIQKRYAEIINRSGKTLLAI 521
Cdd:COG0642   82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 522 LNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVgRYWKGDVIRINQVLNNLVGNAIKFT 601
Cdd:COG0642  161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDL-PTVRGDPDRLRQVLLNLLSNAIKYT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 602 EQGEiDIYVSLNPEDEtQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMnQTGGTGLGLAISRRIIQAMGGCLEVDSDEG 681
Cdd:COG0642  240 PEGG-TVTVSVRREGD-RVRISVEDTGPGIPPEDLERIFEPFFRTDPSR-RGGGTGLGLAIVKRIVELHGGTIEVESEPG 316
                        330
                 ....*....|..
gi 742417147 682 HGSRFWFSIPLE 693
Cdd:COG0642  317 KGTTFTVTLPLA 328
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
457-695 2.13e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 222.86  E-value: 2.13e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 457 AKARKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSG--LNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAG 534
Cdd:COG2205    3 EEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLESG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 535 HLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGrYWKGDVIRINQVLNNLVGNAIKFT-EQGEIDIYVSln 613
Cdd:COG2205   83 KLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSpPGGTITISAR-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 614 pEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGmNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLE 693
Cdd:COG2205  160 -REGDGVRISVSDNGPGIPEEELERIFERFYRGDNS-RGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLA 237

                 ..
gi 742417147 694 ES 695
Cdd:COG2205  238 ES 239
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
338-695 1.03e-61

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 215.19  E-value: 1.03e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 338 SLTVISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAIITARNTAQALKVVAEGE 417
Cdd:COG5002   33 LLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 418 AQAKRELEEHKEHLEELIEQRTSQLKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLID 497
Cdd:COG5002  113 LLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLD 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 498 S--GLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDV 575
Cdd:COG5002  193 GaaDDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDP 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 576 GRYWkGDVIRINQVLNNLVGNAIKFT-EQGEIDIYVSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMN-QT 653
Cdd:COG5002  273 LLVL-GDPDRLEQVLTNLLDNAIKYTpEGGTITVSLR---EEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSrET 348
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 742417147 654 GGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEES 695
Cdd:COG5002  349 GGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
463-828 1.95e-50

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 192.88  E-value: 1.95e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 463 AEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLG 542
Cdd:PRK10841 440 AEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPRE 519
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 543 FDLHQMVedTFQLMNGKAQ-EKKLLFSY-HIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLnpeDETQV 620
Cdd:PRK10841 520 FSPREVI--NHITANYLPLvVKKRLGLYcFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRV---DGDYL 594
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 621 LFEVSDTGIGIAKKDQKTLFDAFTQA-EGGMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPL------- 692
Cdd:PRK10841 595 SFRVRDTGVGIPAKEVVRLFDPFFQVgTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLygaqypq 674
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 693 ---------------------------------------EESEPVET---------VSIASARCKIR------------- 711
Cdd:PRK10841 675 kkgveglqgkrcwlavrnasleqfletllqrsgiqvqryEGQEPTPEdvlitddpvQKKWQGRAVITfcrrhigipleia 754
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 -----------------------------------------------AKVLVVEDNPVNRVVAEGFLESMGHEVILAENG 744
Cdd:PRK10841 755 pgewvhstatphelpallariyrielesddsanalpstdkavsdnddMMILVVDDHPINRRLLADQLGSLGYQCKTANDG 834
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 745 LEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkalnpTPMVAVSAHVFAEEVESYLAAGFDGYLPKPME 824
Cdd:PRK10841 835 VDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLT---------LPVIGVTANALAEEKQRCLEAGMDSCLSKPVT 905

                 ....
gi 742417147 825 KEAL 828
Cdd:PRK10841 906 LDVL 909
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
460-986 1.36e-48

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 188.40  E-value: 1.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  460 RKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYA-EIINRSGKTLLAILNDVLDYSKIEAGHLEI 538
Cdd:PRK09959  702 RNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAiSLAYATGQSLLGLIGEILDVDKIESGNYQL 781
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  539 RSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLNPEDET 618
Cdd:PRK09959  782 QPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDN 861
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  619 QVLFEVS--DTGIGIAKKDQKTLFDAFTQAEGGMNQTgGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESE 696
Cdd:PRK09959  862 HAVIKMTimDSGSGLSQEEQQQLFKRYSQTSAGRQQT-GSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQ 940
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  697 PVETVSiASARCKI----RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGAD 772
Cdd:PRK09959  941 QVATVE-AKAEQPItlpeKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFE 1019
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  773 LIHRLKriERNkpsdkalNPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQlLLPQSGEclaq 852
Cdd:PRK09959 1020 LTRKLR--EQN-------SSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAH-IAPQYRH---- 1085
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  853 deiittsdndtvsvtTDLTAEEpamviinpNVIQSDMKIlgkekMLHIIDLFRQTSADVLSQMESSAQNGESRAVKDLAH 932
Cdd:PRK09959 1086 ---------------LDIEALK--------NNTANDLQL-----MQEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIH 1137
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 742417147  933 KLKGSAGSLGLTALMNTCQSIEIASESLEAYTMLrADLKGQVSDSVIALDELMA 986
Cdd:PRK09959 1138 RIHGAANILNLQKLINISHQLEITPVSDDSKPEI-LQLLNSVKEHIAELDQEIA 1190
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
586-692 5.95e-46

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: 160.35  E-value: 5.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 586 INQVLNNLVGNAIKFTEQGEIDIYVSLNPEDET--QVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMN-QTGGTGLGLAI 662
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTrKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 742417147 663 SRRIIQAMGGCLEVDSDEGHGSRFWFSIPL 692
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
189-695 1.60e-45

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 171.89  E-value: 1.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 189 AQAFQALDALVEVDLDLTERLHELHLLAFKMLNQIEEARTLTNVDRIQQIQTAFEDNLKIMKRRVLAVEDPTRSEQMSQL 268
Cdd:COG4251   17 LLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLAL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 269 LTELGKRQVVFTILLQQYENNEQSQQLMQKTLELFSELNGTVNKLVDDSNKTTRIAVEKLTSTLKFAQWSLTVISIIGLI 348
Cdd:COG4251   97 LLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 349 IVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAIITARNTAQALKVVAEGEAQakRELEEHK 428
Cdd:COG4251  177 ELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLL--LILVLEL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 429 EHLEELIEQRTSQLKQANRRLneevlnhakarkqaEQASRAKSAFLATMSHEIRTPMNGVLGTARLLID---SGLNPIQK 505
Cdd:COG4251  255 LELRLELEELEEELEERTAEL--------------ERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 506 RYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSlgFDLHQMVEDTFQLMNGKAQEKKllfsYHIESDVGRYWKGDVIR 585
Cdd:COG4251  321 EYLERIRDAAERMQALIDDLLAYSRVGRQELEFEP--VDLNELLEEVLEDLEPRIEERG----AEIEVGPLPTVRGDPTL 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 586 INQVLNNLVGNAIKFT---EQGEIDIYVSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGmNQTGGTGLGLAI 662
Cdd:COG4251  395 LRQVFQNLISNAIKYSrpgEPPRIEIGAE---REGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSR-DEYEGTGIGLAI 470
                        490       500       510
                 ....*....|....*....|....*....|...
gi 742417147 663 SRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEES 695
Cdd:COG4251  471 VKKIVERHGGRIWVESEPGEGATFYFTLPKAPA 503
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
446-700 3.32e-44

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 167.46  E-value: 3.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 446 NRRLNEEVLNHAkarkqaEQASRAkSAFLATMSHEIRTPMNGVLGTARLLIDSgLNPIQKRYAEIINRSGKTLLAILNDV 525
Cdd:COG5809  253 ERKKLEELLRKS------EKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDT-IDEEQKTYLDIMLSELDRIESIISEF 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 526 LDYSKIEAGHLEIrslgFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGrYWKGDVIRINQVLNNLVGNAIKFT-EQG 604
Cdd:COG5809  325 LVLAKPQAIKYEP----KDLNTLIEEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQVFINLLKNAIEAMpEGG 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 605 EIdiYVSLNPEDETQVLFEVSDTGIGIAKKDQKTLFDAF-TQAEGGmnqtggTGLGLAISRRIIQAMGGCLEVDSDEGHG 683
Cdd:COG5809  400 NI--TIETKAEDDDKVVISVTDEGCGIPEERLKKLGEPFyTTKEKG------TGLGLMVSYKIIEEHGGKITVESEVGKG 471
                        250
                 ....*....|....*..
gi 742417147 684 SRFWFSIPLEESEPVET 700
Cdd:COG5809  472 TTFSITLPIKLSEQVSM 488
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
400-692 7.05e-38

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 145.71  E-value: 7.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 400 IITARNTAQALKVVAEGEAQAKRELEEHKEHLEELIEQRTSQLKQANRRLNEEVLNHAKARKQAEQASRaksafLATM-- 477
Cdd:COG4191   70 ALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEK-----LAALge 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 478 -----SHEIRTPMNGVLGTA----RLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIrslgFDLHQM 548
Cdd:COG4191  145 laagiAHEINNPLAAILGNAellrRRLEDEPDPEELREALERILEGAERAAEIVRSLRAFSRRDEEEREP----VDLNEL 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 549 VEDTFQLMNGKAQEKKLLFSYHIESDVGRyWKGDVIRINQVLNNLVGNAI---KFTEQGEIDIYVSlnpEDETQVLFEVS 625
Cdd:COG4191  221 IDEALELLRPRLKARGIEVELDLPPDLPP-VLGDPGQLEQVLLNLLINAIdamEEGEGGRITISTR---REGDYVVISVR 296
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742417147 626 DTGIGIAKKDQKTLFDAF--TQAEGGmnqtgGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPL 692
Cdd:COG4191  297 DNGPGIPPEVLERIFEPFftTKPVGK-----GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
581-693 8.93e-37

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 133.93  E-value: 8.93e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   581 GDVIRINQVLNNLVGNAIKFTEQGeIDIYVSLNPEDEtQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQTGGTGLGL 660
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVTLERDGD-HVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGTGLGL 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 742417147   661 AISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLE 693
Cdd:smart00387  79 SIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
2-678 1.54e-35

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 144.06  E-value: 1.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   2 LLATASIGRKLLLSFIAMAMLVMISALIGVSGFSLVAKTERNVVDSAIPAMLEARQVSELSTRIISSVQMLSNAQNEQER 81
Cdd:COG4192    4 LLKRLGIGARLLLAFALSALLTLVASLVALFSWNSLSNQIRYILDDSLPKLQASLKLEENSNELVAALPEFAAATNTTER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  82 KEAGRVLFEQLESLLTHIKELGSESFDSKLLEALENNVQNvidNLAELGVTVERKLWLTKEIDTRVEEMRLLSEELEQLT 161
Cdd:COG4192   84 SQLRNQLNTQLADIEELLAELEQLTQDAGDLRAAVADLRN---LLQQLDSLLTQRIALRRRLQELLEQINWLHQDFNSEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 162 RTQVQNTSTIAVANVTHIYDLLDANKKAQAFQALdalvevdLDLTERLHELhllaFKMLNQIEEARTLTNVD----RIQQ 237
Cdd:COG4192  161 TPLLQEASWQQTRLLDSVETTESLRNLQNELQLL-------LRLLAIENQI----VSLLREVAAARDQADVDnlfdRLQY 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 238 IQTAFEDNLKIMKRRVLAVEdptrSEQMSQLLTELGK-RQVVFTILLQQYENNEQSQQLMQKTLELFSELNGTVNKLVDD 316
Cdd:COG4192  230 LKDELDRNLQALKNYPSTIT----LRQLIDELLAIGSgEGGLPSLRRDELAAQATLEALAEENNSILEQLRTQISGLVGN 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 317 SNKTTRIAVEKLTSTLKFAQWSLTVISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHM 396
Cdd:COG4192  306 SREQLVALNQETAQLVQQSGILLLAIALLSLLLAVLINYFYVRRRLVKRLNALSDAMAAIAAGDLDVPIPVDGNDEIGRI 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 397 GQAIITARNTAQALKVVAEGEaqakreleehkehleelIEQRtsQLKQANRRLNEEVLNHAkarkqAEQASRAKSafLAT 476
Cdd:COG4192  386 ARLLRVFRDQAIEKTQELETE-----------------IEER--KRIEKNLRQTQDELIQA-----AKMAVVGQT--MTS 439
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 477 MSHEIRTP---MNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIrslgFDLHQMVEDTF 553
Cdd:COG4192  440 LAHELNQPlnaMSMYLFSAKKALEQENYAQLPTSLDKIEGLIERMDKIIKSLRQFSRKSDTPLQP----VDLRQVIEQAW 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 554 QLMNGKAqeKKLLFSYHIESDVgrYWKGDVIRINQVLNNLVGNAIK-FTEQGEIDIYVSLNPEDETqvlFEVSDTGIGIA 632
Cdd:COG4192  516 ELVESRA--KPQQITLHIPDDL--MVQGDQVLLEQVLVNLLVNALDaVATQPQISVDLLSNAENLR---VAISDNGNGWP 588
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*.
gi 742417147 633 KKDQktLFDAFTQaeggmNQTGGTGLGLAISRRIIQAMGGCLEVDS 678
Cdd:COG4192  589 LVDK--LFTPFTT-----TKEVGLGLGLSICRSIMQQFGGDLYLAS 627
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
711-840 2.25e-35

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: 130.74  E-value: 2.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNKpsdkal 790
Cdd:COG0784    5 GKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLP------ 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 742417147 791 nPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQ 840
Cdd:COG0784   79 -DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
714-832 1.07e-34

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: 128.36  E-value: 1.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNKPsdkalnPT 793
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGR------RT 74
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALI 832
Cdd:cd17546   75 PIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
475-697 6.55e-33

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: 132.78  E-value: 6.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 475 ATMSHEIRTPMNGVLGTARLL------IDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIrslgFDLHQM 548
Cdd:COG5000  206 RRIAHEIKNPLTPIQLSAERLrrkladKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEP----VDLNEL 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 549 VEDTFQLMNGKAQEKKLLFSYHIESDVgRYWKGDVIRINQVLNNLVGNAIKFTEQ-GEIDIYVSLnpeDETQVLFEVSDT 627
Cdd:COG5000  282 LREVLALYEPALKEKDIRLELDLDPDL-PEVLADRDQLEQVLINLLKNAIEAIEEgGEIEVSTRR---EDGRVRIEVSDN 357
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742417147 628 GIGIAKKDQKTLFDAF--TQAEGgmnqtggTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESEP 697
Cdd:COG5000  358 GPGIPEEVLERIFEPFftTKPKG-------TGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEAE 422
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
458-697 1.58e-32

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 129.97  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 458 KARKQAEQASRAKSA--FLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGH 535
Cdd:COG3852  121 RLERELRRAEKLAAVgeLAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 536 LEIrslgFDLHQMVEDTFQLMNGKAQeKKLLFSYHIESDVGRYWkGDVIRINQVLNNLVGNAIK-FTEQGEIDIYVSLNP 614
Cdd:COG3852  201 REP----VNLHEVLERVLELLRAEAP-KNIRIVRDYDPSLPEVL-GDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVER 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 615 EDET-------QVLFEVSDTGIGIAKKDQKTLFDAF--TQAEGgmnqtggTGLGLAISRRIIQAMGGCLEVDSDEGHGSR 685
Cdd:COG3852  275 QVTLgglrprlYVRIEVIDNGPGIPEEILDRIFEPFftTKEKG-------TGLGLAIVQKIVEQHGGTIEVESEPGKGTT 347
                        250
                 ....*....|..
gi 742417147 686 FWFSIPLEESEP 697
Cdd:COG3852  348 FRIYLPLEQAEE 359
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
462-690 5.00e-32

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: 127.71  E-value: 5.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  462 QAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGL--NPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIR 539
Cdd:TIGR02966 106 RLRRLEQMRRDFVANVSHELRTPLTVLRGYLETLADGPDedPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLE 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  540 SLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVgrYWKGDVIRINQVLNNLVGNAIKFT-EQGEIDIYVSlnpEDET 618
Cdd:TIGR02966 186 DEPVDMPALLDHLRDEAEALSQGKNHQITFEIDGGV--DVLGDEDELRSAFSNLVSNAIKYTpEGGTITVRWR---RDGG 260
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742417147  619 QVLFEVSDTGIGIAKKDQKTLFDAFTQAE-GGMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSI 690
Cdd:TIGR02966 261 GAEFSVTDTGIGIAPEHLPRLTERFYRVDkSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
581-694 2.47e-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: 118.62  E-value: 2.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  581 GDVIRINQVLNNLVGNAIKFTEQGEiDIYVSLNPEDEtqVLFEVSDTGIGIAKKDQKTLFDAFTQAEggMNQTGGTGLGL 660
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGGE--LTLTVEDNGIGIPPEDLPRIFEPFSTAD--KRGGGGTGLGL 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 742417147  661 AISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEE 694
Cdd:pfam02518  76 SIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
711-832 2.45e-26

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: 106.53  E-value: 2.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERnkpsdkaL 790
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPR-------T 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742417147 791 NPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALI 832
Cdd:COG3706   74 ADIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
711-874 2.57e-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: 107.35  E-value: 2.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkal 790
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSD------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 791 npTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQSGECLAQDEIITTSDNDTVsvttDL 870
Cdd:COG0745   74 --IPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDLLDLAAREVTRDGEPV----EL 147

                 ....
gi 742417147 871 TAEE 874
Cdd:COG0745  148 TPKE 151
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
449-692 4.72e-25

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: 108.80  E-value: 4.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 449 LNEEVLNHAKARKQAEQASRAK--SAFLATMSHEIRTPMNGVLGTARLLI-DSGLNPIQKRYAEI----INRSGktllAI 521
Cdd:COG5806  178 LIENLIENILLRKELQRAEKLEvvSELAASIAHEVRNPLTVVRGFIQLLQePELSDEKRKQYIRIaleeLDRAE----AI 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 522 LNDVLDYSKIEAGHLEIRSLGFDLHQMVE--DTFQLMNGKAQEKKLLFSYHIEsdvgrywkGDVIRINQVLNNLVGNAIK 599
Cdd:COG5806  254 ITDYLTFAKPQPEKLEKIDVSEELEHVIDvlSPYANMNNVEIQTELEPGLYIE--------GDRQKLQQCLINIIKNGIE 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 600 FTEQ-GEIDIYVSlnpEDETQVLFEVSDTGIGIAKKDQK---TLFdaFTqaeggmNQTGGTGLGLAISRRIIQAMGGCLE 675
Cdd:COG5806  326 AMPNgGTLTIDVS---IDKNKVIISIKDTGVGMTKEQLErlgEPY--FS------TKEKGTGLGTMVSYRIIEAMNGTIR 394
                        250
                 ....*....|....*..
gi 742417147 676 VDSDEGHGSRFWFSIPL 692
Cdd:COG5806  395 VESEVGKGTTFTITLPL 411
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
711-859 4.96e-25

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: 108.90  E-value: 4.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkal 790
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPD------- 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742417147 791 npTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLpqsgECLAQDEIITTS 859
Cdd:COG2204   75 --LPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRR----ENAEDSGLIGRS 137
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
711-841 8.28e-25

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: 103.71  E-value: 8.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNKpsdkal 790
Cdd:COG3437    6 APTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTR------ 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 742417147 791 nPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQL 841
Cdd:COG3437   80 -DIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRL 129
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
713-824 5.40e-24

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: 97.61  E-value: 5.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALNP 792
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLK-------EDPATRD 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 742417147 793 TPMVAVSAHVFAEEVESYLAAGFDGYLPKPME 824
Cdd:cd17548   74 IPVIALTAYAMKGDREKILEAGCDGYISKPID 105
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
377-700 6.77e-24

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 106.65  E-value: 6.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 377 AQGNLAVELEVKGKDELAHMGQAIitarntaqalkvvaegeaqakreleehkehleeliEQRTSQLKQANRRLneevlnh 456
Cdd:NF040691 227 AAGDLSERMPVKGEDDLARLARSF-----------------------------------NQMADSLQRQIRQL------- 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 457 akarkqaEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDS--GLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAG 534
Cdd:NF040691 265 -------EELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAG 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 535 HLEIRSLGFDL----HQMVEDTFQLMNGKAQEKKL-LFSYHIESDVgrywkgDVIRINQVLNNLVGNAIKFTEQGEIDIY 609
Cdd:NF040691 338 AAELDVEPVDLrplvRRVVDALRQLAERAGVELRVdAPGTPVVAEV------DPRRVERVLRNLVVNAIEHGEGKPVVVT 411
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 610 VSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQT-GGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWF 688
Cdd:NF040691 412 VA---QDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTtGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRL 488
                        330
                 ....*....|..
gi 742417147 689 SIPLEESEPVET 700
Cdd:NF040691 489 TLPRVAGDRLTT 500
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
456-696 9.93e-24

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 106.98  E-value: 9.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 456 HAKARKQAEQASR--AKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEa 533
Cdd:PRK11360 374 RKRLQRRVARQERlaALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPR- 452
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 534 ghlEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYWkGDVIRINQVLNNLVGNAIK-FTEQGEIDIYVSL 612
Cdd:PRK11360 453 ---ESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIW-ADPELLKQVLLNILINAVQaISARGKIRIRTWQ 528
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 613 NPEDetQVLFEVSDTGIGIAKKDQKTLFDAF--TQAEGgmnqtggTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSI 690
Cdd:PRK11360 529 YSDG--QVAVSIEDNGCGIDPELLKKIFDPFftTKAKG-------TGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYL 599

                 ....*.
gi 742417147 691 PLEESE 696
Cdd:PRK11360 600 PINPQG 605
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
715-822 1.78e-23

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 95.76  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 715 LVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkalnpTP 794
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD---------IP 71
                         90       100
                 ....*....|....*....|....*...
gi 742417147 795 MVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:cd00156   72 VIVLTAKADEEDAVRALELGADDYLVKP 99
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
714-832 2.52e-22

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: 92.91  E-value: 2.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNKpsdkalnPT 793
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLA-------NT 73
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALI 832
Cdd:cd17580   74 PAIALTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
454-691 8.45e-22

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: 99.77  E-value: 8.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  454 LNHAKARkqAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNpiQKRYAEIINRSG---KTLLAILNDVLDYSK 530
Cdd:TIGR01386 227 FNAMLGR--LEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQPRT--GEEYREVLESNLeelERLSRMVSDMLFLAR 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  531 IEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVgrywKGDVIRINQVLNNLVGNAIKFTEQG-EIDIY 609
Cdd:TIGR01386 303 ADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLV----RGDPQMFRRAISNLLSNALRHTPDGgTITVR 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  610 VSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGG-MNQTGGTGLGLAISRRIIQAMGGCLEVDSDeGHGSRFWF 688
Cdd:TIGR01386 379 IE---RRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPArSNSGEGTGLGLAIVRSIMEAHGGRASAESP-DGKTRFIL 454

                  ...
gi 742417147  689 SIP 691
Cdd:TIGR01386 455 RFP 457
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
714-833 9.31e-22

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: 91.06  E-value: 9.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIERNKPSdkalnpT 793
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLEL---LKRIRRRDPT------T 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 742417147  794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:pfam00072  72 PVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-692 1.96e-21

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 90.17  E-value: 1.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 586 INQVLNNLVGNAIK-FTEQGEIDIYVSLnpeDETQVLFEVSDTGIGIAKKDQKTLFDAF--TQAEGGmnqtgGTGLGLAI 662
Cdd:cd16943    4 LNQVLLNLLVNAAQaMEGRGRITIRTWA---HVDQVLIEVEDTGSGIDPEILGRIFDPFftTKPVGE-----GTGLGLSL 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 742417147 663 SRRIIQAMGGCLEVDSDEGHGSRFWFSIPL 692
Cdd:cd16943   76 SYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-691 2.00e-21

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 90.08  E-value: 2.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 586 INQVLNNLVGNAIKFTEQG---EIDIYVSLNPEDETqvlFEVSDTGIGIAKKDQKTLFDAFtQAEGGMNQTGGTGLGLAI 662
Cdd:cd16921    1 LGQVLTNLLGNAIKFRRPRrppRIEVGAEDVGEEWT---FYVRDNGIGIDPEYAEKVFGIF-QRLHSREEYEGTGVGLAI 76
                         90       100
                 ....*....|....*....|....*....
gi 742417147 663 SRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16921   77 VRKIIERHGGRIWLESEPGEGTTFYFTLP 105
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
713-842 2.00e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 88.49  E-value: 2.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESM-GHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkal 790
Cdd:COG4565    5 RVLIVEDDPMVAELLRRYLERLpGFEVVGvASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPD------- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742417147 791 npTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLL 842
Cdd:COG4565   78 --VDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLL 127
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
448-836 2.42e-20

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 97.06  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 448 RLNEEVLNHA--KARKQAE---------QASR--AKSAFLATMSHEIRTPMNGVLGTARLLIDS-GLNPIQKRYAEIINR 513
Cdd:PRK13837 415 ELALDCLAHAieRRRLETErdalerrleHARRleAVGTLASGIAHNFNNILGAILGYAEMALNKlARHSRAARYIDEIIS 494
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 514 SGKTLLAILNDVLDYSKIEAGhleiRSLGFDLHQMVEDTFQLMNGKAQEK-KLLFSYHIESDVGrywKGDVIRINQVLNN 592
Cdd:PRK13837 495 AGARARLIIDQILAFGRKGER----NTKPFDLSELVTEIAPLLRVSLPPGvELDFDQDQEPAVV---EGNPAELQQVLMN 567
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 593 LVGNAIK-FTEQGEIDIYVS--------------LNPEDetQVLFEVSDTGIGIakkDQKTL---FDAF--TQAeggmnq 652
Cdd:PRK13837 568 LCSNAAQaMDGAGRVDISLSraklrapkvlshgvLPPGR--YVLLRVSDTGAGI---DEAVLphiFEPFftTRA------ 636
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 653 tGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESEPVETVSiASARCKIR----AKVLVVEDNPVNRVVAE 728
Cdd:PRK13837 637 -GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQA-FFGPGPLPrgrgETVLLVEPDDATLERYE 714
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 729 GFLESMGHEVI--LAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRlkriernkpsdkALNPTPMVAVSAHVFAEE 806
Cdd:PRK13837 715 EKLAALGYEPVgfSTLAAAIAWISKGPERFDLVLVDDRLLDEEQAAAALH------------AAAPTLPIILGGNSKTMA 782
                        410       420       430
                 ....*....|....*....|....*....|
gi 742417147 807 VESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:PRK13837 783 LSPDLLASVAEILAKPISSRTLAYALRTAL 812
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-691 1.65e-19

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: 84.37  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 586 INQVLNNLVGNAIKFTEQGEI---DIYVSLNPEDETQVLFEVSDTGIGIAKKDQKTLFDAF--TQAEGgmnqtggTGLGL 660
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGGCerrELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFytTKSEG-------LGMGL 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 742417147 661 AISRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16920   74 SICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
460-692 2.86e-19

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: 92.49  E-value: 2.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 460 RKQAEQASRaKSAFL-------ATMSHEIRTPMNGVLGTARLLidsGLNPI-QKRYAEI----INRsgktLLAILNDVLD 527
Cdd:COG5805  271 KKEAEELMA-RSEKLsiagqlaAGIAHEIRNPLTSIKGFLQLL---QPGIEdKEEYFDImlseLDR----IESIISEFLA 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 528 YSKIEAGHLEIrslgFDLHQMVEDTFQLMNGKAQEKKLLFSyHIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQ-GEI 606
Cdd:COG5805  343 LAKPQAVNKEK----ENINELIQDVVTLLETEAILHNIQIR-LELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNgGTI 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 607 DIYVSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQaeggmNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRF 686
Cdd:COG5805  418 TIHTE---EEDNSVIIRVIDEGIGIPEERLKKLGEPFFT-----TKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTF 489

                 ....*.
gi 742417147 687 WFSIPL 692
Cdd:COG5805  490 TITLPL 495
PRK09303 PRK09303
histidine kinase;
436-691 3.50e-19

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 90.78  E-value: 3.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 436 EQRTSQLKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMNGV---LGTARLLIDSGLNPIQ-------- 504
Cdd:PRK09303 117 EIDSGRYSQELLQLSDELFVLRQENETLLEQLKFKDRVLAMLAHDLRTPLTAAslaLETLELGQIDEDTELKpalieqlq 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 505 ---KRYAEIINRsgktllaILNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYWkG 581
Cdd:PRK09303 197 dqaRRQLEEIER-------LITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVY-A 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 582 DVIRINQVLNNLVGNAIKFT-EQGEIdiyvSLNPEDET--QVLFEVSDTGIGIAKKDQKTLF-DAF--TQAEGgmnqTGG 655
Cdd:PRK09303 269 DQERIRQVLLNLLDNAIKYTpEGGTI----TLSMLHRTtqKVQVSICDTGPGIPEEEQERIFeDRVrlPRDEG----TEG 340
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 742417147 656 TGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:PRK09303 341 YGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLP 376
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
454-677 5.13e-19

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 91.04  E-value: 5.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 454 LNH-AKARKQAEQASRAksaFLATMSHEIRTPMnGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIE 532
Cdd:NF012163 226 FNQlASTLEKNEQMRRD---FMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSD 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 533 AGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYwkGDVIRINQVLNNLVGNAIKFTEQ-GEIDIYVS 611
Cdd:NF012163 302 EGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSSLVF--GDRDRLMQLFNNLLENSLRYTDSgGSLHISAS 379
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742417147 612 LNPEdetQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQ-TGGTGLGLAISRRIIQAMGGCLEVD 677
Cdd:NF012163 380 QRPK---EVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRaSGGSGLGLAISLNIVQAHGGTLHAA 443
PRK10604 PRK10604
sensor protein RstB; Provisional
478-692 8.50e-19

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 90.43  E-value: 8.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 478 SHEIRTPMngVLGTARLLIDSGLNPIQKryaEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLGFDL----HQMVEDtF 553
Cdd:PRK10604 220 AHELRTPL--VRLRYRLEMSDNLSAAES---QALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLpawlSTHLAD-I 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 554 QLMNgkaQEKkllfsyHIESDV---GRYWKGDVIRINQVLNNLVGNAIKFTEQgeiDIYVSLNPEDEtQVLFEVSDTGIG 630
Cdd:PRK10604 294 QAVT---PEK------TVRLDTphqGDYGALDMRLMERVLDNLLNNALRYAHS---RVRVSLLLDGN-QACLIVEDDGPG 360
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742417147 631 IAKKDQKTLFDAFTQAEGGMNQ-TGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPL 692
Cdd:PRK10604 361 IPPEERERVFEPFVRLDPSRDRaTGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPV 423
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
469-534 3.76e-18

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 79.18  E-value: 3.76e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742417147  469 AKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAG 534
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
713-822 1.23e-17

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: 79.05  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESM-GHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkal 790
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEaGFEVVGeAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPD------- 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 742417147 791 npTPMVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:COG4753   74 --TKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
589-691 1.74e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 78.87  E-value: 1.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 589 VLNNLVGNAIKFTEQ-GEIDIYVSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQTGGTGLGLAISRRII 667
Cdd:cd16948    9 IIGQIVSNALKYSKQgGKIEIYSE---TNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGRNFQESTGMGLYLVKKLC 85
                         90       100
                 ....*....|....*....|....
gi 742417147 668 QAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16948   86 DKLGHKIDVESEVGEGTTFTITFP 109
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
469-534 2.22e-17

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 77.22  E-value: 2.22e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742417147   469 AKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAG 534
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK10490 PRK10490
sensor protein KdpD; Provisional
457-694 1.22e-16

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 85.09  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 457 AKARKQAEQaSRAKSAFLATMSHEIRTPMNGVLGTARLLIDSgLNPIQKRYAEIINRSGKTLLA---ILNDVLDYSKIEA 533
Cdd:PRK10490 652 EQARLASER-EQLRNALLAALSHDLRTPLTVLFGQAEILTLD-LASEGSPHARQASEIRQQVLNttrLVNNLLDMARIQS 729
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 534 GHLEIRSLGFDLHQMVEDTFQLMNgkaqekKLLFSYHIESDVGR---YWKGDVIRINQVLNNLVGNAIKFT-EQGEIDIY 609
Cdd:PRK10490 730 GGFNLRKEWLTLEEVVGSALQMLE------PGLSGHPINLSLPEpltLIHVDGPLFERVLINLLENAVKYAgAQAEIGID 803
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 610 VSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGgMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFS 689
Cdd:PRK10490 804 AH---VEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNK-ESAIPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVT 879

                 ....*
gi 742417147 690 IPLEE 694
Cdd:PRK10490 880 LPLET 884
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
585-691 1.75e-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 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: 75.96  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 585 RINQVLNNLVGNAIKFTEQG-EIDIYVSLNPeDETQVLFEvsDTGIGIAKKDQKTLFDAFTQAEGGMNQ-TGGTGLGLAI 662
Cdd:cd16946    4 RLQQLFVNLLENSLRYTDTGgKLRIRAAQTP-QEVRLDVE--DSAPGVSDDQLARLFERFYRVESSRNRaSGGSGLGLAI 80
                         90       100
                 ....*....|....*....|....*....
gi 742417147 663 SRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16946   81 CHNIALAHGGTISAEHSPLGGLRLVLTLP 109
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
461-691 1.83e-16

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 83.14  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 461 KQAEQASRAksaFLATMSHEIRTPMNGVLGTARLLIDSGLN-PIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLeir 539
Cdd:PRK11006 198 HQLEGARRN---FFANVSHELRTPLTVLQGYLEMMQDQPLEgALREKALHTMREQTQRMEGLVKQLLTLSKIEAAPT--- 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 540 slgFDLHQMVeDTFQLMNGKAQEKKLLFS--YHIESDVGRYWK--GDVIRINQVLNNLVGNAIKFTEQG-EIDIYVSLNP 614
Cdd:PRK11006 272 ---IDLNEKV-DVPMMLRVLEREAQTLSQgkHTITFEVDNSLKvfGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQRVP 347
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742417147 615 EDetqVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMN-QTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:PRK11006 348 QG---AEFSVEDNGPGIAPEHIPRLTERFYRVDKARSrQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
462-692 7.41e-16

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 81.37  E-value: 7.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 462 QAEQASRAKSAFL----ATMSHEIRTPMNGVLGTARLLIDSGLNPIQKR-YAEIINRSGKTLLAILNDVLDYSKieAGHL 536
Cdd:PRK10364 225 QDEMKRKEKLVALghlaAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHqLAQVMAKEADRLNRVVSELLELVK--PTHL 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 537 EIRSLgfDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYwKGDVIRINQVLNNLVGNAIK-FTEQGEIDIYVSlnpE 615
Cdd:PRK10364 303 ALQAV--DLNDLINHSLQLVSQDANSREIQLRFTANDTLPEI-QADPDRLTQVLLNLYLNAIQaIGQHGVISVTAS---E 376
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742417147 616 DETQVLFEVSDTGIGIAKKDQKTLFDAF--TQAEGgmnqtggTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPL 692
Cdd:PRK10364 377 SGAGVKISVTDSGKGIAADQLEAIFTPYftTKAEG-------TGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
555-695 1.17e-15

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 80.28  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 555 LMNGK---AQEKKLLFSYHIESDVgRYWKGDVIRINQVLNNLVGNAI-----KFTEQGEIDIYVSlnpEDETQVLFEVSD 626
Cdd:COG3290  249 LLLGKaarARERGIDLTIDIDSDL-PDLPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSIR---DDGDELVIEVED 324
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742417147 627 TGIGIAKKDQKTLFDA--FTQAEGGmnqtggTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEES 695
Cdd:COG3290  325 SGPGIPEELLEKIFERgfSTKLGEG------RGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
464-700 1.23e-15

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 80.83  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 464 EQASRAksaFLATMSHEIRTPM-----------NGVlgtaRLLIDSGLNPIQkryAEIinrsgKTLLAILNDVLDYSKIE 532
Cdd:PRK10549 237 EQMRRD---FMADISHELRTPLavlrgeleaiqDGV----RKFTPESVASLQ---AEV-----GTLTKLVDDLHQLSLSD 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 533 AGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYwkGDVIRINQVLNNLVGNAIKFT-EQGEIDIyvS 611
Cdd:PRK10549 302 EGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSATVF--GDPDRLMQLFNNLLENSLRYTdSGGSLHI--S 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 612 LNPEDETQVL-FEvsDTGIGIAKKDQKTLFDAFTQAEGGMNQ-TGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFS 689
Cdd:PRK10549 378 AEQRDKTLRLtFA--DSAPGVSDEQLQKLFERFYRTEGSRNRaSGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVE 455
                        250
                 ....*....|.
gi 742417147 690 IPLEESEPVET 700
Cdd:PRK10549 456 LPLERDLQREV 466
envZ PRK09467
osmolarity sensor protein; Provisional
455-694 1.27e-15

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 80.34  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 455 NH-AKARKQAEQaSRAksAFLATMSHEIRTPMNgvlgtaRLLIDSGLNPIQKRY-AEIINRSGKTLLAILNDVLDYskIE 532
Cdd:PRK09467 216 NQmAAGIKQLED-DRT--LLMAGVSHDLRTPLT------RIRLATEMMSEEDGYlAESINKDIEECNAIIEQFIDY--LR 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 533 AGHLEIRSLGfDLHQMVEDTFQLMNGKAQEkkllfsyhIESDVGRY---WKGDVIRINQVLNNLVGNAIKFteqGEIDIY 609
Cdd:PRK09467 285 TGQEMPMEMA-DLNALLGEVIAAESGYERE--------IETALQPGpieVPMNPIAIKRALANLVVNAARY---GNGWIK 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 610 VSLNpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQ---AEGGMnqtgGTGLGLAISRRIIQAMGGCLEV-DSDEGhGSR 685
Cdd:PRK09467 353 VSSG-TEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRgdsARGSS----GTGLGLAIVKRIVDQHNGKVELgNSEEG-GLS 426

                 ....*....
gi 742417147 686 FWFSIPLEE 694
Cdd:PRK09467 427 ARAWLPLTT 435
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
715-822 4.81e-15

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: 71.67  E-value: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 715 LVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLkrieRNKPSDkalnpTP 794
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRL----REKGSD-----IP 71
                         90       100       110
                 ....*....|....*....|....*....|.
gi 742417147 795 MVAVSAhvFAEE---VESyLAAGFDGYLPKP 822
Cdd:cd17574   72 IIMLTA--KDEEedkVLG-LELGADDYITKP 99
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
714-841 8.51e-15

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: 71.46  E-value: 8.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIERNKPsdkalnPT 793
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEI---LKWIQERSL------PT 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 742417147 794 PMVAVSAHVFAE-EVESYLAAGFDgYLPKPMEKEALSALIQDMLDGKQL 841
Cdd:cd17572   72 SVIVITAHGSVDiAVEAMRLGAYD-FLEKPFDADRLRVTVRNALKHRKL 119
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
581-687 9.27e-15

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 71.28  E-value: 9.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 581 GDVIRINQVLNNLVGNAIKFTEQGEIdIYVSLNPEDETQvlFEVSDTGIGIAKKDQKTLFDAFTQAEGgMNqTGGTGLGL 660
Cdd:cd16940    9 GDALLLFLLLRNLVDNAVRYSPQGSR-VEIKLSADDGAV--IRVEDNGPGIDEEELEALFERFYRSDG-QN-YGGSGLGL 83
                         90       100
                 ....*....|....*....|....*..
gi 742417147 661 AISRRIIQAMGGCLEVDSDEGHGSRFW 687
Cdd:cd16940   84 SIVKRIVELHGGQIFLGNAQGGGLEAW 110
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
455-691 1.29e-14

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 77.50  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 455 NHAKARkqAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSglNPIQKRYAEII-------NRSGKtllaILNDVLD 527
Cdd:PRK09835 249 NHMIER--IEDVFTRQSNFSADIAHEIRTPITNLITQTEIALSQ--SRSQKELEDVLysnleelTRMAK----MVSDMLF 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 528 YSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLlfSYHIESDVGRYWkGDVIRINQVLNNLVGNAIKFTEQGEiD 607
Cdd:PRK09835 321 LAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGV--ELRFVGDPCQVA-GDPLMLRRAISNLLSNALRYTPAGE-A 396
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 608 IYVSLNpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQTG-GTGLGLAISRRIIQAMGGCLEVDSDeGHGSRF 686
Cdd:PRK09835 397 ITVRCQ-EVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGeGSGIGLAIVKSIVVAHKGTVAVTSD-ARGTRF 474

                 ....*
gi 742417147 687 WFSIP 691
Cdd:PRK09835 475 VISLP 479
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
713-822 1.64e-14

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: 70.22  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALNP 792
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLK-------EDPETRH 73
                         90       100       110
                 ....*....|....*....|....*....|...
gi 742417147 793 TPMVAVSAhvfAEEVESY---LAAGFDGYLPKP 822
Cdd:cd17538   74 IPVIMITA---LDDREDRirgLEAGADDFLSKP 103
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
714-836 1.64e-14

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: 70.62  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVnrvVAEGF---LESM-GHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRiernkpsdk 788
Cdd:cd17535    1 VLIVDDHPL---VREGLrrlLESEpDIEVVGeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--------- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 742417147 789 ALNPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17535   69 RYPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
582-691 1.91e-14

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: 70.21  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 582 DVIRINQVLNNLVGNAIKFTEQGEIdIYVSLNPEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEG-GMNQTGGTGLGL 660
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGR-IRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGsSTRAHGGTGLGL 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 742417147 661 AISRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16925   80 SIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
590-691 2.00e-14

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 70.31  E-value: 2.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 590 LNNLVGNAIKFT-EQGEIDIYVSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAE-GGMNQTGGTGLGLAISRRII 667
Cdd:cd16952    5 FSNLVSNAVKYTpPSDTITVRWS---QEESGARLSVEDTGPGIPPEHIPRLTERFYRVDiERCRNTGGTGLGLAIVKHVM 81
                         90       100
                 ....*....|....*....|....
gi 742417147 668 QAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16952   82 SRHDARLLIASELGKGSRFTCLFP 105
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
712-785 3.91e-14

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 69.56  E-value: 3.91e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNKP 785
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLP 74
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-687 1.35e-13

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 67.47  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 586 INQVLNNLVGNAIKFTeQGEIDIYVSLNPEdetQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNqTGGTGLGLAISRR 665
Cdd:cd16950    1 LKRVLSNLVDNALRYG-GGWVEVSSDGEGN---RTRIQVLDNGPGIAPEEVDELFQPFYRGDNARG-TSGTGLGLAIVQR 75
                         90       100
                 ....*....|....*....|....
gi 742417147 666 IIQAMGGCLEVDSDEGHG--SRFW 687
Cdd:cd16950   76 ISDAHGGSLTLANRAGGGlcARIE 99
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
589-692 1.54e-13

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 67.46  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 589 VLNNLVGNAIKFTEQgeiDIYVSLNPEDETQVLfEVSDTGIGIAKKDQKTLFDAFTQAEGGMN-QTGGTGLGLAISRRII 667
Cdd:cd16939    4 ALDNLLRNALRYAHR---TVRIALLVSGGRLTL-IVEDDGPGIPAAARERVFEPFVRLDPSRDrATGGFGLGLAIVHRVA 79
                         90       100
                 ....*....|....*....|....*
gi 742417147 668 QAMGGCLEVDSDEGHGSRFWFSIPL 692
Cdd:cd16939   80 LWHGGHVECDDSELGGACFRLTWPR 104
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
467-530 1.84e-13

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 66.08  E-value: 1.84e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742417147 467 SRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGL-NPIQKRYAEIINRSGKTLLAILNDVLDYSK 530
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
578-678 2.36e-13

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: 67.54  E-value: 2.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 578 YWKGDVIRINQVLNNLVGNAIKFTEQGEIdIYVSLNpEDETQVLFEVSDTGIGIAKKDQKTLFD-AFTQAEGGMNQTGGT 656
Cdd:cd16947   13 YANANTEALQRILKNLISNAIKYGSDGKF-LGMTLR-EDEKHVYIDIWDKGKGISETEKDHVFErLYTLEDSRNSAKQGN 90
                         90       100
                 ....*....|....*....|..
gi 742417147 657 GLGLAISRRIIQAMGGCLEVDS 678
Cdd:cd16947   91 GLGLTITKRLAESMGGSIYVNS 112
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
714-822 4.86e-13

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: 65.86  E-value: 4.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALNPT 793
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLR-------KNADFDTI 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 742417147 794 PMVAVSAH-VFAEEVESYlAAGFDGYLPKP 822
Cdd:cd19927   74 PVIFLTAKgMTSDRIKGY-NAGCDGYLSKP 102
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
712-836 6.91e-13

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: 66.12  E-value: 6.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRiernkpsDKALN 791
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKR-------DEMTR 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17618   74 DIPIIMLTARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
476-692 7.74e-13

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 71.80  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 476 TMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQL 555
Cdd:PRK11100 262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 556 MNGKAQEKKLLFSYHIEsdvGRYWKGDVIRINQVLNNLVGNAIKFT-EQGEIDIYVSLnpeDETQVLFEVSDTGIGIAKK 634
Cdd:PRK11100 342 REAQAAAKGITLRLRPD---DARVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEV---DGEQVALSVEDQGPGIPDY 415
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 742417147 635 DQKTLFDAFTQAEGGMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPL 692
Cdd:PRK11100 416 ALPRIFERFYSLPRPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
713-766 1.14e-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: 63.36  E-value: 1.14e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 742417147   713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLP 766
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-688 1.20e-12

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: 64.79  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 586 INQVLNNLVGNAI-KFTEQGEIDIYVSLNPEDETQVLfEVSDTGIGIAKKDQKTLFDAF-TQAEGGMnqtgGTGLGLAIS 663
Cdd:cd16976    1 IQQVLMNLLQNALdAMGKVENPRIRIAARRLGGRLVL-VVRDNGPGIAEEHLSRVFDPFfTTKPVGK----GTGLGLSIS 75
                         90       100
                 ....*....|....*....|....*
gi 742417147 664 RRIIQAMGGCLEVDSDEGHGSRFWF 688
Cdd:cd16976   76 YGIVEEHGGRLSVANEEGAGARFTF 100
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-692 1.76e-12

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


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 64.65  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 586 INQVLNNLVGNAIKFT-EQGEIDIYVslnpeDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMN-QTGGTGLGLAIS 663
Cdd:cd16949    1 LARALENVLRNALRYSpSKILLDISQ-----DGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDrESGGTGLGLAIA 75
                         90       100
                 ....*....|....*....|....*....
gi 742417147 664 RRIIQAMGGCLEVDSDEGHGSRFWFSIPL 692
Cdd:cd16949   76 ERAIEQHGGKIKASNRKPGGLRVRIWLPA 104
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
713-836 1.92e-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: 65.05  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIErnkpSDKALN 791
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKAGGFDFVITDWNMPNMDGLEL---LKTIR----ADGALS 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd19923   75 HLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
714-822 3.08e-12

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: 63.68  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALNPT 793
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLK-------ADPATRHI 73
                         90       100
                 ....*....|....*....|....*....
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:cd19920   74 PVIFLTALTDTEDKVKGFELGAVDYITKP 102
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
588-691 3.24e-12

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 64.13  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 588 QVLNNLVGNAIKFTEQGEIDIYVSLNPEDETQVLfEVSDTGIGIAKKDQKTLFDAF-TQAEGGMNQTGGTGLGLAISRRI 666
Cdd:cd16953    3 QVLRNLIGNAISFSPPDTGRITVSAMPTGKMVTI-SVEDEGPGIPQEKLESIFDRFyTERPANEAFGQHSGLGLSISRQI 81
                         90       100
                 ....*....|....*....|....*....
gi 742417147 667 IQAMGGCLEV----DSDEGHGSRFWFSIP 691
Cdd:cd16953   82 IEAHGGISVAenhnQPGQVIGARFTVQLP 110
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
713-869 3.92e-12

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 67.15  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESM-GHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERnkpsdkal 790
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKYpDLEVVGeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDP-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 791 nPTPMVAVSAHV-FAeeVESYLAAGFDgYLPKPMEKEALSALIQDMLDGKQLLLPQSGECLAQDEIITTSDNDTVSVTTD 869
Cdd:COG3279   75 -PPPIIFTTAYDeYA--LEAFEVNAVD-YLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKDRIFVKSGGKLVKIPLD 150
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
714-833 4.98e-12

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 63.42  E-value: 4.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIID--KHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALn 791
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIR-------LEMDL- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742417147 792 ptPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:cd17584   73 --PVIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQ 112
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
712-833 5.03e-12

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: 63.58  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMGHEVI-LAENGLEAEQIIDKHDFDIALVDINLP-DCNGADLIHRLKRIernkpsdka 789
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK--------- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742417147 790 lNPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:cd17534   72 -FDIPVIFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAIE 114
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
713-834 1.09e-11

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: 64.55  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIErnkpsdkalNP 792
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERD---------PD 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742417147 793 TPMV----------AVSAHvfaeevesylAAGFDGYLPKPMEKEALSALIQD 834
Cdd:COG4567   77 ARIVvltgyasiatAVEAI----------KLGADDYLAKPADADDLLAALER 118
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
714-836 1.48e-11

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 62.34  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALNPT 793
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIK-------SDPDLKDI 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17598   74 PVILLTTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
712-783 1.54e-11

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: 62.07  E-value: 1.54e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMG-HEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERN 783
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGL 73
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
711-833 1.92e-11

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: 64.21  E-value: 1.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRiernkpsdka 789
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISE---------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742417147 790 LNPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:COG3707   73 ERPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALE 116
PRK10816 PRK10816
two-component system response regulator PhoP;
713-836 5.32e-11

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 63.60  E-value: 5.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkalnp 792
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742417147 793 TPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:PRK10816  73 LPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALM 116
PRK13557 PRK13557
histidine kinase; Provisional
602-766 9.30e-11

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 65.46  E-value: 9.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 602 EQGEIDIYVSLNPEDETQVLFEVSDTGIGIAKKDQKTLFDAF--TQAEGGmnqtgGTGLGLAISRRIIQAMGGCLEVDSD 679
Cdd:PRK13557 307 EIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFftTKEEGK-----GTGLGLSMVYGFAKQSGGAVRIYSE 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 680 EGHGS--RFWFSIPLEESEPVETVSIASARCKIRAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKH-DF 756
Cdd:PRK13557 382 VGEGTtvRLYFPASDQAENPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEV 461
                        170
                 ....*....|
gi 742417147 757 DIALVDINLP 766
Cdd:PRK13557 462 DLLFTDLIMP 471
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
714-836 1.24e-10

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 59.60  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDN-PVNRVVAEGfLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkalnp 792
Cdd:cd19934    1 LLLVEDDaLLAAQLKEQ-LSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 793 TPMVAVSAHV-FAEEVESyLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd19934   71 TPVLILTARDsWQDKVEG-LDAGADDYLTKPFHIEELLARLRALI 114
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
473-691 1.40e-10

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: 65.15  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  473 FLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLGFDLHQMVEdt 552
Cdd:TIGR03785 488 MSSRLSHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLS-- 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147  553 fQLMNGKAQ-EKKLLFSYHIESDvGRYWKGDVIRINQVLNNLVGNAIKFTEQGEIdIYVSLNpEDETQVLFEVSDTGIGI 631
Cdd:TIGR03785 566 -GCMQGYQMtYPPQRFELNIPET-PLVMRGSPELIAQMLDKLVDNAREFSPEDGL-IEVGLS-QNKSHALLTVSNEGPPL 641
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742417147  632 AKKDQKTLFDAF-TQAEGGMNQTGGTGLGLAISRRIIQAMGGCLEV-DSDEGHGSRFWFSIP 691
Cdd:TIGR03785 642 PEDMGEQLFDSMvSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAeNRQQNDGVVFRISLP 703
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
714-779 1.45e-10

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: 59.32  E-value: 1.45e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKR 779
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE 68
glnL PRK11073
nitrogen regulation protein NR(II);
447-692 1.54e-10

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 63.95  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 447 RRLNEEVLNHAKarkqaEQASRAKSAFLAtmsHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDVL 526
Cdd:PRK11073 115 RRLSQEQLQHAQ-----QVAARDLVRGLA---HEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLL 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 527 DYSKieAGHLEIRSLgfdlHQMVEDTFQLMNGKAQEK-KLLFSYH-------IESDvgrywkgdviRINQVLNNLVGNAI 598
Cdd:PRK11073 187 GPQR--PGTHVTESI----HKVAERVVQLVSLELPDNvRLIRDYDpslpelaHDPD----------QIEQVLLNIVRNAL 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 599 KFTEQ--GEIDIyvslnpedETQVLF---------------EVSDTGIGIAKKDQKTLFDAFTQAeggmnQTGGTGLGLA 661
Cdd:PRK11073 251 QALGPegGTITL--------RTRTAFqltlhgeryrlaariDIEDNGPGIPPHLQDTLFYPMVSG-----REGGTGLGLS 317
                        250       260       270
                 ....*....|....*....|....*....|.
gi 742417147 662 ISRRIIQAMGGCLEVDSDEGHGSrfwFSIPL 692
Cdd:PRK11073 318 IARNLIDQHSGKIEFTSWPGHTE---FSVYL 345
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
714-822 2.59e-10

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: 57.94  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERnkpsdkalnpT 793
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA----------V 70
                         90       100
                 ....*....|....*....|....*....
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:cd17620   71 PVIVLSARDEESDKIAALDAGADDYLTKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
714-837 3.07e-10

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 58.28  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIERNKPSdkalnpT 793
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLEL---LKEIKEKYPD------L 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 794 PMVAVSAHVFAE-EVESYLAAGFDgYLPKPMEKEALSALIQDMLD 837
Cdd:cd17550   72 PVIMISGHGTIEtAVKATKLGAYD-FIEKPLSLDRLLLTIERALE 115
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
712-835 3.20e-10

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 58.37  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkaln 791
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPD-------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 792 pTPMVAVS-AHVFAEEVESYLAAGFDgYLPKPmekealsalIQDM 835
Cdd:cd17555   73 -TPVIVVSgAGVMSDAVEALRLGAWD-YLTKP---------IEDL 106
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-688 7.28e-10

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: 57.09  E-value: 7.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 582 DVIRINQVLNNLVGNAIKFTEQGEidiYVSLNPEDETQVL-FEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQTGGTGLGL 660
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGG---TVSISIYDEEEYLyFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGHYGMGL 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 742417147 661 AISRRIIQAMGGCLEVDSDEGHGS--RFWF 688
Cdd:cd16975   78 YIAKNLVEKHGGSLIIENSQKGGAevTVKI 107
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
713-834 9.39e-10

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: 57.25  E-value: 9.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMG--HEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRieRNKPSDkal 790
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEQVPgfTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA--AGHDVD--- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742417147 791 nptpMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQD 834
Cdd:cd19925   77 ----VIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
588-691 1.64e-09

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: 56.25  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 588 QVLNNLVGNAIKFT--EQGEIDI------YVSLNPEDETQVL-FEVSDTGIGIAKKDQKTLFDAFTQAeggmnQTGGTGL 658
Cdd:cd16918    3 QVFLNLVRNAAQALagSGGEIILrtrtqrQVTLGHPRHRLALrVSVIDNGPGIPPDLQDTIFYPMVSG-----RENGTGL 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 742417147 659 GLAISRRIIQAMGGCLEVDSDEGHgSRFWFSIP 691
Cdd:cd16918   78 GLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
712-852 1.84e-09

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 58.89  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMGHEVILAE--NGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLkrieRNKPSDKA 789
Cdd:PRK10651   7 ATILLIDDHPMLRTGVKQLISMAPDITVVGEasNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKL----REKSLSGR 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742417147 790 LnptPMVAVSAHvfAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQSGECLAQ 852
Cdd:PRK10651  83 I---VVFSVSNH--EEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGEMVLSEALTPVLAA 140
ompR PRK09468
osmolarity response regulator; Provisional
713-868 2.14e-09

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 59.22  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpsdKALNP 792
Cdd:PRK09468   7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLR---------SQNNP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 793 TPMVAVSAHvfAEEVESY--LAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPqsGECLAQDEIIT------------- 857
Cdd:PRK09468  78 TPIIMLTAK--GEEVDRIvgLEIGADDYLPKPFNPRELLARIRAVLRRQAPELP--GAPSQEEEVIAfgkfklnlgtrel 153
                        170
                 ....*....|.
gi 742417147 858 TSDNDTVSVTT 868
Cdd:PRK09468 154 FRGDEPMPLTT 164
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
714-837 2.26e-09

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: 56.19  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRvvaEGFL-----ESMGHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsd 787
Cdd:cd17536    1 VLIVDDEPLIR---EGLKklidwEELGFEVVGeAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPD---- 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 742417147 788 kalnpTPMVAVSAHvfaEEVEsY----LAAGFDGYLPKPMEKEALSALIQDMLD 837
Cdd:cd17536   74 -----IKIIILSGY---DDFE-YaqkaIRLGVVDYLLKPVDEEELEEALEKAKE 118
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
899-954 2.27e-09

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: 55.05  E-value: 2.27e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 742417147  899 HIIDLFRQTSADVLSQMESSAQNGESRAVKDLAHKLKGSAGSLGLTALMNTCQSIE 954
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELE 56
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
714-822 2.28e-09

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: 55.52  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNP-VNRVVAEGFLESmGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRiernkpsdkALNP 792
Cdd:cd19935    1 ILVVEDEKkLAEYLKKGLTEE-GYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA---------AGKQ 70
                         90       100       110
                 ....*....|....*....|....*....|..
gi 742417147 793 TPMVAVSAH--VfAEEVESyLAAGFDGYLPKP 822
Cdd:cd19935   71 TPVLMLTARdsV-EDRVKG-LDLGADDYLVKP 100
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
713-822 2.48e-09

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: 55.91  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIernKPSDKALN- 791
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAL---QPDARIVVl 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 742417147 792 ------PTpmvAVSAhvfaeevesyLAAGFDGYLPKP 822
Cdd:cd17563   79 tgyasiAT---AVEA----------IKLGADDYLAKP 102
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
713-826 2.60e-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: 55.99  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDfDIALV--DINLPDCNGADLIHRLkrieRNKPSDKAL 790
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHP-DIKLVitDYNMPEMDGFELVREI----RKKYSRDQL 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 742417147 791 nptPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKE 826
Cdd:cd17544   77 ---AIIGISASGDNALSARFIKAGANDFLTKPFLPE 109
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
714-833 3.21e-09

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: 55.57  E-value: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVnrvVAEGF---LESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIERNKPSdkal 790
Cdd:cd17624    1 ILLVEDDAL---LGDGLktgLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDL---LRRWRRQGQS---- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 742417147 791 npTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:cd17624   71 --LPVLILTARDGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
PRK15479 PRK15479
transcriptional regulator TctD;
713-854 4.49e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 57.81  E-value: 4.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNKPsdkALNP 792
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLP---VLLL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742417147 793 TPMVAVSAHVFAeevesyLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQS---GECLAQDE 854
Cdd:PRK15479  79 TARSAVADRVKG------LNVGADDYLPKPFELEELDARLRALLRRSAGQVQEVqqlGELIFHDE 137
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
714-836 4.94e-09

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: 55.08  E-value: 4.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpsdKALNPT 793
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLR---------AAGNDL 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17627   72 PILVLTARDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
714-832 5.25e-09

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: 54.74  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKrieRNKPSdkalnpT 793
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIK---EKHPS------I 71
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALI 832
Cdd:cd17573   72 VVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
713-835 5.34e-09

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: 54.85  E-value: 5.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNR-VVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERnkpsdkaln 791
Cdd:cd17593    2 KVLICDDSSMARkQLARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQL--------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDM 835
Cdd:cd17593   73 ETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
446-699 5.55e-09

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 60.33  E-value: 5.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 446 NRRLNeevlnhaKARKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINRSGKTLLAILNDV 525
Cdd:PRK10618 433 NKKLQ-------QAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNI 505
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 526 LDYSKIEAGHLEIRSLGFDLHQMVEDTFQ----LMNGKAQekKLLFSYHIESDVGRYwkGDVIRINQVLNNLVGNAIKFT 601
Cdd:PRK10618 506 QLLNMLETQDWKPEQELFSLQDLIDEVLPevlpAIKRKGL--QLLIHNHLKAEQLRI--GDRDALRKILLLLLNYAITTT 581
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 602 EQGEIDIYVSLNPEDETQVLFEVSDTGIGIAKKDQKTL-FDAFTQAEGGMNQTgGTGLGLAISRRIIQAMGGCLEVDSDE 680
Cdd:PRK10618 582 AYGKITLEVDQDESSPDRLTIRILDTGAGVSIKELDNLhFPFLNQTQGDRYGK-ASGLTFFLCNQLCRKLGGHLTIKSRE 660
                        250       260
                 ....*....|....*....|
gi 742417147 681 GHGSRFWFSIPLE-ESEPVE 699
Cdd:PRK10618 661 GLGTRYSIHLKMLaADPEVE 680
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
714-833 5.55e-09

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 54.72  E-value: 5.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERnkpsdkalnPT 793
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKV---------KT 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:cd17616   72 PILILSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
709-836 7.96e-09

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 59.09  E-value: 7.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 709 KIRAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGadlIHRLKRIERNKPSdk 788
Cdd:PRK11361   2 TAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDG---IKALKEMRSHETR-- 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 742417147 789 alnpTPMVAVSAhvFAE---EVESYLAAGFDgYLPKPMEKEALSALIQDML 836
Cdd:PRK11361  77 ----TPVILMTA--YAEvetAVEALRCGAFD-YVIKPFDLDELNLIVQRAL 120
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
713-822 9.76e-09

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: 54.32  E-value: 9.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESM-GHEVI-LAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIernkpsdKAL 790
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDpDIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEA---LRRI-------MAE 71
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 742417147 791 NPTPMVAVSAHVF--AEEVESYLAAG-FDgYLPKP 822
Cdd:cd17541   72 RPTPVVMVSSLTEegAEITLEALELGaVD-FIAKP 105
PRK10766 PRK10766
two-component system response regulator TorR;
713-778 1.44e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 56.20  E-value: 1.44e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLK 778
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR 69
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
713-828 1.87e-08

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: 53.56  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQII--DKHDFDIALVDINLPDCNGADLIHRLKriERNKPSDKAL 790
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLasAEHSFQLVLLDLCMPEMDGFEVALRIR--KLFGRRERPL 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 742417147 791 nptpMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEAL 828
Cdd:cd19933   80 ----IVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
589-691 2.32e-08

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 52.67  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 589 VLNNLVGNAIKF---TEQGEIDIYVSLNpEDETQVLFEVSDTGIGIAKKDQKTLFDA-FTQAEggmnqTGGTGLGLAISR 664
Cdd:cd16915    4 IVGNLIDNALDAlaaTGAPNKQVEVFLR-DEGDDLVIEVRDTGPGIAPELRDKVFERgVSTKG-----QGERGIGLALVR 77
                         90       100
                 ....*....|....*....|....*..
gi 742417147 665 RIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16915   78 QSVERLGGSITVESEPGGGTTFSIRIP 104
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
897-986 2.73e-08

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: 52.38  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 897 MLHIIDLFRQTSADVLSQMESSAQNGESR----AVKDLAHKLKGSAGSLGLTALMNTCQSIEIASESLEAYTMLRADLKG 972
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELEDAedlnEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDGLEVTPELID 80
                         90
                 ....*....|....
gi 742417147 973 QVSDSVIALDELMA 986
Cdd:cd00088   81 LLLDALDALKAELE 94
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
589-682 3.09e-08

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: 52.39  E-value: 3.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 589 VLNNLVGNAIKFTEQGEIdIYVSLNPEDETqVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNqTGGTGLGLAISRRIIQ 668
Cdd:cd16923    4 VFSNLLSNAIKYSPENTR-IYITSFLTDDV-VNIMFKNPSSHPLDFKLEKLFERFYRGDNSRN-TEGAGLGLSIAKAIIE 80
                         90
                 ....*....|....
gi 742417147 669 AMGGCLEVDSDEGH 682
Cdd:cd16923   81 LHGGSASAEYDDNH 94
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
713-833 5.81e-08

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: 52.06  E-value: 5.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLkriernkpsdKALNP 792
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTI----------RARSD 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742417147 793 TPMVAVSAHVFAEE-VESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:cd17594   71 VPIIIISGDRRDEIdRVVGLELGADDYLAKPFGLRELLARVR 112
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
715-836 6.22e-08

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: 51.84  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 715 LVVEDNP-VNRVVAEgFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpsdKALNPT 793
Cdd:cd17625    1 LVVEDEKdLSEAITK-HLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLR---------EEGIET 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17625   71 PVLLLTALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
713-833 6.95e-08

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: 52.03  E-value: 6.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVN-RVVAEGFLES-MGHEVILAENGLEAEQIIDKHD-------FDIALVDINLPDCNGADLIHRLKriern 783
Cdd:cd17557    1 TILLVEDNPGDaELIQEAFKEAgVPNELHVVRDGEEALDFLRGEGeyadaprPDLILLDLNMPRMDGFEVLREIK----- 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 742417147 784 kpSDKALNPTPMVAVSAHVFAEEVE-SYlAAGFDGYLPKPMEKEALSALIQ 833
Cdd:cd17557   76 --ADPDLRRIPVVVLTTSDAEEDIErAY-ELGANSYIVKPVDFEEFVEAIR 123
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
711-836 7.35e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 56.19  E-value: 7.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGadlIHRLKRIernkpsdKAL 790
Cdd:PRK10365   5 NIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDG---IATLKEI-------KAL 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 742417147 791 NPT-PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:PRK10365  75 NPAiPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
pleD PRK09581
response regulator PleD; Reviewed
712-832 7.90e-08

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 56.06  E-value: 7.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALN 791
Cdd:PRK09581   3 ARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLK-------SDPATT 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742417147 792 PTPMVAVSA-HVFAEEVESyLAAGFDGYLPKPMEKEALSALI 832
Cdd:PRK09581  76 HIPVVMVTAlDDPEDRVRG-LEAGADDFLTKPINDVALFARV 116
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
713-833 8.37e-08

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: 51.65  E-value: 8.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVI-LAENGLEAEQIIDKHDFDIALVDINLPDCNGADlihrLKRIERNKpsdkalN 791
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIE----AAKIITSE------N 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:cd19932   72 IAPIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIE 113
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
712-836 8.37e-08

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: 51.53  E-value: 8.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLkrieRNKPSDKAln 791
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKEL----RKLPAYKF-- 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 792 pTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17562   75 -TPILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
589-693 9.25e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 56.07  E-value: 9.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 589 VLNNLVGNAIK-FTEQGEIDIYVSLNPEDEtQVLFEVSDTGIGIAKKDQKTLFDaftqaEGGMNQTGGTGLGLAISRRII 667
Cdd:PRK11086 437 ILGNLIENALEaVGGEEGGEISVSLHYRNG-WLHCEVSDDGPGIAPDEIDAIFD-----KGYSTKGSNRGVGLYLVKQSV 510
                         90       100
                 ....*....|....*....|....*.
gi 742417147 668 QAMGGCLEVDSDEGHGSRFWFSIPLE 693
Cdd:PRK11086 511 ENLGGSIAVESEPGVGTQFFVQIPWD 536
PRK10610 PRK10610
chemotaxis protein CheY;
713-828 1.02e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 51.90  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMG-HEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALN 791
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIR-------ADGAMS 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEAL 828
Cdd:PRK10610  80 ALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATL 116
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
713-836 1.04e-07

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: 51.20  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkalnp 792
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPD--------- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742417147 793 TPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17615   72 VPVLFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL 115
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
713-837 1.08e-07

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: 51.40  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESM-GHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLkrieRNKPSDKALn 791
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKL----QANPETQSI- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 742417147 792 ptPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLD 837
Cdd:cd17552   78 --PVILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
713-777 1.09e-07

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 51.43  E-value: 1.09e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESM-GHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRL 777
Cdd:COG2197    3 RVLIVDDHPLVREGLRALLEAEpDIEVVGeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
714-780 1.33e-07

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 50.42  E-value: 1.33e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKH-DFDIALVDINLPD-CNGADLIHRLKRI 780
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARRR 69
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-691 1.63e-07

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 50.61  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 582 DVIRINQVLNNLVGNA---IKFTEQGEIDIYVSLNPEDETQVLFEVSDTGIGIAKKDQKTLFDAFTqaeggMNQTGGTGL 658
Cdd:cd16944    1 DTTQISQVLTNILKNAaeaIEGRPSDVGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPYV-----TTRPKGTGL 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 742417147 659 GLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16944   76 GLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
589-691 1.64e-07

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: 50.50  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 589 VLNNLVGNAIK--FTEQGEI-DIYVSLNPeDETQVLFEVSDTGIGIAKKDQKTLfdaftqAEGGMNQTGGTGLGLA-ISR 664
Cdd:cd16957    5 ALQVLVENAIRhaFPKRKENnEVRVVVKK-DQHKVHVSVSDNGQGIPEERLDLL------GKTTVTSEKGTGTALEnLNR 77
                         90       100
                 ....*....|....*....|....*....
gi 742417147 665 RIIQAMG--GCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16957   78 RLIGLFGseACLHIESEVHGGTEVWFVIP 106
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
713-836 1.69e-07

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: 50.74  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVIL-AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkaln 791
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPN-------- 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 792 pTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17542   74 -AKVIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
713-822 2.59e-07

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: 49.81  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEA-EQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkaln 791
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEAlEKLQQGKDIDIVVTDIVMPEMDGIELAREARKIDPD-------- 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 742417147 792 pTPMVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:cd18160   73 -VKILFISGGAAAAPELLSDAVGDNATLKKP 102
PRK11173 PRK11173
two-component response regulator; Provisional
713-770 4.19e-07

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 52.32  E-value: 4.19e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNG 770
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNG 62
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
714-822 4.59e-07

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: 49.30  E-value: 4.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDK---------HDFDIALVDINLPDCNGADLIHRLKriernk 784
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELR------ 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 742417147 785 pSDKALNPTPMVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:cd19924   75 -DDPRLANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
620-691 6.26e-07

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: 48.92  E-value: 6.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742417147 620 VLFEVSDTGIGIAKKDQKTLFDAF--TQAEGGmnqtgGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16919   48 VCLEVSDTGSGMPAEVLRRAFEPFftTKEVGK-----GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
588-687 7.52e-07

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: 48.61  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 588 QVLNNLVGNAIKFT-EQGEIDIYVSLNPEdetQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQTGGTGLGLAISRRI 666
Cdd:cd16945    7 QAINNLLDNAIDFSpEGGLIALQLEADTE---GIELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQKSTGLGLAFVQEV 83
                         90       100
                 ....*....|....*....|..
gi 742417147 667 IQAMGGCLEV-DSDEGHGSRFW 687
Cdd:cd16945   84 AQLHGGRITLrNRPDGVLAFLT 105
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
713-846 7.83e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 51.08  E-value: 7.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDN-PVNRVVAEGFLESmGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpsdKALN 791
Cdd:PRK09836   2 KLLIVEDEkKTGEYLTKGLTEA-GFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLR---------SANK 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQS 846
Cdd:PRK09836  72 GMPILLLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAVIIES 126
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
715-822 8.11e-07

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: 48.81  E-value: 8.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 715 LVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpSDKALNPTP 794
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILR-------SDPKTSSIP 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 742417147 795 MVAVSAHvfAEEVESY--LAAGFDGYLPKP 822
Cdd:cd19937   74 IIMLTAK--GEEFDKVlgLELGADDYITKP 101
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
593-694 8.12e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 52.71  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 593 LVGNAIKF-----TEQGEIDIYVSlnpEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEggmnqtGGTGLGLAISRRII 667
Cdd:COG2972  344 LVENAIEHgiepkEGGGTIRISIR---KEGDRLVITVEDNGVGMPEEKLEKLLEELSSKG------EGRGIGLRNVRERL 414
                         90       100       110
                 ....*....|....*....|....*....|
gi 742417147 668 QAM---GGCLEVDSDEGHGSRFWFSIPLEE 694
Cdd:COG2972  415 KLYygeEYGLEIESEPGEGTTVTIRIPLEE 444
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
714-836 1.22e-06

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: 48.07  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDN-PVNRVVAEgFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIERNkpsdkalNP 792
Cdd:cd17623    1 ILLIDDDrELTELLTE-YLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDV---LKELRKT-------SQ 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 742417147 793 TPMVAVSAHvfAEEVESY--LAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17623   70 VPVLMLTAR--GDDIDRIlgLELGADDYLPKPFNPRELVARIRAIL 113
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
714-829 1.93e-06

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: 47.53  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVIL--AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRieRNKPsdkaln 791
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDIEIVgeAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSK--LAKP------ 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742417147 792 ptPMVavsahVFAEEVESYLAAGFD----GYLPKPMEKEALS 829
Cdd:cd17532   73 --PLI-----VFVTAYDEYAVEAFElnavDYLLKPFSEERLA 107
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
893-962 2.30e-06

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: 46.86  E-value: 2.30e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   893 GKEKMLHIIDLFRQTSADVLSQMESSAQNGESRAVKDLAHKLKGSAGSLGLTALMNTCQSIEIASESLEA 962
Cdd:smart00073   2 GLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRS 71
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
713-767 2.39e-06

first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 47.17  E-value: 2.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 742417147 713 KVLVVEDNP-VNRVVAEGFLESMGHEVILAENGLEAEQIIDKH-DFDIALVDINLPD 767
Cdd:cd19921    1 KVLIVEDSKtFSKVLKHLIAQELGLEVDVAETLAEAKALLEEGdDYFAALVDLNLPD 57
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
714-822 2.81e-06

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 46.76  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIhrlKRIERNKPSdkalnpT 793
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELV---QHIQQRLPQ------T 71
                         90       100
                 ....*....|....*....|....*....
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:cd19926   72 PVAVITAYGSLDTAIEALKAGAFDFLTKP 100
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
589-697 3.76e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 50.67  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 589 VLNNLVGNAIKF----TEQGEIDIYVSLnpeDETQVLFEVSDTGIGIAKkdqktlfdaftqaegGMNQTGGTGLGLAISR 664
Cdd:COG3920  403 ILNELVTNALKHaflsGEGGRIRVSWRR---EDGRLRLTVSDNGVGLPE---------------DVDPPARKGLGLRLIR 464
                         90       100       110
                 ....*....|....*....|....*....|...
gi 742417147 665 RIIQAMGGCLEVDSDEghGSRFWFSIPLEESEP 697
Cdd:COG3920  465 ALVRQLGGTLELDRPE--GTRVRITFPLAELAA 495
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
711-934 4.72e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 50.25  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 711 RAKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIERNKPSdkal 790
Cdd:PRK10923   3 RGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLAL---LKQIKQRHPM---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 791 npTPMVAVSAHV-FAEEVESYLAAGFDgYLPKPMEKEALSALIQDMLDGKQlllpqsgeclaqdEIITTSDNDTVSVTTD 869
Cdd:PRK10923  76 --LPVIIMTAHSdLDAAVSAYQQGAFD-YLPKPFDIDEAVALVERAISHYQ-------------EQQQPRNIQVNGPTTD 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742417147 870 LTAEEPAMviinpnviQSDMKILGKekmlhiidlFRQTSADVLSqmessaqNGESRAVKDL-AHKL 934
Cdd:PRK10923 140 IIGEAPAM--------QDVFRIIGR---------LSRSSISVLI-------NGESGTGKELvAHAL 181
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
403-668 6.31e-06

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 49.93  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 403 ARNTAQALKVVAEGE-AQAKReleehkehleelIEQRTSQLKQANRRLNEEVLNhakarkqAEQASRAKSAFLATMSHEI 481
Cdd:PRK09470 194 ARKLKNAADEVAQGNlRQHPE------------LETGPQEFRQAGASFNQMVTA-------LERMMTSQQRLLSDISHEL 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 482 RTPMNGV-LGTARLLIDSGLNPIQKRyaeiINRSGKTLLAILNDVLDYSKIEA-GHLE-----IRSLGFDlhqMVEDT-F 553
Cdd:PRK09470 255 RTPLTRLqLATALLRRRQGESKELER----IETEAQRLDSMINDLLVLSRNQQkNHLEretfkANSLWSE---VLEDAkF 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 554 QLmngkAQEKKLLfsyHIESDVGRYW-KGDVIRINQVLNNLVGNAIKFTEQgEIDIYVSLnpeDETQVLFEVSDTGIGIA 632
Cdd:PRK09470 328 EA----EQMGKSL---TVSAPPGPWPiNGNPNALASALENIVRNALRYSHT-KIEVAFSV---DKDGLTITVDDDGPGVP 396
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 742417147 633 KKDQKTLFDAFTQA-EGGMNQTGGTGLGLAISRRIIQ 668
Cdd:PRK09470 397 EEEREQIFRPFYRVdEARDRESGGTGLGLAIVENAIQ 433
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
713-783 8.90e-06

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: 45.62  E-value: 8.90e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERN 783
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDEN 72
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
101-987 8.95e-06

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


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 49.66  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 101 ELGSESFDSKLLEALENNVQNVIDNLAELGVTVERKLWLTKEIDTRVEEMRLLSEELEQLTRTQVQNTSTIAVANVTHIY 180
Cdd:COG2198    2 ALLLLALLLLLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 181 DLLDANKKAQAFQALDALVEVDLDLTERLHELHLLAFKMLNQIEEARTLTNVDRIQQIQTAFEDNLKIMKRRVLAVEDPT 260
Cdd:COG2198   82 LLLLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 261 RSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQLMQKTLELFSELNGTVNKLVDDSNKTTRIAVEKLTSTLKFAQWSLT 340
Cdd:COG2198  162 LLALLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAEL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 341 VISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAIITARNTAQALKVVAEGEAQA 420
Cdd:COG2198  242 AALLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 421 KRELEEHKEHLEELIEQRTSQLKQANRRLNEEVLNHAKARKQAEQASRAKSAFLATMSHEIRTPMNGVLGTARLLIDSGL 500
Cdd:COG2198  322 LLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLL 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 501 NPIQKRYAEIINRSGKTLLAILNDVLDYSKIEAGHLEIRSLGFDLHQMVEDTFQLMNGKAQEKKLLFSYHIESDVGRYWK 580
Cdd:COG2198  402 LLLSLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLL 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 581 GDVIRINQVLNNLVGNAIKFTEQGEIDIYVSLNPEDETQVLFEVSDTGIGIAKKDQKTLFDAFTQAEGGMNQTGGTGLGL 660
Cdd:COG2198  482 LLLLLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALL 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 661 AISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLEESEPVETVSIASARCKIRAKVLVVEDNPVNRVVAEGFLESMGHEVIL 740
Cdd:COG2198  562 LGLGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLL 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 741 AENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIernkpsDKALNPTPMVAVSAHVFAEEVESYLAAGFDGYLP 820
Cdd:COG2198  642 LLLLLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMML------DDMMAEAARARALAARAAAIAAAAAAAAAAAAAA 715
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 821 KPMEKEALSALIQDMLDGKQLLLPQSGECLAQDEIITTSDNDTVSVTTDLTAEEPAMViinpnviqsdmkilGKEKMLHI 900
Cdd:COG2198  716 AAAAAALLAALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLDLEALRRLGG--------------DPELLREL 781
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 901 IDLFRQTSADVLSQMESSAQNGESRAVKDLAHKLKGSAGSLGLTALMNTCQSIEIA--SESLEAYTMLRADLKGQVSDSV 978
Cdd:COG2198  782 LELFLEELPELLAELRQALAAGDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAarAGDLEEAEELLAELEAELERVL 861

                 ....*....
gi 742417147 979 IALDELMAE 987
Cdd:COG2198  862 AALEALLAE 870
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
714-822 9.60e-06

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: 45.82  E-value: 9.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQII-----------DKHDFDIALVDINLPDCNGADLihrLKRIer 782
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnfNEPKVNMIITDYCMPGMTGYDL---LKKV-- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 742417147 783 nKPSdKALNPTPMVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:cd17581   76 -KES-SALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
713-843 1.08e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 48.61  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLES---MghEVI-LAENGLEAEQIIDKHDFDIALVDINLPDCNGadlIHRLKRIERnkpsdk 788
Cdd:PRK00742   5 RVLVVDDSAFMRRLISEILNSdpdI--EVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDG---LDALEKIMR------ 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 742417147 789 aLNPTPMVAVSA--HVFAEEVESYLAAG-FDgYLPKPMEKEALsaliqDMLDGKQLLL 843
Cdd:PRK00742  74 -LRPTPVVMVSSltERGAEITLRALELGaVD-FVTKPFLGISL-----GMDEYKEELA 124
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
713-836 1.37e-05

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 47.49  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKhDFDIALVDINLPDCNGadlIHRLKRIERNKPsdkalnp 792
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNG---IDTLKELRQTHQ------- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 742417147 793 TPMVAVSAHvfAEEVESYLAA--GFDGYLPKPMEKEALSALIQDML 836
Cdd:PRK10955  72 TPVIMLTAR--GSELDRVLGLelGADDYLPKPFNDRELVARIRAIL 115
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
90-306 1.72e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.81  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147    90 EQLESLLThIKELGSESFDSKllEALENNVQNVIDNLAELGVTVERKLWLTKEIDTRVEEMRLLSEELEQLTRTQVqntS 169
Cdd:TIGR00618  659 RVREHALS-IRVLPKELLASR--QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLG---S 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147   170 TIAVANVTHIYDLLDANK------KAQAFQALDALVEVDLDLtERLHELHLLAFKMLNQIEEARTLTN--VDRIQQIQTA 241
Cdd:TIGR00618  733 DLAAREDALNQSLKELMHqartvlKARTEAHFNNNEEVTAAL-QTGAELSHLAAEIQFFNRLREEDTHllKTLEAEIGQE 811
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742417147   242 FEDNLKImkRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQY-ENNEQSQQLMQKTLELFSEL 306
Cdd:TIGR00618  812 IPSDEDI--LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYeECSKQLAQLTQEQAKIIQLS 875
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
473-691 2.98e-05

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 47.27  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 473 FLATMSHEIRTPMNGVLGTARLLIDSGLNPIQKRYAEIINrsgktLLAILNDVLDYSKIE----AGHLEIRSLGFDLHQM 548
Cdd:PRK10755 140 FTADVAHELRTPLAGIRLHLELLEKQHHIDVAPLIARLDQ-----MMHTVEQLLQLARAGqsfsSGHYQTVKLLEDVILP 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 549 VEDTFQLMNGKAQEKKLLfsyhIESDVGRYWKGDVIRINQVLNNLVGNAIKFTEQGEiDIYVSLNpEDETQVLFEVSDTG 628
Cdd:PRK10755 215 SQDELSEMLEQRQQTLLL----PESAADITVQGDATLLRLLLRNLVENAHRYSPEGS-TITIKLS-QEDGGAVLAVEDEG 288
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742417147 629 IGIAKKDQKTLFDAFTQaeggMNQT-GGTGLGLAISRRIIQAMGGCLEV-DSDEGHGSRFWFSIP 691
Cdd:PRK10755 289 PGIDESKCGELSKAFVR----MDSRyGGIGLGLSIVSRITQLHHGQFFLqNRQERSGTRAWVWLP 349
PRK13435 PRK13435
response regulator; Provisional
713-777 4.35e-05

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 44.66  E-value: 4.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVI-LAENGLEAEQIIDKHDFDIALVDINLPD-CNGADLIHRL 777
Cdd:PRK13435   7 KVLIVEDEALIALELEKLVEEAGHEVVgIAMSSEQAIALGRRRQPDVALVDVHLADgPTGVEVARRL 73
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
714-843 4.54e-05

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 44.02  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIernkpsDKALnpt 793
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIREL------DPDL--- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742417147 794 PMVAVSAH--VfAEEVESYLAAGFDgYLPKPMEKEALSALIQDMLDGKQLLL 843
Cdd:cd17549   72 PVILITGHgdV-PMAVEAMRAGAYD-FLEKPFDPERLLDVVRRALEKRRLVL 121
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
714-833 4.90e-05

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: 43.80  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNR--VVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpsDKALN 791
Cdd:cd19930    1 VLIAEDQEMVRgaLAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELR--------EELPD 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742417147 792 pTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQ 833
Cdd:cd19930   73 -TKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIR 113
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
606-685 6.10e-05

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 44.64  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 606 IDIYVSLNPEDetqVLFEVSDTGIGIAKKDQKTLFD-AFTQAE-------------GGMNQTGGTGLGLAISRRIIQAMG 671
Cdd:cd16929   73 IKVTVAKGDED---LTIKISDRGGGIPREDLARLFSyMYSTAPqpslddfsdlisgTQPSPLAGFGYGLPMSRLYAEYFG 149
                         90
                 ....*....|....
gi 742417147 672 GCLEVDSDEGHGSR 685
Cdd:cd16929  150 GDLDLQSMEGYGTD 163
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
714-822 6.83e-05

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 42.88  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIernKPSdkalnpT 793
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKA---RPD------L 71
                         90       100       110
                 ....*....|....*....|....*....|
gi 742417147 794 PMVAVSA-HVFAEEVESYLAAGFDgYLPKP 822
Cdd:cd19928   72 PIIVMSAqNTLMTAVKAAERGAFE-YLPKP 100
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
713-869 7.00e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 45.23  E-value: 7.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAE--NGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRiernkpsDKAL 790
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELDPGFEVVAEagDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRR-------DGVT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742417147 791 NPTPMVAVSAHvfAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQSGECLAQDEIITTSDnDTVSVTTD 869
Cdd:PRK10403  81 AQIIILTVSDA--SSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAKGSKVFSERVNQYLREREMFGAEE-DPFSVLTE 156
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
714-822 1.03e-04

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: 42.39  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIID--KHDFDIALVDINLPDCNGADLihrLKRIERNkpsdKALN 791
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEdeQNEIDLILTEVDLPVSSGFKL---LSYIMRH----KICK 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKP 822
Cdd:cd17582   74 NIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
PRK10643 PRK10643
two-component system response regulator PmrA;
713-836 1.55e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 44.26  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNpvnRVVAEGFLESMGHE---VILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIERNKpsdka 789
Cdd:PRK10643   2 KILIVEDD---TLLLQGLILALQTEgyaCDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHL---LRRWRQKK----- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 742417147 790 lNPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:PRK10643  71 -YTLPVLILTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALI 116
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
714-828 2.39e-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: 41.56  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAE--NGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRiernkpsDKALN 791
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEasSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALRE-------EGVSA 73
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 742417147 792 PTPMVAVSAHvfAEEVESYLAAGFDGYLPKPMEKEAL 828
Cdd:cd19931   74 RIVILTVSDA--EDDVVTALRAGADGYLLKDMEPEDL 108
PRK15369 PRK15369
two component system response regulator;
713-863 2.55e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 43.53  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPV------NRVVAEGFLESMGHevilAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKrieRNKPs 786
Cdd:PRK15369   5 KILLVDDHELiingikNMLAPYPRYKIVGQ----VDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLH---QRWP- 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742417147 787 dkALNptpMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDMLDGKQLLLPQsgecLAQDEIITTSDNDT 863
Cdd:PRK15369  77 --AMN---ILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKRYIDPA----LNREAILALLNADD 144
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
596-695 3.54e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 43.45  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 596 NAIKFTEQGEIDIYVSlnpEDETQVLFEVSDTGIGIAkkdqktlfdaftqaeggMNQTGGTGLGLAISRRIIQAMGGCLE 675
Cdd:COG4585  173 NALKHAGATRVTVTLE---VDDGELTLTVRDDGVGFD-----------------PEAAPGGGLGLRGMRERAEALGGTLT 232
                         90       100
                 ....*....|....*....|
gi 742417147 676 VDSDEGHGSRFWFSIPLEES 695
Cdd:COG4585  233 IGSAPGGGTRVRATLPLAAA 252
orf27 CHL00148
Ycf27; Reviewed
713-836 4.07e-04

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 43.17  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernKPSDkalnp 792
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR-----KESD----- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 742417147 793 TPMVAVSAhvfAEEVESYLAA---GFDGYLPKPMEKEALSALIQDML 836
Cdd:CHL00148  78 VPIIMLTA---LGDVSDRITGlelGADDYVVKPFSPKELEARIRSVL 121
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
713-836 4.33e-04

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: 40.82  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNP-VNRVVAEgFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNkpsdkaln 791
Cdd:cd17622    2 RILLVEDDPkLARLIAD-FLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG-------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 792 ptPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17622   73 --PILLLTALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
157-469 4.52e-04

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 43.86  E-value: 4.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 157 LEQLTRTQVQNTSTIAVANVTHIYDLLDANKKAQAFQALDALVEVDLDLTERLHELHLLAFKMLNQIEEARTLTNVDRIQ 236
Cdd:COG0840    4 LLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 237 QIQTAFEDNLKIMKRRVLAVEDPTRSEQMSQLLTELGKRQVVFTILLQQYENNEQSQQLMQKTLELFSELngtVNKLVDD 316
Cdd:COG0840   84 LLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALL---AAAAAAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 317 SNKTTRIAVEKLTSTLKFAQWSLTVISIIGLIIVVLILWRVVYVSVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHM 396
Cdd:COG0840  161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 397 GQAIITA----RNTAQALKVVAEGEAQAKRELEEHKEHLEELIEQRTSQLKQANRRLNE------EVLNHAK-ARKQAEQ 465
Cdd:COG0840  241 ADAFNRMienlRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEElsatvqEVAENAQqAAELAEE 320

                 ....
gi 742417147 466 ASRA 469
Cdd:COG0840  321 ASEL 324
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
549-686 4.86e-04

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: 41.08  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 549 VEDTFQLMNGKAQEKKLLFSYHIESDVgrYWKGDVIRINQVLNNLVGNAIKFTEqGEIDIYVSLNPEdetQVLFEVSDTG 628
Cdd:cd16954    3 LDSLCSALNKVYQRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCL-EFVEVTARQTDG---GLHLIVDDDG 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 742417147 629 IGIAKKDQKTLFDAFTQAEggmNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRF 686
Cdd:cd16954   77 PGVPESQRSKIFQRGQRLD---EQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
714-765 5.41e-04

phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response regulators; This subfamily is composed of stand-alone response regulators (RRs) containing the PFxFATG[G/Y] motif; RRs with such a motif are also called ''FAT GUY'' response regulators. Included in this subfamily are Sphingomonas melonis SdrG, Sinorhizobium meliloti Sma0114, and Erythrobacter litoralis EL_LovR. SdrG is involved in the control of the general stress response. Sma0114 is part of the Sma0113/Sma0114 two-component system (TCS) that is involved in catabolite repression and polyhydroxy butyrate synthesis. EL_LovR is involved in a light-regulated TCS. PFxFATG[G/Y] RRs are typically associated with histidine-tryptophan-glutamate (HWE) histidine kinases that constitute a subclass of the larger histidine kinase superfamily characterized by an altered ATP binding site, which lacks the F-box that is normally an integral component of the ATP lid. The PFxFATG[G/Y] motif is involved in conformational changes after phosphorylation that results in the activation of the RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 40.53  E-value: 5.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGH-EVILAENGLEAEQIIDKHDFDIALVDINL 765
Cdd:cd17586    1 VLVLEDEPLIAMNLEDALEDLGGkEVVTAATCAEALRSLADGPIDIAILDVNL 53
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
714-822 8.20e-04

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: 39.66  E-value: 8.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIErnkpsdkALNPT 793
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSS-------ALKDT 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 742417147 794 PMVAVSAHvfAEEVESYLA--AGFDGYLPKP 822
Cdd:cd17602   74 PIIMLTGK--DGLVDRIRAkmAGASGYLTKP 102
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
713-833 1.15e-03

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: 39.56  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLihrLKRIERNKPSdkalnp 792
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLAL---LAQIKQRHPD------ 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742417147 793 TPMVAVSAHVFAEE-VESYLAAGFDgYLPKPMEKEALSALIQ 833
Cdd:cd19919   73 LPVIIMTAHSDLDSaVSAYQGGAFE-YLPKPFDIDEAVALVE 113
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
714-837 1.39e-03

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 40.85  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERnkpsdkalnPT 793
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGS---------PL 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 742417147 794 PMVAVSAH------VFAeevesyLAAG-FDgYLPKPMEKEALSALIQDMLD 837
Cdd:COG4566   73 PVIFLTGHgdvpmaVRA------MKAGaVD-FLEKPFDDQALLDAVRRALA 116
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
581-672 1.54e-03

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: 39.18  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 581 GDVIRINQVLNNLVGNAIKFT--EQGEIDIYVSLNPE---DETQVL---FEVSDTGIGIAKKdqktLFDAFTQAEGGMNQ 652
Cdd:cd16932    2 GDQIRLQQVLADFLLNAVRFTpsPGGWVEIKVSPTKKqigDGVHVIhleFRITHPGQGLPEE----LVQEMFEENQWTTQ 77
                         90       100
                 ....*....|....*....|
gi 742417147 653 tggTGLGLAISRRIIQAMGG 672
Cdd:cd16932   78 ---EGLGLSISRKLVKLMNG 94
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
596-691 1.56e-03

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 38.69  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 596 NAIKFTEQGEIDIYVSlnpEDETQVLFEVSDTGIGIAKKDQKtlfdaftqaeggmnqtGGTGLGLAISRRIIQAMGGCLE 675
Cdd:cd16917   11 NALKHAGASRVRVTLS---YTADELTLTVVDDGVGFDGPAPP----------------GGGGFGLLGMRERAELLGGTLT 71
                         90
                 ....*....|....*.
gi 742417147 676 VDSDEGHGSRFWFSIP 691
Cdd:cd16917   72 IGSRPGGGTRVTARLP 87
PRK09191 PRK09191
two-component response regulator; Provisional
692-767 2.10e-03

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 40.99  E-value: 2.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742417147 692 LEESEPVETVSIASA--RCKIRAKVLVVEDNPVNRVVAEGFLESMGHEVI-LAENGLEAEQIIDKHDFDIALVDINLPD 767
Cdd:PRK09191 116 VDPAEAEALLDDARAeiARQVATRVLIIEDEPIIAMDLEQLVESLGHRVTgIARTRAEAVALAKKTRPGLILADIQLAD 194
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
715-779 2.20e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 40.65  E-value: 2.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742417147 715 LVVEDNPVNRVVAEGFLESMGHEVILA-ENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKR 779
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILAElTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRK 69
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
714-822 2.50e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 40.82  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIernkpSDkalnpT 793
Cdd:PRK10710  13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRF-----SD-----I 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 742417147 794 PMVAVSAHVfaEEVESYLA--AGFDGYLPKP 822
Cdd:PRK10710  83 PIVMVTAKI--EEIDRLLGleIGADDYICKP 111
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
714-822 2.53e-03

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: 38.33  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLkriernkpsdKALNPT 793
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQL----------RARSNV 70
                         90       100       110
                 ....*....|....*....|....*....|.
gi 742417147 794 PMVAVSAHvfAEEVESY--LAAGFDGYLPKP 822
Cdd:cd17621   71 PVIMVTAK--DSEIDKVvgLELGADDYVTKP 99
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
713-836 2.79e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 40.47  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRiernkpsDKALNP 792
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKR-------ESMTRD 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742417147 793 TPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:PRK10161  77 IPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
712-836 2.95e-03

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: 38.60  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 AKVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKriernkpsdkALN 791
Cdd:cd17626    1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR----------AES 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17626   71 GVPIVMLTAKSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
714-836 3.96e-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: 38.03  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGadlIHRLKRIernkpsdKALNPT 793
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDG---FYWCREI-------RQISNV 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 742417147 794 PMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd18159   71 PIIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
714-830 3.99e-03

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: 38.45  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNP--VNRVVAEgflESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERNKpsdkaln 791
Cdd:cd17539    1 VLLVDDRPssAERIAAM---LSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTR------- 70
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 742417147 792 PTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSA 830
Cdd:cd17539   71 QLPILAVADPGDRGRLIRALEIGVNDYLVRPIDPNELLA 109
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
714-872 4.49e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 39.79  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMGHEVILAEN---GLeAEQIIDKHDFDIalVDINLPDCNGADLIHRLKRiernkpsdkaL 790
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETlqrGL-LEAATRKPDLII--LDLGLPDGDGIEFIRDLRQ----------W 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 791 NPTPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEkealsalIQDMLDGKQLLLPQSGECLAQDEIITTSDndtvsVTTDL 870
Cdd:PRK10529  71 SAIPVIVLSARSEESDKIAALDAGADDYLSKPFG-------IGELQARLRVALRRHSATPAPDPLVKFSD-----VTVDL 138

                 ..
gi 742417147 871 TA 872
Cdd:PRK10529 139 AA 140
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
363-400 4.63e-03

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: 35.88  E-value: 4.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 742417147 363 IKRLgeySSALLSVAQGNLAVELEVKGKDELAHMGQAI 400
Cdd:cd06225    4 LRRL---TEAARRIAEGDLDVRVPVRSKDEIGELARAF 38
PRK10337 PRK10337
sensor protein QseC; Provisional
544-671 5.02e-03

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 40.40  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 544 DLHQMVEDTFQLMNGKAQEKKLLFSYHIESDvgrywkgDVIRINQVL------NNLVGNAIKFTEQGEIdIYVSLNPEde 617
Cdd:PRK10337 312 PLEDLLQSAVMDIYHTAQQAGIDVRLTLNAH-------PVIRTGQPLllsllvRNLLDNAIRYSPQGSV-VDVTLNAR-- 381
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 742417147 618 tqvLFEVSDTGIGIAKKDQKTLFDAFTQAEGgmNQTGGTGLGLAISRRIIQAMG 671
Cdd:PRK10337 382 ---NFTVRDNGPGVTPEALARIGERFYRPPG--QEATGSGLGLSIVRRIAKLHG 430
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
712-822 5.52e-03

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 39.56  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 712 AKVLVVEDNPVnrvVAEGF---LESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIernkPSDk 788
Cdd:PRK11083   4 PTILLVEDEQA---IADTLvyaLQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAF----HPA- 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 742417147 789 alnpTPMVAVSAHvfAEEVESY--LAAGFDGYLPKP 822
Cdd:PRK11083  76 ----LPVIFLTAR--SDEVDRLvgLEIGADDYVAKP 105
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
714-829 5.86e-03

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 37.63  E-value: 5.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDNPVNRVVAEGFLESMG-HEVILAENGLEAEQIIDKHDFDIALVDINLPD-CNGADLIHRLKRiernkpsDKALN 791
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGvTRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRH-------KKLIS 73
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 742417147 792 PTPM-VAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALS 829
Cdd:cd17589   74 PSTVfIMVTGESSRAMVLSALELEPDDYLLKPFTVSELR 112
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
655-691 5.93e-03

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 38.72  E-value: 5.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 742417147 655 GTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIP 691
Cdd:cd16916  142 GRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
655-706 6.36e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 40.17  E-value: 6.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742417147 655 GTGLGLAISRRIIQAMGGCLEVDSDEGHGSRFWFSIPLeesepveTVSIASA 706
Cdd:COG0643  381 GRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL-------TLAIIDG 425
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
714-836 7.41e-03

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: 37.40  E-value: 7.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 714 VLVVEDN-PVNRVVaEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLKRIERnkpsdkalnp 792
Cdd:cd17614    1 ILVVDDEkPISDIL-KFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSN---------- 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 742417147 793 TPMVAVSAHvfAEEVESYLA--AGFDGYLPKPMEKEALSALIQDML 836
Cdd:cd17614   70 VPIIMLTAK--DSEVDKVLGleLGADDYVTKPFSNRELLARVKANL 113
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
581-686 7.44e-03

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: 37.82  E-value: 7.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 581 GDVIRINQVLNNLVGNAIKFTEQ-GEIDIYVSL------------------NPEDETQVLFEVSDTGIGIAKKDQKTLFD 641
Cdd:cd16938    7 GDERRVFQVLLHMLGNLLKMRNGgGNITFRVFLeggsedrsdrdwgpwrpsMSDESVEIRFEVEINDSGSPSIESASMRN 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742417147 642 afTQAEGGMNQTGGTGLGLAISRRIIQAMGGCLEVDSDEGHGSRF 686
Cdd:cd16938   87 --SLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTM 129
PRK11517 PRK11517
DNA-binding response regulator HprR;
713-836 8.80e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 38.73  E-value: 8.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742417147 713 KVLVVEDNPVNRVVAEGFLESMGHEVILAENGLEAEQIIDKHDFDIALVDINLPDCNGADLIHRLkriernkpsdKALNP 792
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTL----------RTAKQ 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742417147 793 TPMVAVSAHVFAEEVESYLAAGFDGYLPKPMEKEALSALIQDML 836
Cdd:PRK11517  72 TPVICLTARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQL 115
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
361-400 8.94e-03

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 35.30  E-value: 8.94e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 742417147   361 SVIKRLGEYSSALLSVAQGNLAVELEVKGKDELAHMGQAI 400
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAF 41
 
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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