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Conserved domains on  [gi|1986385785|ref|WP_203760054|]
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SpoIIE family protein phosphatase [Paractinoplanes deccanensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
294-516 2.52e-71

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


:

Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 237.88  E-value: 2.52e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRL-PALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATD 372
Cdd:COG2205     13 ERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLsPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLSLELEPVD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  373 LADYTWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDT 451
Cdd:COG2205     93 LAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSpPGGTITISARREGDGVRISVSDN 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  452 GVGIPADQQPLLFDRFHRVTGawARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG2205    173 GPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLP 235
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
623-1042 2.83e-64

Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


:

Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 224.94  E-value: 2.83e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  623 PRLDGFGLIAALRADERTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQIISRLRGL 702
Cdd:COG2208      6 LRAALLLLLELLLAAALLLLLLLLLAALLALELLALLLALLLLLLALLLLLLLLLALRLALLLLALLLALLLLAALLLLA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  703 VDTAAALNTVRTTAEVLDVAAQHVRAMTTAGRVVVSVPGSRAEVDGGAAPGTQPDSVLPLPDTSGATVGELRVWSPPDGA 782
Cdd:COG2208     86 LLALALLLALLAALLLVLLLLLLLLLGLLAVALLLLLALLLLLALLLLALLLGLLLLLLLLLLLAALLLALALALALALL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  783 LEPAVLIQLARLIGLRLENARL--------YEAEHRIASTLQHSLLPQSLPRMPGTIVASRYLAGSneaEVGGDWYDVIA 854
Cdd:COG2208    166 LLLALAAALALLAALLLENARLeeeeknrrLERELELARRIQRSLLPPRLPEVPGLDIAARYRPAD---EVGGDFYDVFP 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  855 APDEQLVLVIGDVVGKGVQAAAGMGQLRNALRAYILEGFDCGEALTRLNR-LVDNLGRRQFATVVCVRYDPVTRGLHYSS 933
Cdd:COG2208    243 LDDGRLAVVIGDVSGHGVPAALLMAMLRSALRALAREGLDPAEVLERLNRaLYEDLGGGRFVTAFLGVLDPETGRLTYAN 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  934 AGHPPPVLVPPGdlGSFLYTSALGPPIGALADAVYPTLETEMPAGSRLLLYTDGLVE-----DRRIGIDsGLADLTADAA 1008
Cdd:COG2208    323 AGHPPPLLLRAD--GEVEELDGGGLPLGLLPDAEYEEHEIPLEPGDRLLLYTDGLTEarngdGELFGEE-RLLELLAENA 399
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1986385785 1009 K--PAEHVEDLLDDLLAKAVRRTRRDDIALLALQVT 1042
Cdd:COG2208    400 DlpAEELLDALLEALEEFRGGGPQEDDITLLALRRR 435
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
67-516 7.92e-36

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


:

Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 143.39  E-value: 7.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   67 LGRPGSEMWAEAWTVLQPLFDGVVTGDEAFWAADYPFRLERHGFLEETYFDISYDPIRLDSGEVGGLFCIVSDTTGRVLG 146
Cdd:COG4251     52 LLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  147 ERRVRTLSALGSRLADSPDQAALAAEVVAVLGENAADAPFAELVLDDAVGPHPVVRQVIESGQPARVALTEIVERPPADA 226
Cdd:COG4251    132 LALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLL 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  227 AAEALVLPITVGTATAGALVVGLSRYLELGGGYRDFLELAAAQISRAVGNLRAYEQERARAAELAALDQAKTNFFSNVSH 306
Cdd:COG4251    212 LLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASH 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  307 EFRTPL-------TLILGPLEDVLDDPRLPALQRerllpMQRNGLRLLKLVNTVLDFSRLesGRLRAEYRATDLADYTWR 379
Cdd:COG4251    292 DLREPLrkisgfsQLLEEDYGDKLDEEGREYLER-----IRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEE 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  380 LASTFRSAAERAGLELVVETPPlsaPVYVDREMWEKIVLNLLSNAVKFTAAGRV-VVRIGA--DAGDAVLSVEDTGVGIP 456
Cdd:COG4251    365 VLEDLEPRIEERGAEIEVGPLP---TVRGDPTLLRQVFQNLISNAIKYSRPGEPpRIEIGAerEGGEWVFSVRDNGIGID 441
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  457 ADQQPLLFDRFHRVTGAwaRSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG4251    442 PEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
REC super family cl19078
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
571-673 3.50e-29

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.


The actual alignment was detected with superfamily member cd17538:

Pssm-ID: 473134 [Multi-domain]  Cd Length: 104  Bit Score: 112.21  E-value: 3.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPF 673
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
1049-1165 4.16e-24

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


:

Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 98.83  E-value: 4.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1049 LRLPAEPGRLSVLRRRLEDFLTGNGVPDDDVFDLTVAVSEAAANAIEH--PVDPvEPVITVEASLVDGAVVITVRDSGRW 1126
Cdd:COG2172      2 LSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHayGGDP-DGPVEVELELDPDGLEIEVRDEGPG 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1986385785 1127 RETAA-------EGFRGRGLALIGALS-ELSVSRSDSGTSVTLRRPL 1165
Cdd:COG2172     81 FDPEDlpdpystLAEGGRGLFLIRRLMdEVEYESDPGGTTVRLVKRL 127
 
Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
294-516 2.52e-71

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 237.88  E-value: 2.52e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRL-PALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATD 372
Cdd:COG2205     13 ERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLsPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLSLELEPVD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  373 LADYTWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDT 451
Cdd:COG2205     93 LAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSpPGGTITISARREGDGVRISVSDN 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  452 GVGIPADQQPLLFDRFHRVTGawARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG2205    173 GPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLP 235
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
623-1042 2.83e-64

Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 224.94  E-value: 2.83e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  623 PRLDGFGLIAALRADERTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQIISRLRGL 702
Cdd:COG2208      6 LRAALLLLLELLLAAALLLLLLLLLAALLALELLALLLALLLLLLALLLLLLLLLALRLALLLLALLLALLLLAALLLLA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  703 VDTAAALNTVRTTAEVLDVAAQHVRAMTTAGRVVVSVPGSRAEVDGGAAPGTQPDSVLPLPDTSGATVGELRVWSPPDGA 782
Cdd:COG2208     86 LLALALLLALLAALLLVLLLLLLLLLGLLAVALLLLLALLLLLALLLLALLLGLLLLLLLLLLLAALLLALALALALALL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  783 LEPAVLIQLARLIGLRLENARL--------YEAEHRIASTLQHSLLPQSLPRMPGTIVASRYLAGSneaEVGGDWYDVIA 854
Cdd:COG2208    166 LLLALAAALALLAALLLENARLeeeeknrrLERELELARRIQRSLLPPRLPEVPGLDIAARYRPAD---EVGGDFYDVFP 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  855 APDEQLVLVIGDVVGKGVQAAAGMGQLRNALRAYILEGFDCGEALTRLNR-LVDNLGRRQFATVVCVRYDPVTRGLHYSS 933
Cdd:COG2208    243 LDDGRLAVVIGDVSGHGVPAALLMAMLRSALRALAREGLDPAEVLERLNRaLYEDLGGGRFVTAFLGVLDPETGRLTYAN 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  934 AGHPPPVLVPPGdlGSFLYTSALGPPIGALADAVYPTLETEMPAGSRLLLYTDGLVE-----DRRIGIDsGLADLTADAA 1008
Cdd:COG2208    323 AGHPPPLLLRAD--GEVEELDGGGLPLGLLPDAEYEEHEIPLEPGDRLLLYTDGLTEarngdGELFGEE-RLLELLAENA 399
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1986385785 1009 K--PAEHVEDLLDDLLAKAVRRTRRDDIALLALQVT 1042
Cdd:COG2208    400 DlpAEELLDALLEALEEFRGGGPQEDDITLLALRRR 435
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
295-683 6.04e-54

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: 205.01  E-value: 6.04e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  295 QAKTNFFSNVSHEFRTPLTLILGPLEdVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLA 374
Cdd:TIGR02956  462 RAKSAFLATMSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLN 540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  375 DYTWRLASTFRSAAERAGLELVVETPP-LSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIG-ADAGDAVLSVEDTG 452
Cdd:TIGR02956  541 ALLDDVHHLMVSRAQLKGIQLRLNIPEqLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSlNDDSSLLFEVEDTG 620
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  453 VGIPADQQPLLFDRFHRVTGawARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFgtahlpadrvlpdgE 532
Cdd:TIGR02956  621 CGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL--------------T 684
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  533 RIAPEFDArpyaeeaehwwTGDEPVTLPlpppagrrPGRILLADDN-ADLRDHVARLLRPHWDVTTAVDGQAALELTRRG 611
Cdd:TIGR02956  685 RGKPAEDS-----------ATLTVIDLP--------PQRVLLVEDNeVNQMVAQGFLTRLGHKVTLAESGQSALECFHQH 745
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  612 RFDLVLTDVMMPRLDGFGLIAALRADERTRD-VPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:TIGR02956  746 AFDLALLDINLPDGDGVTLLQQLRAIYGAKNeVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIA 818
PRK15347 PRK15347
two component system sensor kinase;
297-678 1.80e-50

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 193.70  E-value: 1.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  297 KTNFFSNVSHEFRTPLTLILGPLEdVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATD---L 373
Cdd:PRK15347   398 KSEHLTTISHEIRTPLNGVLGALE-LLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETAllpL 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  374 ADYTwrlASTFRSAAERAGLEL---VVETPPLSApvYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIGADAGDAVLSVED 450
Cdd:PRK15347   477 LDQA---MLTIQGPAQSKSLTLrtfVGAHVPLYL--HLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVED 551
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  451 TGVGIPADQQPLLFDRFHRVTGawarsHE-GTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFGTAHLPAD---- 525
Cdd:PRK15347   552 TGCGIDIQQQQQIFTPFYQADT-----HSqGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEPlkge 626
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  526 --------RVL-----------PDGERIAPE---FDARPYAE-EAEHWWTGDEP-VTLPLPPpagrRPGRILLADDNADL 581
Cdd:PRK15347   627 lsaplalhRQLsawgitcqpghQNPALLDPElayLPGRLYDLlQQIIQGAPNEPvINLPLQP----WQLQILLVDDVETN 702
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  582 RDHVARLLRP--HwDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADE--RTRDVPIVVLSARAGEESA 657
Cdd:PRK15347   703 RDIIGMMLVElgQ-QVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPnnLDPDCMIVALTANAAPEEI 781
                          410       420
                   ....*....|....*....|.
gi 1986385785  658 VEGLGAGADDYLVKPFSARDL 678
Cdd:PRK15347   782 HRCKKAGMNHYLTKPVTLAQL 802
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
856-1041 2.03e-49

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 462119 [Multi-domain]  Cd Length: 192  Bit Score: 173.60  E-value: 2.03e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  856 PDEQLVLVIGDVVGKGVQAAAGMGQLRNALRAYILEGFDCGEALTRLNRLV-DNLGRRQFATVVCVRYDPVTRGLHYSSA 934
Cdd:pfam07228    1 PDGRLALVIGDVMGHGLPAALLMGLLRTALRALAAEGLDPAEVLKRLNRLLqRNLEEDMFATAVLAVYDPETGTLEYANA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  935 GHPPPVLVPPGDlGSFLYTSALGPPIGALADAVYPTLETEMPAGSRLLLYTDGLVE--DRRIGIDSGLADLTADAAKPAE 1012
Cdd:pfam07228   81 GHPPPLLLRPDG-GVVELLESPGLPLGILPDAPYEVVELELEPGDTLLLYTDGLTEarDPDGELFGLERLLALLAERHGL 159
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1986385785 1013 HVEDLLDDLLAKAVRRT---RRDDIALLALQV 1041
Cdd:pfam07228  160 PPEELLDALLEALLRLGggeLEDDITLLVLRV 191
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
416-517 3.99e-39

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: 141.09  E-value: 3.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSNAVKFTAAGRVVVRI---GADAGDAVL--SVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRE 490
Cdd:cd16922      4 ILLNLLGNAIKFTEEGEVTLRVsleEEEEDGVQLrfSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISKK 83
                           90       100
                   ....*....|....*....|....*..
gi 1986385785  491 LAELHGGSASAASEPGRGSVFTVRVPF 517
Cdd:cd16922     84 LVELMGGDISVESEPGQGSTFTFTLPL 110
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
828-1023 3.26e-36

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 135.94  E-value: 3.26e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   828 PGTIVASRYLAGSneaEVGGDWYDVIAAPDEQLVLVIGDVVGKGVQAAAGMGQLRNALRAYILEGFDCGEALTRLNRLVD 907
Cdd:smart00331    2 DGGLIAQYYEDAT---QVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   908 NLG-RRQFATVVCVRYDPVTRGLHYSSAGHPPPVLVPPGDlGSFLYTSALGPPIGALADAVYPTLETEMPAGSRLLLYTD 986
Cdd:smart00331   79 ENGeDGMFATLFLALYDFAGGTLSYANAGHSPPYLLRADG-GLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTD 157
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1986385785   987 GLVEDRRIGIDSG-LADLTADAakPAEHVEDLLDDLLA 1023
Cdd:smart00331  158 GLTEARNPERLEElLEELLGSP--PAEIAQRILEELLE 193
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
67-516 7.92e-36

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 143.39  E-value: 7.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   67 LGRPGSEMWAEAWTVLQPLFDGVVTGDEAFWAADYPFRLERHGFLEETYFDISYDPIRLDSGEVGGLFCIVSDTTGRVLG 146
Cdd:COG4251     52 LLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  147 ERRVRTLSALGSRLADSPDQAALAAEVVAVLGENAADAPFAELVLDDAVGPHPVVRQVIESGQPARVALTEIVERPPADA 226
Cdd:COG4251    132 LALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLL 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  227 AAEALVLPITVGTATAGALVVGLSRYLELGGGYRDFLELAAAQISRAVGNLRAYEQERARAAELAALDQAKTNFFSNVSH 306
Cdd:COG4251    212 LLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASH 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  307 EFRTPL-------TLILGPLEDVLDDPRLPALQRerllpMQRNGLRLLKLVNTVLDFSRLesGRLRAEYRATDLADYTWR 379
Cdd:COG4251    292 DLREPLrkisgfsQLLEEDYGDKLDEEGREYLER-----IRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEE 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  380 LASTFRSAAERAGLELVVETPPlsaPVYVDREMWEKIVLNLLSNAVKFTAAGRV-VVRIGA--DAGDAVLSVEDTGVGIP 456
Cdd:COG4251    365 VLEDLEPRIEERGAEIEVGPLP---TVRGDPTLLRQVFQNLISNAIKYSRPGEPpRIEIGAerEGGEWVFSVRDNGIGID 441
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  457 ADQQPLLFDRFHRVTGAwaRSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG4251    442 PEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
409-517 3.12e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 126.99  E-value: 3.12e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   409 DREMWEKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRvTGAWARSHEGTGIGLAL 487
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFR-TDKRSRKIGGTGLGLSI 80
                            90       100       110
                    ....*....|....*....|....*....|
gi 1986385785   488 VRELAELHGGSASAASEPGRGSVFTVRVPF 517
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITLPL 110
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
294-517 2.43e-33

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 137.19  E-value: 2.43e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEdVLDDprlPALQRERLLP-----MQRNGLRLLKLVNTVLDFSRLESGRLRAEY 368
Cdd:NF033092   369 EQERREFVANVSHELRTPLTTMRSYLE-ALAD---GAWKDPELAPrflgvTQNETERMIRLVNDLLQLSRMDSKDYKLNK 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  369 RATDLADYTWRLASTFRSAAERAGLELVVETPPLSAPVYVDRemwEKI--VL-NLLSNAVKFT-AAGRVVVRIGADAGDA 444
Cdd:NF033092   445 EWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDT---DKItqVLdNIISNAIKYSpEGGTITFRLLETHNRI 521
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  445 VLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPF 517
Cdd:NF033092   522 IISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLPY 594
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
573-684 1.34e-31

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: 119.63  E-value: 1.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  573 LLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrDVPIVVLSAR 651
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGI--ETPVLLLTAL 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1986385785  652 AGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:cd17625     79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIRA 111
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
300-516 5.40e-31

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 128.99  E-value: 5.40e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  300 FFSNVSHEFRTPLTLILGPlEDVLDDPRL---PALQRERLLpMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLADY 376
Cdd:NF040691   274 FVSDVSHELRTPLTTIRMA-ADVIHDSRDdfdPATARSAEL-LHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPL 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  377 TWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIGADaGDAV-LSVEDTGVGI 455
Cdd:NF040691   352 VRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQD-DTAVaVTVRDHGVGL 430
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1986385785  456 PADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:NF040691   431 KPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLP 491
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
416-517 1.88e-29

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: 113.23  E-value: 1.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSNAVKFTA-AGRVVVRIGADaGDAVLSVEDTGVGIPADQQPLLFDRFHRVTgawARSHEGTGIGLALVRELAEL 494
Cdd:pfam02518    9 VLSNLLDNALKHAAkAGEITVTLSEG-GELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGLGLSIVRKLVEL 84
                           90       100
                   ....*....|....*....|...
gi 1986385785  495 HGGSASAASEPGRGSVFTVRVPF 517
Cdd:pfam02518   85 LGGTITVESEPGGGTTVTLTLPL 107
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
571-673 3.50e-29

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: 112.21  E-value: 3.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPF 673
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
294-516 1.60e-27

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 117.62  E-value: 1.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRlpALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDL 373
Cdd:NF012163   237 EQMRRDFMADISHELRTPLAVLRAELEAIQDGIR--KFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  374 ADYTWRLASTFRSAAERAGLELVVETPPlSAPVYVDREMWEKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDTG 452
Cdd:NF012163   315 VPLLEVEGGAFRERFASAGLELEVSLPD-SSLVFGDRDRLMQLFNNLLENSLRYTdSGGSLHISASQRPKEVTLTVADSA 393
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1986385785  453 VGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:NF012163   394 PGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
571-672 2.44e-27

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: 107.17  E-value: 2.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVV 647
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILEWEAGfevVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIR--ELDPDTKIII 78
                           90       100
                   ....*....|....*....|....*
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKP 672
Cdd:COG4753     79 LSGYSDFEYAQEAIKLGADDYLLKP 103
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
571-686 2.28e-26

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 108.57  E-value: 2.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLR-PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:TIGR02154    4 RILVVEDEPAIRELIAYNLEkAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPIIMLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:TIGR02154   84 ARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVL 120
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
1049-1165 4.16e-24

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 98.83  E-value: 4.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1049 LRLPAEPGRLSVLRRRLEDFLTGNGVPDDDVFDLTVAVSEAAANAIEH--PVDPvEPVITVEASLVDGAVVITVRDSGRW 1126
Cdd:COG2172      2 LSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHayGGDP-DGPVEVELELDPDGLEIEVRDEGPG 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1986385785 1127 RETAA-------EGFRGRGLALIGALS-ELSVSRSDSGTSVTLRRPL 1165
Cdd:COG2172     81 FDPEDlpdpystLAEGGRGLFLIRRLMdEVEYESDPGGTTVRLVKRL 127
pleD PRK09581
response regulator PleD; Reviewed
571-683 5.58e-24

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 106.91  E-value: 5.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADD-NADLRDHVARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:PRK09581     4 RILVVDDiPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVT 83
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:PRK09581    84 ALDDPEDRVRGLEAGADDFLTKPINDVALFARVK 117
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
572-727 1.59e-23

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 99.94  E-value: 1.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAderTRDVPIVVLSA 650
Cdd:NF040689     1 ILVVDDDPALAEMLGIVLRAEgFETVFCADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIRA---ESGVPIIMLTA 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRAnldlgqarrqiisRLRGLVDTAAalNTVRTTAEVLDVAAQHVR 727
Cdd:NF040689    78 KSDTVDVVRGLEAGADDYVVKPFKPKELVARIRA-------------RLRRSEDEES--EVLRIGDLTIDVAGHEVT 139
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
187-686 1.88e-23

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 107.46  E-value: 1.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  187 AELVLDDAVGPHPVVrqviesgQPARVALTEIVERPPADAAAEALVLPITVGTATAGALVVGL-SRYLELGGGYRDFLEL 265
Cdd:PRK13837   344 RALASTVKAAERDVV-------FVDRNGPVRKRSCLTRRGPALWACLAFKSGDRIVALLGLGRqRYGLRPPAGELQLLEL 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  266 AAAQISRAVGNLRAYEQERARAAELAALD--QAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRLPALQRERLLPMQRNG 343
Cdd:PRK13837   417 ALDCLAHAIERRRLETERDALERRLEHARrlEAVGTLASGIAHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAG 496
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  344 LRLLKLVNTVLDFSRlesgRLRAEYRATDLADYTWRLASTFRSAAERaGLELVVETPPLSAPVYVDREMWEKIVLNLLSN 423
Cdd:PRK13837   497 ARARLIIDQILAFGR----KGERNTKPFDLSELVTEIAPLLRVSLPP-GVELDFDQDQEPAVVEGNPAELQQVLMNLCSN 571
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  424 AVK-FTAAGRVVVRIGA--------------DAGD-AVLSVEDTGVGIPADQQPLLFDRFHRVTGAwarsheGTGIGLAL 487
Cdd:PRK13837   572 AAQaMDGAGRVDISLSRaklrapkvlshgvlPPGRyVLLRVSDTGAGIDEAVLPHIFEPFFTTRAG------GTGLGLAT 645
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  488 VRELAELHGGSASAASEPGRGSVFTVRvpfgtahlpadrvLPDGERIAPefdarpyaeeaehwwtgdEPVTLPLPPPAGR 567
Cdd:PRK13837   646 VHGIVSAHAGYIDVQSTVGRGTRFDVY-------------LPPSSKVPV------------------APQAFFGPGPLPR 694
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  568 RPGRI--LLADDNADLRDHVARLLRPHWDVTTAVDGQAALELTRRG--RFDLVLTDvmMPRLDGFGLIAALRADERTrdv 643
Cdd:PRK13837   695 GRGETvlLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKGpeRFDLVLVD--DRLLDEEQAAAALHAAAPT--- 769
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1986385785  644 PIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:PRK13837   770 LPIILGGNSKTMALSPDLLASVAEILAKPISSRTLAYALRTAL 812
resp_reg_YycF NF040534
response regulator YycF;
571-686 5.23e-21

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 93.25  E-value: 5.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVA-RLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadeRTRDVPIVVLS 649
Cdd:NF040534     2 KILVVDDEKPIADILEfNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVR---KKYDMPIIMLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:NF040534    79 AKDSEIDKVLGLELGADDYVTKPFSTRELIARVKANL 115
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
1051-1162 1.01e-16

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 77.71  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1051 LPAEPGRLSVLRRRLEDFLTGNGVPDDDVFDLTVAVSEAAANAIEH--PVDPVEPVItVEASLVDGAVVITVRDSGRW-- 1126
Cdd:pfam13581    1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHayREGPEGPVE-VRLTSDGGGLVVTVADSGPPfd 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1986385785 1127 ----------RETAAEGFRGRGLALIGALS-ELSVSRSDSGTSVTLR 1162
Cdd:pfam13581   80 pltlpppdleEPDEDRKEGGRGLALIRGLMdDVEYTRGGEGNTVRMR 126
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
1084-1162 5.61e-13

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 65.75  E-value: 5.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1084 VAVSEAAANAIEH-PVDPVEPVITVEASLVDGAVVITVRDSGRWR---------ETAAEGfrGRGLALIGALS-ELSVSR 1152
Cdd:cd16936      3 LAVSEAVTNAVRHaYRHDGPGPVRLELDLDPDRLRVEVTDSGPGFdplrpadpdAGLREG--GRGLALIRALMdEVGYRR 80
                           90
                   ....*....|
gi 1986385785 1153 SDSGTSVTLR 1162
Cdd:cd16936     81 TPGGKTVWLE 90
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
571-623 4.38e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.82  E-value: 4.38e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1986385785   571 RILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMP 623
Cdd:smart00448    2 RILVVDDDPLLRELLKALLeKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
572-673 1.00e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 65.44  E-value: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRP-HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTrdVPIVVLSA 650
Cdd:PRK10365     8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPA--IPVLIMTA 85
                           90       100
                   ....*....|....*....|...
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPF 673
Cdd:PRK10365    86 YSSVETAVEALKTGALDYLIKPL 108
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
1049-1161 1.99e-05

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 46.07  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1049 LRLPAEPGRLSVLRrrledfLTGNGVPD------DDVFDLTVAVSEAAANAIEHPVDPVEP-VITVEASLVDGAVVITVR 1121
Cdd:PRK04069    10 MKIPAKAEYVSIIR------LTLSGVANrmgfsyDDIEDMKIAVSEACTNAVQHAYKEDEVgEIHIRFEIYEDRLEIVVA 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785 1122 DSG------RWRETAA------------EGfrGRGLALIGAL-SELSVsRSDSGTSVTL 1161
Cdd:PRK04069    84 DNGvsfdyeTLKSKLGpydiskpiedlrEG--GLGLFLIETLmDDVTV-YKDSGVTVSM 139
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1085-1166 3.68e-05

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.18  E-value: 3.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  1085 AVSEAAANAIEHPvdPVEPVITVEASLVDGAVVITVRDSGR------------------WRETAAEGFrGRGLALIGALS 1146
Cdd:smart00387    9 VLSNLLDNAIKYT--PEGGRITVTLERDGDHVEITVEDNGPgippedlekifepffrtdKRSRKIGGT-GLGLSIVKKLV 85
                            90       100
                    ....*....|....*....|....*.
gi 1986385785  1147 E-----LSV-SRSDSGTSVTLRRPLS 1166
Cdd:smart00387   86 ElhggeISVeSEPGGGTTFTITLPLE 111
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
1077-1124 7.55e-04

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980 [Multi-domain]  Cd Length: 137  Bit Score: 41.06  E-value: 7.55e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1986385785 1077 DDVFDLTVAVSEAAANAIEHPVDP-VEPVITVEASLVDGAVVITVRDSG 1124
Cdd:TIGR01925   35 EELTDIKTAVSEAVTNAIIHGYEEnCEGVVYISATIEDHEVYITVRDEG 83
 
Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
294-516 2.52e-71

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 237.88  E-value: 2.52e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRL-PALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATD 372
Cdd:COG2205     13 ERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLsPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLSLELEPVD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  373 LADYTWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDT 451
Cdd:COG2205     93 LAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSpPGGTITISARREGDGVRISVSDN 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  452 GVGIPADQQPLLFDRFHRVTGawARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG2205    173 GPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLP 235
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
189-516 8.69e-71

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 239.81  E-value: 8.69e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  189 LVLDDAVGPHPVVRQVIESGQPARVALTEIVERPPADAAAEALVLPITVGTATAGALVVGLSRYLELGGGYRDFLELAAA 268
Cdd:COG0642      2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  269 QISRAVGNLRAYEQERARAAELAALDQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPrlPALQRERLLPMQRNGLRLLK 348
Cdd:COG0642     82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL--DEEQREYLETILRSADRLLR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  349 LVNTVLDFSRLESGRLRAEYRATDLADYTWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFT 428
Cdd:COG0642    160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYT 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  429 AAG-RVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGawARSHEGTGIGLALVRELAELHGGSASAASEPGR 507
Cdd:COG0642    240 PEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVESEPGK 317

                   ....*....
gi 1986385785  508 GSVFTVRVP 516
Cdd:COG0642    318 GTTFTVTLP 326
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
294-516 2.04e-70

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 240.99  E-value: 2.04e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRLPALQRERLLP-MQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATD 372
Cdd:COG5002    162 EQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEERREYLEiILEEAERLSRLVNDLLDLSRLESGELKLEKEPVD 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  373 LADYTWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAG-RVVVRIGADAGDAVLSVEDT 451
Cdd:COG5002    242 LAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSLREEDDQVRISVRDT 321
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  452 GVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG5002    322 GIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLP 386
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
623-1042 2.83e-64

Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 224.94  E-value: 2.83e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  623 PRLDGFGLIAALRADERTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQIISRLRGL 702
Cdd:COG2208      6 LRAALLLLLELLLAAALLLLLLLLLAALLALELLALLLALLLLLLALLLLLLLLLALRLALLLLALLLALLLLAALLLLA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  703 VDTAAALNTVRTTAEVLDVAAQHVRAMTTAGRVVVSVPGSRAEVDGGAAPGTQPDSVLPLPDTSGATVGELRVWSPPDGA 782
Cdd:COG2208     86 LLALALLLALLAALLLVLLLLLLLLLGLLAVALLLLLALLLLLALLLLALLLGLLLLLLLLLLLAALLLALALALALALL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  783 LEPAVLIQLARLIGLRLENARL--------YEAEHRIASTLQHSLLPQSLPRMPGTIVASRYLAGSneaEVGGDWYDVIA 854
Cdd:COG2208    166 LLLALAAALALLAALLLENARLeeeeknrrLERELELARRIQRSLLPPRLPEVPGLDIAARYRPAD---EVGGDFYDVFP 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  855 APDEQLVLVIGDVVGKGVQAAAGMGQLRNALRAYILEGFDCGEALTRLNR-LVDNLGRRQFATVVCVRYDPVTRGLHYSS 933
Cdd:COG2208    243 LDDGRLAVVIGDVSGHGVPAALLMAMLRSALRALAREGLDPAEVLERLNRaLYEDLGGGRFVTAFLGVLDPETGRLTYAN 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  934 AGHPPPVLVPPGdlGSFLYTSALGPPIGALADAVYPTLETEMPAGSRLLLYTDGLVE-----DRRIGIDsGLADLTADAA 1008
Cdd:COG2208    323 AGHPPPLLLRAD--GEVEELDGGGLPLGLLPDAEYEEHEIPLEPGDRLLLYTDGLTEarngdGELFGEE-RLLELLAENA 399
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1986385785 1009 K--PAEHVEDLLDDLLAKAVRRTRRDDIALLALQVT 1042
Cdd:COG2208    400 DlpAEELLDALLEALEEFRGGGPQEDDITLLALRRR 435
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
295-683 6.04e-54

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: 205.01  E-value: 6.04e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  295 QAKTNFFSNVSHEFRTPLTLILGPLEdVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLA 374
Cdd:TIGR02956  462 RAKSAFLATMSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLN 540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  375 DYTWRLASTFRSAAERAGLELVVETPP-LSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIG-ADAGDAVLSVEDTG 452
Cdd:TIGR02956  541 ALLDDVHHLMVSRAQLKGIQLRLNIPEqLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSlNDDSSLLFEVEDTG 620
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  453 VGIPADQQPLLFDRFHRVTGawARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFgtahlpadrvlpdgE 532
Cdd:TIGR02956  621 CGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL--------------T 684
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  533 RIAPEFDArpyaeeaehwwTGDEPVTLPlpppagrrPGRILLADDN-ADLRDHVARLLRPHWDVTTAVDGQAALELTRRG 611
Cdd:TIGR02956  685 RGKPAEDS-----------ATLTVIDLP--------PQRVLLVEDNeVNQMVAQGFLTRLGHKVTLAESGQSALECFHQH 745
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  612 RFDLVLTDVMMPRLDGFGLIAALRADERTRD-VPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:TIGR02956  746 AFDLALLDINLPDGDGVTLLQQLRAIYGAKNeVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIA 818
PRK15347 PRK15347
two component system sensor kinase;
297-678 1.80e-50

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 193.70  E-value: 1.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  297 KTNFFSNVSHEFRTPLTLILGPLEdVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATD---L 373
Cdd:PRK15347   398 KSEHLTTISHEIRTPLNGVLGALE-LLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETAllpL 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  374 ADYTwrlASTFRSAAERAGLEL---VVETPPLSApvYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIGADAGDAVLSVED 450
Cdd:PRK15347   477 LDQA---MLTIQGPAQSKSLTLrtfVGAHVPLYL--HLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVED 551
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  451 TGVGIPADQQPLLFDRFHRVTGawarsHE-GTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFGTAHLPAD---- 525
Cdd:PRK15347   552 TGCGIDIQQQQQIFTPFYQADT-----HSqGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEPlkge 626
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  526 --------RVL-----------PDGERIAPE---FDARPYAE-EAEHWWTGDEP-VTLPLPPpagrRPGRILLADDNADL 581
Cdd:PRK15347   627 lsaplalhRQLsawgitcqpghQNPALLDPElayLPGRLYDLlQQIIQGAPNEPvINLPLQP----WQLQILLVDDVETN 702
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  582 RDHVARLLRP--HwDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADE--RTRDVPIVVLSARAGEESA 657
Cdd:PRK15347   703 RDIIGMMLVElgQ-QVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPnnLDPDCMIVALTANAAPEEI 781
                          410       420
                   ....*....|....*....|.
gi 1986385785  658 VEGLGAGADDYLVKPFSARDL 678
Cdd:PRK15347   782 HRCKKAGMNHYLTKPVTLAQL 802
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
856-1041 2.03e-49

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 462119 [Multi-domain]  Cd Length: 192  Bit Score: 173.60  E-value: 2.03e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  856 PDEQLVLVIGDVVGKGVQAAAGMGQLRNALRAYILEGFDCGEALTRLNRLV-DNLGRRQFATVVCVRYDPVTRGLHYSSA 934
Cdd:pfam07228    1 PDGRLALVIGDVMGHGLPAALLMGLLRTALRALAAEGLDPAEVLKRLNRLLqRNLEEDMFATAVLAVYDPETGTLEYANA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  935 GHPPPVLVPPGDlGSFLYTSALGPPIGALADAVYPTLETEMPAGSRLLLYTDGLVE--DRRIGIDSGLADLTADAAKPAE 1012
Cdd:pfam07228   81 GHPPPLLLRPDG-GVVELLESPGLPLGILPDAPYEVVELELEPGDTLLLYTDGLTEarDPDGELFGLERLLALLAERHGL 159
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1986385785 1013 HVEDLLDDLLAKAVRRT---RRDDIALLALQV 1041
Cdd:pfam07228  160 PPEELLDALLEALLRLGggeLEDDITLLVLRV 191
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
297-680 2.44e-49

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 189.00  E-value: 2.44e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  297 KTNFFSNVSHEFRTPLTLILGpLEDVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLADY 376
Cdd:PRK11091   283 KTTFISTISHELRTPLNGIVG-LSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDF 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  377 TWRLASTFRSAAERAGLELVVE-TPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIGADAGDAVL-SVEDTGVG 454
Cdd:PRK11091   362 LADLENLSGLQAEQKGLRFDLEpLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGDMLTfEVEDSGIG 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  455 IPADQQPLLFDRFHRVT-GAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVrvpfgTAHLPAdrvlpdger 533
Cdd:PRK11091   442 IPEDELDKIFAMYYQVKdSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTL-----TIHAPA--------- 507
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  534 iapefdarpYAEEAEhwwtgDEPVTLPLPPPAgrrpGRILLADDnADLRDHVARLL---RPHwDVTTAVDGQAALELTRR 610
Cdd:PRK11091   508 ---------VAEEVE-----DAFDEDDMPLPA----LNILLVED-IELNVIVARSVlekLGN-SVDVAMTGKEALEMFDP 567
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1986385785  611 GRFDLVLTDVMMPRLDGFGLIAALRADERTRDV-PIVVLSARAGEESAvEGLGAGADDYLVKPFSARDLIA 680
Cdd:PRK11091   568 DEYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTANVLKDKK-EYLDAGMDDVLSKPLSVPALTA 637
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
294-514 8.35e-44

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: 162.38  E-value: 8.35e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRL-PALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATD 372
Cdd:TIGR02966  111 EQMRRDFVANVSHELRTPLTVLRGYLETLADGPDEdPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVD 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  373 LADYTWRLASTFRSAAERAGLELVVETPPlSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVV-VRIGADAGDAVLSVEDT 451
Cdd:TIGR02966  191 MPALLDHLRDEAEALSQGKNHQITFEIDG-GVDVLGDEDELRSAFSNLVSNAIKYTPEGGTItVRWRRDGGGAEFSVTDT 269
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  452 GVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVR 514
Cdd:TIGR02966  270 GIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFI 332
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
295-683 3.23e-41

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 164.76  E-value: 3.23e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  295 QAKTNFFSNVSHEFRTPLTLILGPLeDVLDDPRLPAlQRERLL-PMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRatdl 373
Cdd:PRK10841   445 QSKSMFLATVSHELRTPLYGIIGNL-DLLQTKELPK-GVDRLVtAMNNSSSLLLKIISDILDFSKIESEQLKIEPR---- 518
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  374 aDYTWRLASTFRSAAEragLELVVETP--------PlSAPVYV--DREMWEKIVLNLLSNAVKFTAAGRVVVRIGADAGD 443
Cdd:PRK10841   519 -EFSPREVINHITANY---LPLVVKKRlglycfieP-DVPVALngDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDGDY 593
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  444 AVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFGTAHLP 523
Cdd:PRK10841   594 LSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLYGAQYP 673
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  524 ADRVLPD----------------------------------GERIAP--------------------EFDAR---PYAEE 546
Cdd:PRK10841   674 QKKGVEGlqgkrcwlavrnasleqfletllqrsgiqvqryeGQEPTPedvlitddpvqkkwqgraviTFCRRhigIPLEI 753
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  547 AEHWWT---------------------GDEPVTLPLPPPAGRRPG----RILLADDNADLRdhvaRLLRPH-----WDVT 596
Cdd:PRK10841   754 APGEWVhstatphelpallariyrielESDDSANALPSTDKAVSDnddmMILVVDDHPINR----RLLADQlgslgYQCK 829
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  597 TAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTrdVPIVVLSARAGEESAVEGLGAGADDYLVKPFSAR 676
Cdd:PRK10841   830 TANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLT--LPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLD 907
                          490
                   ....*....|....
gi 1986385785  677 DL-------IARVR 683
Cdd:PRK10841   908 VLkqtltvyAERVR 921
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
571-736 9.65e-41

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: 149.34  E-value: 9.65e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrDVPIVVLS 649
Cdd:COG0745      3 RILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPS--DIPIIMLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRAnldLGQARRQIISRLRGLVDTAAalNTVRTTAEVLDVAAQHVRA- 728
Cdd:COG0745     81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRA---LLRRRAAEVLRVGDLLDLAA--REVTRDGEPVELTPKEFRLl 155
                          170
                   ....*....|.
gi 1986385785  729 ---MTTAGRVV 736
Cdd:COG0745    156 ellMRNPGRVV 166
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
299-516 2.26e-39

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: 152.93  E-value: 2.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  299 NFFSNVSHEFRTPLTLILGPLEDVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLADYTW 378
Cdd:TIGR01386  243 QFSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELA 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  379 RLASTFRSAAERAGLELVVETpplSAPVYVDREMWEKIVLNLLSNAVKFTAAG-RVVVRIGADAGDAVLSVEDTGVGIPA 457
Cdd:TIGR01386  323 KVAEYFEPLAEERGVRIRVEG---EGLVRGDPQMFRRAISNLLSNALRHTPDGgTITVRIERRSDEVRVSVSNPGPGIPP 399
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785  458 DQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRgSVFTVRVP 516
Cdd:TIGR01386  400 EHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILRFP 457
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
569-682 2.64e-39

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: 144.28  E-value: 2.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  569 PGRILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVV 647
Cdd:COG3706      1 PARILVVDDDPTNRKLLRRLLEAAgYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKPFSARDLIARV 682
Cdd:COG3706     81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
416-517 3.99e-39

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: 141.09  E-value: 3.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSNAVKFTAAGRVVVRI---GADAGDAVL--SVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRE 490
Cdd:cd16922      4 ILLNLLGNAIKFTEEGEVTLRVsleEEEEDGVQLrfSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISKK 83
                           90       100
                   ....*....|....*....|....*..
gi 1986385785  491 LAELHGGSASAASEPGRGSVFTVRVPF 517
Cdd:cd16922     84 LVELMGGDISVESEPGQGSTFTFTLPL 110
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
568-706 1.24e-37

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: 141.07  E-value: 1.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  568 RPGRILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIV 646
Cdd:COG3437      5 QAPTVLIVDDDPENLELLRQLLRTLgYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVI 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  647 VLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQIISRLRGLVDTA 706
Cdd:COG3437     85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAA 144
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
296-674 1.77e-37

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 153.35  E-value: 1.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  296 AKTNFFSNVSHEFRTPLTLILGPLEdVLDDPRLPALQRERLLPMQ-RNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLA 374
Cdd:PRK09959   711 AKSQFLATMSHEIRTPISSIMGFLE-LLSGSGLSKEQRVEAISLAyATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIP 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  375 DYTWRLASTFRSAAERAGLELVVE-TPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVVVR---IGADAGDAV--LSV 448
Cdd:PRK09959   790 TLVQNTCHSFGAIAASKSIALSCSsTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITtslGHIDDNHAVikMTI 869
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  449 EDTGVGIPADQQPLLFDRFHRVTGAwaRSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFgtahlpadrvl 528
Cdd:PRK09959   870 MDSGSGLSQEEQQQLFKRYSQTSAG--RQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPV----------- 936
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  529 pdgeriapEFDARPYAEEAEhwwtGDEPVTLPlpppagrRPGRILLADDNADLRDHVARLLRP-HWDVTTAVDGQAALEL 607
Cdd:PRK09959   937 --------EISQQVATVEAK----AEQPITLP-------EKLSILIADDHPTNRLLLKRQLNLlGYDVDEATDGVQALHK 997
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986385785  608 TRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFS 674
Cdd:PRK09959   998 VSMQHYDLLITDVNMPNMDGFELTRKLR--EQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLT 1062
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
567-691 3.47e-37

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 136.13  E-value: 3.47e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  567 RRPGRILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPI 645
Cdd:COG0784      3 LGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPI 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1986385785  646 VVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQA 691
Cdd:COG0784     83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
828-1023 3.26e-36

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 135.94  E-value: 3.26e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   828 PGTIVASRYLAGSneaEVGGDWYDVIAAPDEQLVLVIGDVVGKGVQAAAGMGQLRNALRAYILEGFDCGEALTRLNRLVD 907
Cdd:smart00331    2 DGGLIAQYYEDAT---QVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   908 NLG-RRQFATVVCVRYDPVTRGLHYSSAGHPPPVLVPPGDlGSFLYTSALGPPIGALADAVYPTLETEMPAGSRLLLYTD 986
Cdd:smart00331   79 ENGeDGMFATLFLALYDFAGGTLSYANAGHSPPYLLRADG-GLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTD 157
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1986385785   987 GLVEDRRIGIDSG-LADLTADAakPAEHVEDLLDDLLA 1023
Cdd:smart00331  158 GLTEARNPERLEElLEELLGSP--PAEIAQRILEELLE 193
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
67-516 7.92e-36

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 143.39  E-value: 7.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   67 LGRPGSEMWAEAWTVLQPLFDGVVTGDEAFWAADYPFRLERHGFLEETYFDISYDPIRLDSGEVGGLFCIVSDTTGRVLG 146
Cdd:COG4251     52 LLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  147 ERRVRTLSALGSRLADSPDQAALAAEVVAVLGENAADAPFAELVLDDAVGPHPVVRQVIESGQPARVALTEIVERPPADA 226
Cdd:COG4251    132 LALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLL 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  227 AAEALVLPITVGTATAGALVVGLSRYLELGGGYRDFLELAAAQISRAVGNLRAYEQERARAAELAALDQAKTNFFSNVSH 306
Cdd:COG4251    212 LLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASH 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  307 EFRTPL-------TLILGPLEDVLDDPRLPALQRerllpMQRNGLRLLKLVNTVLDFSRLesGRLRAEYRATDLADYTWR 379
Cdd:COG4251    292 DLREPLrkisgfsQLLEEDYGDKLDEEGREYLER-----IRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEE 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  380 LASTFRSAAERAGLELVVETPPlsaPVYVDREMWEKIVLNLLSNAVKFTAAGRV-VVRIGA--DAGDAVLSVEDTGVGIP 456
Cdd:COG4251    365 VLEDLEPRIEERGAEIEVGPLP---TVRGDPTLLRQVFQNLISNAIKYSRPGEPpRIEIGAerEGGEWVFSVRDNGIGID 441
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  457 ADQQPLLFDRFHRVTGAwaRSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG4251    442 PEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
297-672 1.67e-34

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 143.45  E-value: 1.67e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  297 KTNFFSNVSHEFRTPLTLILGPLEDVLDDPrLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAE-----YRAT 371
Cdd:PRK11107   293 KSEFLANMSHELRTPLNGVIGFTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLEnipfsLRET 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  372 dlADYTWRLASTfrSAAERaGLELVVETPPlSAPVYV--DREMWEKIVLNLLSNAVKFTAAGRVVVRI--GADAGDAVL- 446
Cdd:PRK11107   372 --LDEVVTLLAH--SAHEK-GLELTLNIDP-DVPDNVigDPLRLQQIITNLVGNAIKFTESGNIDILVelRALSNTKVQl 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  447 --SVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFGTAHLPA 524
Cdd:PRK11107   446 evQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPI 525
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  525 DRVLP----DGERIApEFDARPYAEEA-----EHWWT-----------GDE----------------------------- 555
Cdd:PRK11107   526 IDGLPtdclAGKRLL-YVEPNSAAAQAtldilSETPLevtysptlsqlPEAhydilllglpvtfrepltmlherlakaks 604
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  556 -------------------------------PVT------------------LPLPPPAGRRPGRILLADDN-------- 578
Cdd:PRK11107   605 mtdflilalpcheqvlaeqlkqdgadaclskPLShtrllpallepchhkqppLLPPTDESRLPLTVMAVDDNpanlklig 684
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  579 ADLRDHVArllrphwDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSARAGEESAV 658
Cdd:PRK11107   685 ALLEEQVE-------HVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERE 757
                          490
                   ....*....|....
gi 1986385785  659 EGLGAGADDYLVKP 672
Cdd:PRK11107   758 RLLSAGMDDYLAKP 771
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
409-517 3.12e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 126.99  E-value: 3.12e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785   409 DREMWEKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRvTGAWARSHEGTGIGLAL 487
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFR-TDKRSRKIGGTGLGLSI 80
                            90       100       110
                    ....*....|....*....|....*....|
gi 1986385785   488 VRELAELHGGSASAASEPGRGSVFTVRVPF 517
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITLPL 110
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
302-516 3.53e-34

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 135.31  E-value: 3.53e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  302 SNVSHEFRTPLTLILG---PLEDVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAeyraTDLADYTW 378
Cdd:COG4191    147 AGIAHEINNPLAAILGnaeLLRRRLEDEPDPEELREALERILEGAERAAEIVRSLRAFSRRDEEEREP----VDLNELID 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  379 RLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSN---AVKFTAAGRVVVRIGADAGDAVLSVEDTGVGI 455
Cdd:COG4191    223 EALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINaidAMEEGEGGRITISTRREGDYVVISVRDNGPGI 302
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  456 PADQQPLLFDRFH--RVTGawarshEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG4191    303 PPEVLERIFEPFFttKPVG------KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
294-517 2.43e-33

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 137.19  E-value: 2.43e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEdVLDDprlPALQRERLLP-----MQRNGLRLLKLVNTVLDFSRLESGRLRAEY 368
Cdd:NF033092   369 EQERREFVANVSHELRTPLTTMRSYLE-ALAD---GAWKDPELAPrflgvTQNETERMIRLVNDLLQLSRMDSKDYKLNK 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  369 RATDLADYTWRLASTFRSAAERAGLELVVETPPLSAPVYVDRemwEKI--VL-NLLSNAVKFT-AAGRVVVRIGADAGDA 444
Cdd:NF033092   445 EWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDT---DKItqVLdNIISNAIKYSpEGGTITFRLLETHNRI 521
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  445 VLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPF 517
Cdd:NF033092   522 IISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLPY 594
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
573-672 1.94e-32

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: 121.36  E-value: 1.94e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  573 LLADDNADLRDHVARLLRP-HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtRDVPIVVLSAR 651
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKeGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1986385785  652 AGEESAVEGLGAGADDYLVKP 672
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
573-684 1.34e-31

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: 119.63  E-value: 1.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  573 LLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrDVPIVVLSAR 651
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGI--ETPVLLLTAL 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1986385785  652 AGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:cd17625     79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIRA 111
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
568-717 1.39e-31

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: 128.93  E-value: 1.39e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  568 RPGRILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIV 646
Cdd:COG2204      1 SMARILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELR--ALDPDLPVI 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1986385785  647 VLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQiISRLRGLVDTAAALNTVRTTAE 717
Cdd:COG2204     79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRE-NAEDSGLIGRSPAMQEVRRLIE 148
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
300-516 5.40e-31

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 128.99  E-value: 5.40e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  300 FFSNVSHEFRTPLTLILGPlEDVLDDPRL---PALQRERLLpMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLADY 376
Cdd:NF040691   274 FVSDVSHELRTPLTTIRMA-ADVIHDSRDdfdPATARSAEL-LHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPL 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  377 TWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIGADaGDAV-LSVEDTGVGI 455
Cdd:NF040691   352 VRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQD-DTAVaVTVRDHGVGL 430
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1986385785  456 PADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:NF040691   431 KPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLP 491
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
571-686 6.29e-31

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: 117.74  E-value: 6.29e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:cd17618      2 TILIVEDEPAIREMIAFNLeRAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17618     82 ARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
304-516 4.04e-30

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: 124.69  E-value: 4.04e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  304 VSHEFRTPLT---LILGPLEDVLDDPRLPALQR-ERLLPM-QRNGLRLLKLVNTVLDFSRLEsgrlRAEYRATDLADYTW 378
Cdd:COG5000    208 IAHEIKNPLTpiqLSAERLRRKLADKLEEDREDlERALDTiIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLR 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  379 RLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAA-GRVVVRIGADAGDAVLSVEDTGVGIPA 457
Cdd:COG5000    284 EVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEgGEIEVSTRREDGRVRIEVSDNGPGIPE 363
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785  458 DQQPLLFDRFhrVTGawarSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG5000    364 EVLERIFEPF--FTT----KPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLP 416
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
573-672 7.27e-30

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 114.25  E-value: 7.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  573 LLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtRDVPIVVLSAR 651
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1986385785  652 AGEESAVEGLGAGADDYLVKP 672
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
416-517 1.88e-29

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: 113.23  E-value: 1.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSNAVKFTA-AGRVVVRIGADaGDAVLSVEDTGVGIPADQQPLLFDRFHRVTgawARSHEGTGIGLALVRELAEL 494
Cdd:pfam02518    9 VLSNLLDNALKHAAkAGEITVTLSEG-GELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGLGLSIVRKLVEL 84
                           90       100
                   ....*....|....*....|...
gi 1986385785  495 HGGSASAASEPGRGSVFTVRVPF 517
Cdd:pfam02518   85 LGGTITVESEPGGGTTVTLTLPL 107
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
571-673 3.50e-29

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: 112.21  E-value: 3.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPF 673
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
573-686 4.50e-29

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: 112.37  E-value: 4.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  573 LLADDNADLRDHVA-RLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSAR 651
Cdd:cd19937      1 LVVDDEEDIVELLKyNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  652 AGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd19937     81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
294-630 5.80e-29

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 125.40  E-value: 5.80e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRLPAlQRERLLPMQRNGLRLLKLVNTVLDFSRLESG----RLRAE-Y 368
Cdd:PRK11466   441 SQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNA-QRDDLRAITDSGESLLTILNDILDYSAIEAGgknvSVSDEpF 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  369 RATDLADYTWRLAStfrSAAERAGLELVVE-TPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIGADAGDAVLS 447
Cdd:PRK11466   520 EPRPLLESTLQLMS---GRVKGRPIRLATDiADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRTDGEQWLVE 596
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  448 VEDTGVGIPADQQPLLFDRFHRVTGawarSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFGTAHLPAdrv 527
Cdd:PRK11466   597 VEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPV--- 669
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  528 lPDGERIAPEFDARpyaeeaehwwtgdepvtlplpppagrrpgRILLADDNADLRDHVARLLRPHW-DVTTAVDGQAALE 606
Cdd:PRK11466   670 -PKTVNQAVRLDGL-----------------------------RLLLIEDNPLTQRITAEMLNTSGaQVVAVGNAAQALE 719
                          330       340
                   ....*....|....*....|....*
gi 1986385785  607 LTRRGR-FDLVLTDVMMPRLDGFGL 630
Cdd:PRK11466   720 TLQNSEpFAAALVDFDLPDYDGITL 744
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
302-524 1.45e-28

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 118.80  E-value: 1.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  302 SNVSHEFRTPLTLILGP---LEDVLDDPRLpalqRERLLPMQRNGLRLLKLVNTVLDFSRlesgRLRAEYRATDLADYTW 378
Cdd:COG3852    140 AGLAHEIRNPLTGIRGAaqlLERELPDDEL----REYTQLIIEEADRLNNLVDRLLSFSR----PRPPEREPVNLHEVLE 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  379 RLASTFRSAAERaGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAA-GRVVVRIGADAGD----------AVLS 447
Cdd:COG3852    212 RVLELLRAEAPK-NIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEgGTITIRTRVERQVtlgglrprlyVRIE 290
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986385785  448 VEDTGVGIPADQQPLLFDRFhrVTGawarSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFGTAHLPA 524
Cdd:COG3852    291 VIDNGPGIPEEILDRIFEPF--FTT----KEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
572-683 2.35e-28

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 110.32  E-value: 2.35e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHW-DVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLSA 650
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGyVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIR--RRDPTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
409-516 3.03e-28

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: 109.89  E-value: 3.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  409 DREMWEKIVLNLLSNAVKFT-AAGRVVVRIGA-DAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLA 486
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTpDGGRIRCILEKfRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLS 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785  487 LVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16925     81 IVKEFVELHGGTVTVSDAPGGGALFQVELP 110
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
297-516 6.06e-28

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 119.11  E-value: 6.06e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  297 KTNFFSNVSHEFRTPLTLILGPLEDVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLADY 376
Cdd:PRK09835   262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  377 TWRLASTFRSAAERAGLEL-VVETPPLsapVYVDREMWEKIVLNLLSNAVKFTAAG-RVVVRIGADAGDAVLSVEDTGVG 454
Cdd:PRK09835   342 VGKVFDFFEAWAEERGVELrFVGDPCQ---VAGDPLMLRRAISNLLSNALRYTPAGeAITVRCQEVDHQVQLVVENPGTP 418
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1986385785  455 IPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPgRGSVFTVRVP 516
Cdd:PRK09835   419 IAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLP 479
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
571-683 1.54e-27

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: 108.16  E-value: 1.54e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLR-PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:cd17562      2 KILAVDDSASIRQMVSFTLRgAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd17562     82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVK 115
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
294-516 1.60e-27

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 117.62  E-value: 1.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRlpALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDL 373
Cdd:NF012163   237 EQMRRDFMADISHELRTPLAVLRAELEAIQDGIR--KFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  374 ADYTWRLASTFRSAAERAGLELVVETPPlSAPVYVDREMWEKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDTG 452
Cdd:NF012163   315 VPLLEVEGGAFRERFASAGLELEVSLPD-SSLVFGDRDRLMQLFNNLLENSLRYTdSGGSLHISASQRPKEVTLTVADSA 393
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1986385785  453 VGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:NF012163   394 PGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
571-672 2.44e-27

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: 107.17  E-value: 2.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVV 647
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILEWEAGfevVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIR--ELDPDTKIII 78
                           90       100
                   ....*....|....*....|....*
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKP 672
Cdd:COG4753     79 LSGYSDFEYAQEAIKLGADDYLLKP 103
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
572-680 3.55e-27

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: 106.78  E-value: 3.55e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERT-RDVPIVVLS 649
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLgYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGgRRTPIIALT 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIA 680
Cdd:cd17546     81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKE 111
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
572-673 9.58e-27

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 105.29  E-value: 9.58e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSA 650
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAgYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                           90       100
                   ....*....|....*....|...
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPF 673
Cdd:cd19920     81 LTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
572-686 1.55e-26

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: 105.16  E-value: 1.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLR-PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrDVPIVVLSA 650
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRfEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGN--DLPILVLTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17627     79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
306-516 1.95e-26

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 114.56  E-value: 1.95e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  306 HEFRTPLTLILGPLEdVLDDPrLPALQRERLLP-MQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLADYTWRLASTF 384
Cdd:PRK11100   265 HELKSPLAAIRGAAE-LLQED-PPPEDRARFTGnILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAR 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  385 RSAAERAGLELVVETPPLSapVYVDREMWEKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLL 463
Cdd:PRK11100   343 EAQAAAKGITLRLRPDDAR--VLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVDGEQVALSVEDQGPGIPDYALPRI 420
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1986385785  464 FDRFHRVtgawARSHEG---TGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:PRK11100   421 FERFYSL----PRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLP 472
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
571-686 2.28e-26

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 108.57  E-value: 2.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLR-PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:TIGR02154    4 RILVVEDEPAIRELIAYNLEkAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPIIMLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:TIGR02154   84 ARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVL 120
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
296-516 3.02e-26

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 113.18  E-value: 3.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  296 AKTNFFSNVSHEFRTPLTLILGPLEdVLDDPRLPALQRER-LLPMQRNGLRLLKLVNTVLDFSRLESG------------ 362
Cdd:PRK11006   203 ARRNFFANVSHELRTPLTVLQGYLE-MMQDQPLEGALREKaLHTMREQTQRMEGLVKQLLTLSKIEAAptidlnekvdvp 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  363 -RLRA-EYRATDLADYTWRLasTFRSAAeraglelvvetpplSAPVYVDREMWEKIVLNLLSNAVKFTAAG-RVVVRIGA 439
Cdd:PRK11006   282 mMLRVlEREAQTLSQGKHTI--TFEVDN--------------SLKVFGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQR 345
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986385785  440 DAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:PRK11006   346 VPQGAEFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
571-686 3.29e-26

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: 104.45  E-value: 3.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLR--PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:cd17551      2 RILIVDDNPTNLLLLEALLRsaGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVRaNL 686
Cdd:cd17551     82 TADTDREVRLRALEAGATDFLTKPFDPVELLARVR-NL 118
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
571-682 2.29e-25

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: 102.03  E-value: 2.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRP--HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:cd19923      2 KVLVVDDFSTMRRIIKNLLKElgFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARV 682
Cdd:cd19923     82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
571-686 7.07e-25

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: 100.50  E-value: 7.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLR-PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrDVPIVVLS 649
Cdd:cd17615      1 RVLVVDDEPNITELLSMALRyEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGP--DVPVLFLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17615     79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL 115
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
572-684 7.41e-25

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: 100.25  E-value: 7.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAdeRTRDVPIVVLSA 650
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTA 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:cd17624     79 RDGVDDRVAGLDAGADDYLVKPFALEELLARLRA 112
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
572-686 2.07e-24

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: 99.03  E-value: 2.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVA-RLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadeRTRDVPIVVLSA 650
Cdd:cd17614      1 ILVVDDEKPISDILKfNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR---KTSNVPIIMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17614     78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
572-672 3.48e-24

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: 97.90  E-value: 3.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVAR-LLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAdeRTRDVPIVVLSA 650
Cdd:cd19935      1 ILVVEDEKKLAEYLKKgLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLMLTA 78
                           90       100
                   ....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKP 672
Cdd:cd19935     79 RDSVEDRVKGLDLGADDYLVKP 100
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
1049-1165 4.16e-24

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 98.83  E-value: 4.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1049 LRLPAEPGRLSVLRRRLEDFLTGNGVPDDDVFDLTVAVSEAAANAIEH--PVDPvEPVITVEASLVDGAVVITVRDSGRW 1126
Cdd:COG2172      2 LSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHayGGDP-DGPVEVELELDPDGLEIEVRDEGPG 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1986385785 1127 RETAA-------EGFRGRGLALIGALS-ELSVSRSDSGTSVTLRRPL 1165
Cdd:COG2172     81 FDPEDlpdpystLAEGGRGLFLIRRLMdEVEYESDPGGTTVRLVKRL 127
pleD PRK09581
response regulator PleD; Reviewed
571-683 5.58e-24

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 106.91  E-value: 5.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADD-NADLRDHVARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:PRK09581     4 RILVVDDiPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVT 83
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:PRK09581    84 ALDDPEDRVRGLEAGADDFLTKPINDVALFARVK 117
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
304-516 5.77e-24

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 108.13  E-value: 5.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  304 VSHEFRTPLTLILGPLEDVLDDPRLPAlQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRaEYRATDLADYTWRLast 383
Cdd:PRK11360   397 VAHEIRNPLTAIRGYVQIWRQQTSDPP-SQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQ-PVSLNALVEEVLQL--- 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  384 FRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVK-FTAAGRVVVRIG-ADAGDAVLSVEDTGVGIPADQQP 461
Cdd:PRK11360   472 FQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQaISARGKIRIRTWqYSDGQVAVSIEDNGCGIDPELLK 551
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  462 LLFDRFHrVTGAwarshEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:PRK11360   552 KIFDPFF-TTKA-----KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
572-727 1.59e-23

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 99.94  E-value: 1.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAderTRDVPIVVLSA 650
Cdd:NF040689     1 ILVVDDDPALAEMLGIVLRAEgFETVFCADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIRA---ESGVPIIMLTA 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRAnldlgqarrqiisRLRGLVDTAAalNTVRTTAEVLDVAAQHVR 727
Cdd:NF040689    78 KSDTVDVVRGLEAGADDYVVKPFKPKELVARIRA-------------RLRRSEDEES--EVLRIGDLTIDVAGHEVT 139
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
187-686 1.88e-23

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 107.46  E-value: 1.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  187 AELVLDDAVGPHPVVrqviesgQPARVALTEIVERPPADAAAEALVLPITVGTATAGALVVGL-SRYLELGGGYRDFLEL 265
Cdd:PRK13837   344 RALASTVKAAERDVV-------FVDRNGPVRKRSCLTRRGPALWACLAFKSGDRIVALLGLGRqRYGLRPPAGELQLLEL 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  266 AAAQISRAVGNLRAYEQERARAAELAALD--QAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRLPALQRERLLPMQRNG 343
Cdd:PRK13837   417 ALDCLAHAIERRRLETERDALERRLEHARrlEAVGTLASGIAHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAG 496
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  344 LRLLKLVNTVLDFSRlesgRLRAEYRATDLADYTWRLASTFRSAAERaGLELVVETPPLSAPVYVDREMWEKIVLNLLSN 423
Cdd:PRK13837   497 ARARLIIDQILAFGR----KGERNTKPFDLSELVTEIAPLLRVSLPP-GVELDFDQDQEPAVVEGNPAELQQVLMNLCSN 571
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  424 AVK-FTAAGRVVVRIGA--------------DAGD-AVLSVEDTGVGIPADQQPLLFDRFHRVTGAwarsheGTGIGLAL 487
Cdd:PRK13837   572 AAQaMDGAGRVDISLSRaklrapkvlshgvlPPGRyVLLRVSDTGAGIDEAVLPHIFEPFFTTRAG------GTGLGLAT 645
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  488 VRELAELHGGSASAASEPGRGSVFTVRvpfgtahlpadrvLPDGERIAPefdarpyaeeaehwwtgdEPVTLPLPPPAGR 567
Cdd:PRK13837   646 VHGIVSAHAGYIDVQSTVGRGTRFDVY-------------LPPSSKVPV------------------APQAFFGPGPLPR 694
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  568 RPGRI--LLADDNADLRDHVARLLRPHWDVTTAVDGQAALELTRRG--RFDLVLTDvmMPRLDGFGLIAALRADERTrdv 643
Cdd:PRK13837   695 GRGETvlLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKGpeRFDLVLVD--DRLLDEEQAAAALHAAAPT--- 769
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1986385785  644 PIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:PRK13837   770 LPIILGGNSKTMALSPDLLASVAEILAKPISSRTLAYALRTAL 812
orf27 CHL00148
Ycf27; Reviewed
571-686 2.59e-23

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 100.18  E-value: 2.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVA-RLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtrDVPIVVLS 649
Cdd:CHL00148     8 KILVVDDEAYIRKILEtRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES---DVPIIMLT 84
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:CHL00148    85 ALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
572-686 2.70e-23

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: 95.83  E-value: 2.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtrDVPIVVLSA 650
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEgFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17623     78 RGDDIDRILGLELGADDYLPKPFNPRELVARIRAIL 113
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
571-694 3.15e-23

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 96.58  E-value: 3.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLR---PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVV 647
Cdd:COG4565      5 RVLIVEDDPMVAELLRRYLErlpGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELR--ARGPDVDVIV 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQ 694
Cdd:COG4565     83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
572-680 2.46e-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: 2.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSA 650
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIA 680
Cdd:cd17580     81 YGQPEDRERALEAGFDAHLVKPVDPDELIE 110
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
571-683 2.46e-22

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: 92.99  E-value: 2.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd17548     81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
572-684 1.62e-21

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: 90.80  E-value: 1.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHV-ARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTrdVPIVVLSA 650
Cdd:cd19934      1 LLLVEDDALLAAQLkEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--TPVLILTA 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:cd19934     79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLRA 112
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
571-688 1.88e-21

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: 91.04  E-value: 1.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALE-LTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:cd17544      2 KVLVVDDSATSRNHLRALLRRHnFQVLEAANGQEALEvLEQHPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDL 688
Cdd:cd17544     82 SASGDNALSARFIKAGANDFLTKPFLPEEFYCRVTQNLET 121
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
572-683 2.32e-21

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: 90.46  E-value: 2.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSA 650
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIK 113
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
571-686 4.47e-21

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: 89.45  E-value: 4.47e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtrDVPIVVLS 649
Cdd:cd17626      2 RILVVDDDAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES---GVPIVMLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17626     79 AKSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
571-700 4.78e-21

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: 89.76  E-value: 4.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGfglIAALRADERTRDVPIVV 647
Cdd:cd17541      2 RVLIVDDSAVMRKLLSRILESDPDievVGTARDGEEALEKIKELKPDVITLDIEMPVMDG---LEALRRIMAERPTPVVM 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  648 LSARAGEESAV--EGLGAGADDYLVKPFSARDliarvranLDLGQARRQIISRLR 700
Cdd:cd17541     79 VSSLTEEGAEItlEALELGAVDFIAKPSGGIS--------LDLEEIAEELIEKIK 125
resp_reg_YycF NF040534
response regulator YycF;
571-686 5.23e-21

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 93.25  E-value: 5.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVA-RLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadeRTRDVPIVVLS 649
Cdd:NF040534     2 KILVVDDEKPIADILEfNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVR---KKYDMPIIMLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:NF040534    79 AKDSEIDKVLGLELGADDYVTKPFSTRELIARVKANL 115
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
571-727 5.67e-21

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 93.10  E-value: 5.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWDVTTAVD-GQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAdeRTRDVPIVVLS 649
Cdd:PRK11083     5 TILLVEDEQAIADTLVYALQSEGFTVEWFErGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLA--FHPALPVIFLT 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRAnldlgqarrqiisRLRGLVDTAAALNTVRTTAEVLDVAAQHVR 727
Cdd:PRK11083    83 ARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRT-------------ILRRVKKFAAPSPVIRIGHFELDEPAARIS 147
PRK10490 PRK10490
sensor protein KdpD; Provisional
294-520 6.06e-21

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 99.34  E-value: 6.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDD------PRLP-ALQ-RERLLPMQRnglrllkLVNTVLDFSRLESG--R 363
Cdd:PRK10490   661 EQLRNALLAALSHDLRTPLTVLFGQAEILTLDlasegsPHARqASEiRQQVLNTTR-------LVNNLLDMARIQSGgfN 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  364 LRAEYRATDLAdytwrLASTFRSAAER-AGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAgRVVVRIGADAG 442
Cdd:PRK10490   734 LRKEWLTLEEV-----VGSALQMLEPGlSGHPINLSLPEPLTLIHVDGPLFERVLINLLENAVKYAGA-QAEIGIDAHVE 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  443 DAVLSVE--DTGVGIPADQQPLLFDRFHRvtGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFGTA 520
Cdd:PRK10490   808 GERLQLDvwDNGPGIPPGQEQLIFDKFAR--GNKESAIPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLETP 885
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-516 6.63e-21

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: 89.06  E-value: 6.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  409 DREMWEKIVLNLLSNAVKFTAAGRVVvRIGADAGDAV--LSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLA 486
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGKL-RIRAAQTPQEvrLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLA 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785  487 LVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16946     80 ICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
PRK13557 PRK13557
histidine kinase; Provisional
304-687 6.67e-21

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 98.20  E-value: 6.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  304 VSHEFRTPLTLILGPLEDVLDDPRLPALQRERllpMQRNG-------LRLLKLVNTVLDFSRlesgRLRAEYRATDLADy 376
Cdd:PRK13557   170 IAHDFNNLLQVMSGYLDVIQAALSHPDADRGR---MARSVeniraaaERAATLTQQLLAFAR----KQRLEGRVLNLNG- 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  377 twrLASTFRSAAERA---GLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTA-AGRVVVR-----IGADAGDA--- 444
Cdd:PRK13557   242 ---LVSGMGELAERTlgdAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPeGGRVTIRtrnveIEDEDLAMyhg 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  445 -------VLSVEDTGVGIPADQQPLLFDRFHRVTGawarSHEGTGIGLALVRELAELHGGSASAASEPGRGSvfTVRVPF 517
Cdd:PRK13557   319 lppgryvSIAVTDTGSGMPPEILARVMDPFFTTKE----EGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGT--TVRLYF 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  518 gtahlPAdrvlpDGERIAPEFDARPYAEEAehwwTGDEpvtlplpppagrrpgRILLADDNADlrdhVARLLRPHWD--- 594
Cdd:PRK13557   393 -----PA-----SDQAENPEQEPKARAIDR----GGTE---------------TILIVDDRPD----VAELARMILEdfg 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  595 --VTTAVDGQAALELTRRG-RFDLVLTDVMMP-RLDGFGLiaalrADERTRDVP-IVVLSARAGEESAVEGLGAGAD--D 667
Cdd:PRK13557   440 yrTLVASNGREALEILDSHpEVDLLFTDLIMPgGMNGVML-----AREARRRQPkIKVLLTTGYAEASIERTDAGGSefD 514
                          410       420
                   ....*....|....*....|
gi 1986385785  668 YLVKPFSARDLIARVRANLD 687
Cdd:PRK13557   515 ILNKPYRRAELARRVRMVLD 534
ompR PRK09468
osmolarity response regulator; Provisional
571-694 7.46e-21

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 93.11  E-value: 7.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrDVPIVVLS 649
Cdd:PRK09468     7 KILVVDDDMRLRALLERYLTEQgFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNN--PTPIIMLT 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLdlgqaRRQ 694
Cdd:PRK09468    85 AKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVL-----RRQ 124
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
571-686 1.16e-20

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 88.58  E-value: 1.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVAR-LLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTrDVPIVVLS 649
Cdd:cd19939      1 RILIVEDELELARLTRDyLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR--EHS-HVPILMLT 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd19939     78 ARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
571-684 1.86e-20

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: 88.24  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNAD----LRDHVARLLRPHwDVTTAVDGQAALE-LTRRGRF------DLVLTDVMMPRLDGFGLIAALRADER 639
Cdd:cd17557      1 TILLVEDNPGdaelIQEAFKEAGVPN-ELHVVRDGEEALDfLRGEGEYadaprpDLILLDLNMPRMDGFEVLREIKADPD 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1986385785  640 TRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:cd17557     80 LRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
572-709 1.87e-20

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: 90.54  E-value: 1.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLSA 650
Cdd:COG4566      2 VYIVDDDEAVRDSLAFLLESAgLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELA--ARGSPLPVIFLTG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQIISRLRGLVDTAAAL 709
Cdd:COG4566     80 HGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRARLASL 138
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
295-516 3.42e-20

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 95.08  E-value: 3.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  295 QAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRLPAlqRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLA 374
Cdd:PRK10549   238 QMRRDFMADISHELRTPLAVLRGELEAIQDGVRKFT--PESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVDLV 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  375 DYTWRLASTFRSAAERAGLELVVETPPlSAPVYVDREMWEKIVLNLLSNAVKFTAA-GRVVVRIGADAGDAVLSVEDTGV 453
Cdd:PRK10549   316 PLLEVAGGAFRERFASRGLTLQLSLPD-SATVFGDPDRLMQLFNNLLENSLRYTDSgGSLHISAEQRDKTLRLTFADSAP 394
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  454 GIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:PRK10549   395 GVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELP 457
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
571-686 6.63e-20

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 89.86  E-value: 6.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRrGRFDLVLTDVMMPRLDGFGLIAALRADERTrdvPIVVLS 649
Cdd:PRK10955     3 KILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTHQT---PVIMLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:PRK10955    79 ARGSELDRVLGLELGADDYLPKPFNDRELVARIRAIL 115
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
419-516 1.19e-19

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: 85.33  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  419 NLLSNAVKFTA-AGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGG 497
Cdd:cd16952      7 NLVSNAVKYTPpSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVMSRHDA 86
                           90
                   ....*....|....*....
gi 1986385785  498 SASAASEPGRGSVFTVRVP 516
Cdd:cd16952     87 RLLIASELGKGSRFTCLFP 105
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
571-687 1.47e-19

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: 85.30  E-value: 1.47e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLR--PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:cd17552      3 RILVIDDEEDIREVVQACLEklAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILL 82
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLD 687
Cdd:cd17552     83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
PRK11517 PRK11517
DNA-binding response regulator HprR;
571-686 2.03e-19

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 88.42  E-value: 2.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWDVTTAV-DGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTrdvPIVVLS 649
Cdd:PRK11517     2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVsDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT---PVICLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:PRK11517    79 ARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQL 115
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
410-516 2.13e-19

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: 84.40  E-value: 2.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  410 REMWEKIVLNLLSNAVK-FTAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFH--RVTGawarshEGTGIGLA 486
Cdd:cd16943      1 PSQLNQVLLNLLVNAAQaMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFttKPVG------EGTGLGLS 74
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785  487 LVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16943     75 LSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
572-672 3.02e-19

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: 84.35  E-value: 3.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRP-HWDVTTAVDGQAALELT---------RRGRFDLVLTDVMMPRLDGFGLIAALRADERTR 641
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNlGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1986385785  642 DVPIVVLSARAGEESAVEGLGAGADDYLVKP 672
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
416-516 3.49e-19

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 83.92  E-value: 3.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSNAVKFTAAGRV-VVRIGA--DAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWArsHEGTGIGLALVRELA 492
Cdd:cd16921      4 VLTNLLGNAIKFRRPRRPpRIEVGAedVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSREE--YEGTGVGLAIVRKII 81
                           90       100
                   ....*....|....*....|....
gi 1986385785  493 ELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16921     82 ERHGGRIWLESEPGEGTTFYFTLP 105
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
571-683 3.90e-19

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


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 88.70  E-value: 3.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVV 647
Cdd:COG5801      6 KVLIADDNREFCELLEEYLSSQPDmevVGVAYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLREMNLEKRPKVIM 85
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1986385785  648 LSARAGE---ESAVEglgAGADDYLVKPFSARDLIARVR 683
Cdd:COG5801     86 LTAFGQEditQRAVE---LGADYYILKPFDLDVLAERIR 121
PRK15479 PRK15479
transcriptional regulator TctD;
571-703 4.04e-19

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 87.47  E-value: 4.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVAR-LLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLS 649
Cdd:PRK15479     2 RLLLAEDNRELAHWLEKaLVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLR--KRGQTLPVLLLT 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQIISRLRGLV 703
Cdd:PRK15479    80 ARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSAGQVQEVQQLGELI 133
PRK09303 PRK09303
histidine kinase;
304-516 4.73e-19

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 90.78  E-value: 4.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  304 VSHEFRTPLT---LILGPLEDVLDDP---RLPALqRERLLPMQRNGLRLLKLVNTVLdfsrLESGR-----LRAEYRATD 372
Cdd:PRK09303   158 LAHDLRTPLTaasLALETLELGQIDEdteLKPAL-IEQLQDQARRQLEEIERLITDL----LEVGRtrweaLRFNPQKLD 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  373 LADYTWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAG-------------RVVVriga 439
Cdd:PRK09303   233 LGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGgtitlsmlhrttqKVQV---- 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  440 dagdavlSVEDTGVGIPADQQPLLFD---RFHRvtgawARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:PRK09303   309 -------SICDTGPGIPEEEQERIFEdrvRLPR-----DEGTEGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLP 376
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
572-684 5.20e-19

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: 83.65  E-value: 5.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtrDVPIVVLSA 650
Cdd:cd17594      2 VLVVDDDAAMRHLLILYLRERgFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS---DVPIIIISG 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  651 RAGEESA-VEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:cd17594     79 DRRDEIDrVVGLELGADDYLAKPFGLRELLARVRA 113
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
572-684 7.42e-19

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: 83.33  E-value: 7.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVL 648
Cdd:cd17535      1 VLIVDDHPLVREGLRRLLESEPDievVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLR--RRYPDLKVIVL 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:cd17535     79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRA 114
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
571-686 2.68e-18

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: 81.66  E-value: 2.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadeRTRDVPIVVLS 649
Cdd:cd17622      2 RILLVEDDPKLARLIADFLESHgFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLR---PKYQGPILLLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17622     79 ALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
572-687 3.51e-18

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: 81.61  E-value: 3.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLrpHWD------VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPI 645
Cdd:cd17536      1 VLIVDDEPLIREGLKKLI--DWEelgfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIR--ELYPDIKI 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1986385785  646 VVLSARAGEESAVEGLGAGADDYLVKPFSARDLIA---RVRANLD 687
Cdd:cd17536     77 IILSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEaleKAKEELD 121
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
304-516 3.61e-18

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: 89.26  E-value: 3.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  304 VSHEFRTPLTLILGPL----EDVLDDprlpalQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRlraeYRATDLADYTWR 379
Cdd:COG5809    277 IAHEIRNPLTSLKGFIqllkDTIDEE------QKTYLDIMLSELDRIESIISEFLVLAKPQAIK----YEPKDLNTLIEE 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  380 LASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTA-AGRVVVRIGADAGDAV-LSVEDTGVGIPA 457
Cdd:COG5809    347 VIPLLQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPeGGNITIETKAEDDDKVvISVTDEGCGIPE 426
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785  458 DQQPLLFDRFhrvtgaWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG5809    427 ERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLP 479
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
386-516 3.62e-18

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 87.98  E-value: 3.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  386 SAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAvkFTAA-------GRVVVRIGADAGDAVLSVEDTGVGIPAD 458
Cdd:COG3290    255 ARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNA--IEAVeklpeeeRRVELSIRDDGDELVIEVEDSGPGIPEE 332
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1986385785  459 QQPLLFDRfhrvtGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG3290    333 LLEKIFER-----GFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLP 385
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
568-714 3.68e-18

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: 83.85  E-value: 3.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  568 RPGRILLADDNADLRDHVARLLR--PHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGfglIAALRADERTRDVPI 645
Cdd:COG3707      2 RGLRVLVVDDEPLRRADLREGLReaGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDG---LEAARQISEERPAPV 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  646 VVLSARAGEESAVEGLGAGADDYLVKPFSARDLiarvRANLDLGQARRQIISRLRGLVDTA-AALNTVRT 714
Cdd:COG3707     79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDL----LPALELALARFRELRALRRELAKLrEALEERKL 144
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
571-684 4.82e-18

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 84.38  E-value: 4.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLS 649
Cdd:PRK10161     4 RILVVEDEAPIREMVCFVLEQNgFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:PRK10161    84 ARGEEEDRVRGLETGADDYITKPFSPKELVARIKA 118
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
571-686 6.18e-18

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 80.50  E-value: 6.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLrdhvARLLRPH-----WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadeRTRDVPI 645
Cdd:cd19938      1 RILIVEDEPKL----AQLLIDYlraagYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR---RFSDVPI 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1986385785  646 VVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd19938     74 IMVTARVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
572-678 6.92e-18

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: 80.36  E-value: 6.92e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRP-HWDVTTAVDGQAALELTR--RGRFDLVLTDVMMPRLDGFGLIAALRADertRDVPIVVL 648
Cdd:cd17584      1 VLVVDDDPTCLAILKRMLLRcGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIRLE---MDLPVIMM 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDL 678
Cdd:cd17584     78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
416-516 8.45e-18

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: 80.02  E-value: 8.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSNAVKFTAA-----GRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRfhrvtGAWARSHEGTGIGLALVRE 490
Cdd:cd16915      4 IVGNLIDNALDALAAtgapnKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLALVRQ 78
                           90       100
                   ....*....|....*....|....*.
gi 1986385785  491 LAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16915     79 SVERLGGSITVESEPGGGTTFSIRIP 104
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
572-684 1.14e-17

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: 79.76  E-value: 1.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrDVPIVVLSAR 651
Cdd:cd17616      2 LLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKV--KTPILILSGL 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1986385785  652 AGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:cd17616     80 ADIEDKVKGLGFGADDYMTKPFHKDELVARIHA 112
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
571-684 1.82e-17

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: 81.50  E-value: 1.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLS 649
Cdd:COG4567      6 SLLLVDDDEAFARVLARALERRgFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALR--ERDPDARIVVLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:COG4567     84 GYASIATAVEAIKLGADDYLAKPADADDLLAALER 118
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
304-516 1.95e-17

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 86.76  E-value: 1.95e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  304 VSHEFRTPLTLILGPLEDVLDdpRLPALQRERLLP--MQRNGLRLLKLVNTVLDFSRleSGRLRaeYRATDLADYTWRLA 381
Cdd:PRK10364   244 VAHEIRNPLSSIKGLAKYFAE--RAPAGGEAHQLAqvMAKEADRLNRVVSELLELVK--PTHLA--LQAVDLNDLINHSL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  382 STFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVVVRIGADAGDAV-LSVEDTGVGIPADQQ 460
Cdd:PRK10364   318 QLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVkISVTDSGKGIAADQL 397
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1986385785  461 PLLFDRFHRVTGawarshEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:PRK10364   398 EAIFTPYFTTKA------EGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLP 447
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-514 2.63e-17

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: 78.60  E-value: 2.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  402 LSAPVYV--DREMWEKIVLNLLSNAVKFTAAG-RVVVRIGADAGdAVLSVEDTGVGIPADQQPLLFDRFHRVTGawaRSH 478
Cdd:cd16940      1 SAADIQVqgDALLLFLLLRNLVDNAVRYSPQGsRVEIKLSADDG-AVIRVEDNGPGIDEEELEALFERFYRSDG---QNY 76
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  479 EGTGIGLALVRELAELHGGSASAASEPGRGSVFTVR 514
Cdd:cd16940     77 GGSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVR 112
PRK10604 PRK10604
sensor protein RstB; Provisional
303-520 3.06e-17

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 85.81  E-value: 3.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  303 NVSHEFRTPLTLILGPLE--DVLDDPRLPALQRERLlpmqrnglRLLKLVNTVLDFSRLESGRLRAEYRATDLADYTWRL 380
Cdd:PRK10604   218 GIAHELRTPLVRLRYRLEmsDNLSAAESQALNRDIG--------QLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTH 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  381 ASTFRSAaeRAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFtAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQ 460
Cdd:PRK10604   290 LADIQAV--TPEKTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRY-AHSRVRVSLLLDGNQACLIVEDDGPGIPPEER 366
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  461 PLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFGTA 520
Cdd:PRK10604   367 ERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPVWHN 426
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
572-672 3.45e-17

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: 78.19  E-value: 3.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHV-ARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSA 650
Cdd:cd19927      1 ILLVDDDPGIRLAVkDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                           90       100
                   ....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKP 672
Cdd:cd19927     81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
571-672 3.64e-17

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: 78.40  E-value: 3.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLS 649
Cdd:cd17555      2 TILVIDDDEVVRESIAAYLEDSgFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQIT--KESPDTPVIVVS 79
                           90       100
                   ....*....|....*....|...
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKP 672
Cdd:cd17555     80 GAGVMSDAVEALRLGAWDYLTKP 102
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
571-688 5.49e-17

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 81.40  E-value: 5.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVV 647
Cdd:COG3279      3 KILIVDDEPLARERLERLLEKYPDlevVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLR--ELDPPPPIIF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1986385785  648 LSARagEESAVEGLGAGADDYLVKPFSARDL---IARVRANLDL 688
Cdd:COG3279     81 TTAY--DEYALEAFEVNAVDYLLKPIDEERLakaLEKAKERLEA 122
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
572-694 5.90e-17

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: 78.12  E-value: 5.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSAR 651
Cdd:cd17539      1 VLLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVADP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1986385785  652 AGEESAVEGLGAGADDYLVKPFSARDLIARVRAnldlgQARRQ 694
Cdd:cd17539     81 GDRGRLIRALEIGVNDYLVRPIDPNELLARVRT-----QIRRK 118
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
1051-1162 1.01e-16

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 77.71  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1051 LPAEPGRLSVLRRRLEDFLTGNGVPDDDVFDLTVAVSEAAANAIEH--PVDPVEPVItVEASLVDGAVVITVRDSGRW-- 1126
Cdd:pfam13581    1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHayREGPEGPVE-VRLTSDGGGLVVTVADSGPPfd 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1986385785 1127 ----------RETAAEGFRGRGLALIGALS-ELSVSRSDSGTSVTLR 1162
Cdd:pfam13581   80 pltlpppdleEPDEDRKEGGRGLALIRGLMdDVEYTRGGEGNTVRMR 126
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
571-678 1.03e-16

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: 77.19  E-value: 1.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWDVTT--AVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVL 648
Cdd:cd17593      2 KVLICDDSSMARKQLARALPADWDVEItfAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALP--VEQLETKVIVV 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDL 678
Cdd:cd17593     80 SGDVQPEAKERVLELGALAFLKKPFDPEKL 109
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
571-673 1.63e-16

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 76.49  E-value: 1.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVV 647
Cdd:cd17561      3 KVLIADDNREFVQLLEEYLNSQPDmevVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIM 82
                           90       100
                   ....*....|....*....|....*.
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKPF 673
Cdd:cd17561     83 LTAFGQEDITQRAVELGASYYILKPF 108
cztR_silR_copR TIGR01387
heavy metal response regulator; Members of this family contain a response regulator receiver ...
572-702 2.03e-16

heavy metal response regulator; Members of this family contain a response regulator receiver domain (pfam00072) and an associated transcriptional regulatory region (pfam00486). 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. Most members encoded by genes adjacent to genes for encoding a member of the heavy metal sensor histidine kinase family (TIGRFAMs:TIGR01386), its partner in the two-component response regulator system. [Regulatory functions, DNA interactions]


Pssm-ID: 130454 [Multi-domain]  Cd Length: 218  Bit Score: 79.46  E-value: 2.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVAR-LLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRdvPIVVLSA 650
Cdd:TIGR01387    1 ILVVEDEQKTAEYLQQgLSESGYVVDAASNGRDGLHLALKDDYDLIILDVMLPGMDGWQILQTLRRSGKQT--PVLFLTA 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQIISRLRGL 702
Cdd:TIGR01387   79 RDSVADKVKGLDLGADDYLVKPFSFSELLARVRTLLRRSHSLNSTVLEIADL 130
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
572-683 2.40e-16

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: 76.00  E-value: 2.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLSA 650
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIK--EKYPDLPVIMISG 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd17550     79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIE 111
PRK10610 PRK10610
chemotaxis protein CheY;
571-678 2.65e-16

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 76.55  E-value: 2.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRP--HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:PRK10610     7 KFLVVDDFSTMRRIVRNLLKElgFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDL 678
Cdd:PRK10610    87 TAEAKKENIIAAAQAGASGYVVKPFTAATL 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
572-672 3.25e-16

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 75.28  E-value: 3.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadeRTRDVPIVVLSA 650
Cdd:cd17620      1 ILVIEDEPQIRRFLRTALEAHgYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSA 77
                           90       100
                   ....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKP 672
Cdd:cd17620     78 RDEESDKIAALDAGADDYLTKP 99
pleD PRK09581
response regulator PleD; Reviewed
569-693 5.86e-16

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 81.87  E-value: 5.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  569 PGRILLADDNADLRDHVARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:PRK09581   155 DGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLL 234
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVRAnldlgQARR 693
Cdd:PRK09581   235 VDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRT-----QIRR 274
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
572-686 5.97e-16

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: 74.88  E-value: 5.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHWDVT---TAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrdVPIVVL 648
Cdd:cd17532      1 ALIVDDEPLAREELRYLLEEHPDIEivgEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAK---PPLIVF 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1986385785  649 sARAGEESAVEGLGAGADDYLVKPFSARDL---IARVRANL 686
Cdd:cd17532     78 -VTAYDEYAVEAFELNAVDYLLKPFSEERLaeaLAKLRKRL 117
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
296-362 8.72e-16

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 72.63  E-value: 8.72e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986385785  296 AKTNFFSNVSHEFRTPLTLILGPLEdVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESG 362
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLE-LLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
571-683 9.41e-16

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 74.75  E-value: 9.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWDVT--TAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:cd17575      2 MVLLVDDQAIIGEAVRRALADEEDIDfhYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVL 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd17575     82 STKEEPEVKSEAFALGANDYLVKLPDKIELVARIR 116
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
414-516 9.84e-16

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: 73.97  E-value: 9.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  414 EKIVLNLLSNAVKFTAAGRV-----VVRIGADAGDAV-LSVEDTGVGIPADQQPLLFDRFHrVTGAwarshEGTGIGLAL 487
Cdd:cd16920      2 QQVLINLVRNGIEAMSEGGCerrelTIRTSPADDRAVtISVKDTGPGIAEEVAGQLFDPFY-TTKS-----EGLGMGLSI 75
                           90       100
                   ....*....|....*....|....*....
gi 1986385785  488 VRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16920     76 CRSIIEAHGGRLSVESPAGGGATFQFTLP 104
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
572-700 1.69e-15

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: 74.06  E-value: 1.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLSA 650
Cdd:cd17549      1 VLLVDDDADVREALQQTLELAgFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIR--ELDPDLPVILITG 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDlgqARRQII--SRLR 700
Cdd:cd17549     79 HGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALE---KRRLVLenRRLR 127
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
571-702 2.29e-15

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 80.28  E-value: 2.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLS 649
Cdd:PRK11361     6 RILIVDDEDNVRRMLSTAFaLQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMR--SHETRTPVILMT 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQIISRLRGL 702
Cdd:PRK11361    84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQAL 136
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
419-516 3.49e-15

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: 72.36  E-value: 3.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  419 NLLSNAVKFtAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGS 498
Cdd:cd16949      7 NVLRNALRY-SPSKILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIEQHGGK 85
                           90
                   ....*....|....*...
gi 1986385785  499 ASAASEPGRGSVFTVRVP 516
Cdd:cd16949     86 IKASNRKPGGLRVRIWLP 103
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
571-683 3.53e-15

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: 72.80  E-value: 3.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERtrdVPIVVLS 649
Cdd:cd17619      2 HILIVEDEPVTRATLKSYFEQEgYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE---VGIILVT 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd17619     79 GRDDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
571-683 4.12e-15

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


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 76.76  E-value: 4.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVV 647
Cdd:TIGR02875    4 RIVIADDNKEFCNLLKEYLAAQPDmevVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARPRVIM 83
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:TIGR02875   84 LSAFGQEKITQRAVALGADYYVLKPFDLEILAARIR 119
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
572-672 4.68e-15

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 71.71  E-value: 4.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtrDVPIVVLSA 650
Cdd:cd19936      1 IALVDDDRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS---TLPVIFLTS 77
                           90       100
                   ....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKP 672
Cdd:cd19936     78 KDDEIDEVFGLRMGADDYITKP 99
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
296-362 5.31e-15

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 70.67  E-value: 5.31e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986385785   296 AKTNFFSNVSHEFRTPLTLILGPLEdVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESG 362
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLE-LLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
571-680 6.85e-15

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: 72.06  E-value: 6.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRP--HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGfglIAALRADERTRDVPIVVL 648
Cdd:cd19932      2 RVLIAEDEALIRMDLREMLEEagYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDG---IEAAKIITSENIAPIVLL 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIA 680
Cdd:cd19932     79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIP 110
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
419-516 9.87e-15

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: 70.88  E-value: 9.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  419 NLLSNAVKFtAAGRVVVRIGADAGDAVLSVEDTGVG-IPADQQP-LLFDRFHRvtGAWARSHEGTGIGLALVRELAELHG 496
Cdd:cd16923      7 NLLSNAIKY-SPENTRIYITSFLTDDVVNIMFKNPSsHPLDFKLeKLFERFYR--GDNSRNTEGAGLGLSIAKAIIELHG 83
                           90       100
                   ....*....|....*....|
gi 1986385785  497 GSASAASEpGRGSVFTVRVP 516
Cdd:cd16923     84 GSASAEYD-DNHDLFKVRLP 102
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
413-516 1.44e-14

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: 70.78  E-value: 1.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  413 WEKIVLN-LLSNAVKFTA-AGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHrvTGAWAR-SHEGTGIGLALVR 489
Cdd:cd16948      5 WLSFIIGqIVSNALKYSKqGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGF--TGENGRnFQESTGMGLYLVK 82
                           90       100
                   ....*....|....*....|....*..
gi 1986385785  490 ELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16948     83 KLCDKLGHKIDVESEVGEGTTFTITFP 109
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
405-513 1.61e-14

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: 71.39  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  405 PVY--VDREMWEKIVLNLLSNAVKFTAAGRVV-VRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGT 481
Cdd:cd16947     11 PIYanANTEALQRILKNLISNAIKYGSDGKFLgMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGN 90
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1986385785  482 GIGLALVRELAELHGGSASAASEPGRGSVFTV 513
Cdd:cd16947     91 GLGLTITKRLAESMGGSIYVNSKPYEKTVFTV 122
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
562-686 2.17e-14

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 73.95  E-value: 2.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  562 PPPAGRRPGRILLADDNADLrdhvARLL---------RPHWdvttAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIA 632
Cdd:PRK10710     3 ELPIDENTPRILIVEDEPKL----GQLLidylqaasyATTL----LSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCR 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1986385785  633 ALRadeRTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:PRK10710    75 EIR---RFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTIL 125
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
571-683 2.19e-14

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 70.39  E-value: 2.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH--WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGfglIAALRA-DERTRDVPIVV 647
Cdd:cd17542      2 KVLIVDDAAFMRMMLKDILTKAgyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDG---IEALKEiKKIDPNAKVIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd17542     79 CSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVE 114
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
414-516 3.48e-14

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 69.77  E-value: 3.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  414 EKIVLNLLSNAVKFtAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAE 493
Cdd:cd16939      2 ARALDNLLRNALRY-AHRTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVAL 80
                           90       100
                   ....*....|....*....|...
gi 1986385785  494 LHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16939     81 WHGGHVECDDSELGGACFRLTWP 103
PRK10337 PRK10337
sensor protein QseC; Provisional
300-514 3.92e-14

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 76.23  E-value: 3.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  300 FFSNVSHEFRTPLTLILGPLEDV---LDDPRLpalqRERLLPMQRNGL-RLLKLVNTVLDFSRLESGRLRAEYRATDLAD 375
Cdd:PRK10337   240 FTSDAAHELRSPLAALKVQTEVAqlsDDDPQA----RKKALLQLHAGIdRATRLVDQLLTLSRLDSLDNLQDVAEIPLED 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  376 YTWRLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAGRVV-VRIGADAgdavLSVEDTGVG 454
Cdd:PRK10337   316 LLQSAVMDIYHTAQQAGIDVRLTLNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSVVdVTLNARN----FTVRDNGPG 391
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  455 IPADQQPLLFDRFHRVTGawaRSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVR 514
Cdd:PRK10337   392 VTPEALARIGERFYRPPG---QEATGSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKVS 448
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
294-358 4.08e-14

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: 68.01  E-value: 4.08e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  294 DQAKTNFFSNVSHEFRTPLTLILGPLEDVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSR 358
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
572-686 6.03e-14

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 69.16  E-value: 6.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAdeRTRDVPIVVLSA 650
Cdd:cd17537      3 VYVVDDDEAVRDSLAFLLRSVgLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLA--RGSNIPIIFITG 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17537     81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
571-680 6.89e-14

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: 69.01  E-value: 6.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVAR-LLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLS 649
Cdd:cd17563      2 SLLLVDDDEVFAERLARaLERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLR--ALQPDARIVVLT 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIA 680
Cdd:cd17563     80 GYASIATAVEAIKLGADDYLAKPADADEILA 110
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
571-691 8.09e-14

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 72.26  E-value: 8.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVAR-LLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAdeRTRDVPIVVLS 649
Cdd:PRK09836     2 KLLIVEDEKKTGEYLTKgLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLLT 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQA 691
Cdd:PRK09836    80 ALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAA 121
PRK10816 PRK10816
two-component system response regulator PhoP;
571-684 1.10e-13

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 71.69  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRP--HwDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTrdVPIVVL 648
Cdd:PRK10816     2 RVLVVEDNALLRHHLKVQLQDagH-QVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVL 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:PRK10816    79 TARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQA 114
PRK10643 PRK10643
two-component system response regulator PmrA;
595-684 1.16e-13

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 71.61  E-value: 1.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  595 VTTAVDGQAALELtrrGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFS 674
Cdd:PRK10643    30 ASTAREAEALLES---GHYSLVVLDLGLPDEDGLHLLRRWR--QKKYTLPVLILTARDTLEDRVAGLDVGADDYLVKPFA 104
                           90
                   ....*....|
gi 1986385785  675 ARDLIARVRA 684
Cdd:PRK10643   105 LEELHARIRA 114
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
572-682 2.12e-13

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: 67.46  E-value: 2.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHW---DVTTAV-DGQAALELTRrgrFDLVLTDVMMPRLDGFGLIAalRADERTRDVPIVV 647
Cdd:cd17573      1 ILLIEDDSTLGKEISKGLNEKGyqaDVAESLkDGEYYIDIRN---YDLVLVSDKLPDGNGLSIVS--RIKEKHPSIVVIV 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKPFSARDLIARV 682
Cdd:cd17573     76 LSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
572-672 2.19e-13

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: 67.43  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRP-HWDVTTAVDGQAALEL--TRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:cd17582      1 VLLVENDDSTRQIVTALLRKcSYEVTAASDGLQAWDVleDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                           90       100
                   ....*....|....*....|....
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKP 672
Cdd:cd17582     81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
572-672 2.21e-13

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: 67.22  E-value: 2.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAderTRDVPIVVLSA 650
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEgFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA---RSNVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKP 672
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
570-683 2.95e-13

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: 67.30  E-value: 2.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  570 GRILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVL 648
Cdd:cd19919      1 KTVWIVDDDSSIRWVLERALaGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIK--QRHPDLPVIIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd19919     79 TAHSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVE 113
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
302-516 4.12e-13

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 73.04  E-value: 4.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  302 SNVSHEFRTPLTlilgpledvlddpRLpalQRERLLPMQRNG------------LRLLKLVNTVLDFSR--LESGRLRAE 367
Cdd:PRK09470   248 SDISHELRTPLT-------------RL---QLATALLRRRQGeskelerieteaQRLDSMINDLLVLSRnqQKNHLERET 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  368 YRATDLADYTWRLAStFRsaAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAgRVVVRIGADAGDAVLS 447
Cdd:PRK09470   312 FKANSLWSEVLEDAK-FE--AEQMGKSLTVSAPPGPWPINGNPNALASALENIVRNALRYSHT-KIEVAFSVDKDGLTIT 387
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785  448 VEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:PRK09470   388 VDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEDSPLGGLRLTIWLP 456
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
571-683 5.05e-13

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: 66.48  E-value: 5.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRdhvaRLLRPH-----WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPI 645
Cdd:cd17554      2 KILVVDDEENIR----ELYKEEledegYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR--EKKPDLPV 75
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1986385785  646 VVLSARAGEESAVEGLgaGADDYLVKPFSARDLIARVR 683
Cdd:cd17554     76 IICTAYSEYKSDFSSW--AADAYVVKSSDLTELKETIK 111
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
1084-1162 5.61e-13

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 65.75  E-value: 5.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1084 VAVSEAAANAIEH-PVDPVEPVITVEASLVDGAVVITVRDSGRWR---------ETAAEGfrGRGLALIGALS-ELSVSR 1152
Cdd:cd16936      3 LAVSEAVTNAVRHaYRHDGPGPVRLELDLDPDRLRVEVTDSGPGFdplrpadpdAGLREG--GRGLALIRALMdEVGYRR 80
                           90
                   ....*....|
gi 1986385785 1153 SDSGTSVTLR 1162
Cdd:cd16936     81 TPGGKTVWLE 90
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
572-693 6.05e-13

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: 66.45  E-value: 6.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLrdhvARL----LRP-HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIV 646
Cdd:cd17572      1 VLLVEDSPSL----AALyqeyLSDeGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQ--ERSLPTSVI 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1986385785  647 VLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARR 693
Cdd:cd17572     75 VITAHGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK 121
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
299-516 1.18e-12

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: 72.47  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  299 NFFSNVSHEFRTPLTLILGPLEDvLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAEYRATDLADYTW 378
Cdd:TIGR03785  487 NMSSRLSHELRTPVAVVRSSLEN-LELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLS 565
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  379 RLASTFRSAAERAGLELVVETPPLsaPVYVDREMWEKIVLNLLSNAVKFTAAGRVV-VRIGADAGDAVLSVEDTGVGIPA 457
Cdd:TIGR03785  566 GCMQGYQMTYPPQRFELNIPETPL--VMRGSPELIAQMLDKLVDNAREFSPEDGLIeVGLSQNKSHALLTVSNEGPPLPE 643
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  458 DQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEP-GRGSVFTVRVP 516
Cdd:TIGR03785  644 DMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
571-683 1.19e-12

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 65.50  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRP-HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAalRADERTRDVPIVVLS 649
Cdd:cd17569      2 TILLVDDEPNILKALKRLLRReGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLK--RVRERYPDTVRILLT 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  650 ARAGEESAVEGLGAGA-DDYLVKPFSARDLIARVR 683
Cdd:cd17569     80 GYADLDAAIEAINEGEiYRFLTKPWDDEELKETIR 114
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
415-516 1.21e-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: 65.29  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  415 KIVLNLLSNAVKFT--AAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELA 492
Cdd:cd16953      3 QVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISRQII 82
                           90       100
                   ....*....|....*....|....*...
gi 1986385785  493 ELHGGSASAA--SEPG--RGSVFTVRVP 516
Cdd:cd16953     83 EAHGGISVAEnhNQPGqvIGARFTVQLP 110
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
571-708 2.23e-12

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 69.79  E-value: 2.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGfglIAALRADERTRDVPIVV 647
Cdd:PRK00742     5 RVLVVDDSAFMRRLISEILNSDPDievVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDG---LDALEKIMRLRPTPVVM 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1986385785  648 LSA--RAGEESAVEGLGAGADDYLVKPFS---------ARDLIARVRAnldLGQARRQIISRLRGLVDTAAA 708
Cdd:PRK00742    82 VSSltERGAEITLRALELGAVDFVTKPFLgislgmdeyKEELAEKVRA---AARARVRALPPRAAAAARAAA 150
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
414-516 3.06e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 64.34  E-value: 3.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  414 EKIVLNLLSNAVKFTAA--GRVVVRIGADAG----------DAVLSVEDTGVGIPADQQPLLFDRFhrVTGawarSHEGT 481
Cdd:cd16918      2 IQVFLNLVRNAAQALAGsgGEIILRTRTQRQvtlghprhrlALRVSVIDNGPGIPPDLQDTIFYPM--VSG----RENGT 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  482 GIGLALVRELAELHGGSASAASEPGRgSVFTVRVP 516
Cdd:cd16918     76 GLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
414-506 4.15e-12

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: 63.63  E-value: 4.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  414 EKIVLNLLSNAVKFT-AAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVtgawARSHEG---TGIGLALVR 489
Cdd:cd16945      6 RQAINNLLDNAIDFSpEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSL----PRPHSGqksTGLGLAFVQ 81
                           90
                   ....*....|....*..
gi 1986385785  490 ELAELHGGSASAASEPG 506
Cdd:cd16945     82 EVAQLHGGRITLRNRPD 98
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
572-686 4.19e-12

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: 63.84  E-value: 4.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRP-HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAderTRDVPIVVLSA 650
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFISS 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd18159     78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
571-623 4.38e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.82  E-value: 4.38e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1986385785   571 RILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMP 623
Cdd:smart00448    2 RILVVDDDPLLRELLKALLeKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
415-508 7.36e-12

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: 62.85  E-value: 7.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  415 KIVLNLLSNAVKFtAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRvtGAWARSHEGTGIGLALVRELAEL 494
Cdd:cd16950      3 RVLSNLVDNALRY-GGGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYR--GDNARGTSGTGLGLAIVQRISDA 79
                           90
                   ....*....|....
gi 1986385785  495 HGGSASAASEPGRG 508
Cdd:cd16950     80 HGGSLTLANRAGGG 93
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
572-683 9.25e-12

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: 63.06  E-value: 9.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:cd19930      1 VLIAEDQEMVRGALAALLELEDDlevVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1986385785  649 SARAGE-ESAVEglgAGADDYLVKPFSARDLIARVR 683
Cdd:cd19930     81 FGRPGYfRRALA---AGVDGYVLKDRPIEELADAIR 113
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
414-513 9.41e-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: 62.47  E-value: 9.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  414 EKIVLNLLSNAvkFTAAGRVV---VRIGAD--AGDAVLSVEDTGVGIPADQQPLLFDRFH--RVTGawarshEGTGIGLA 486
Cdd:cd16976      2 QQVLMNLLQNA--LDAMGKVEnprIRIAARrlGGRLVLVVRDNGPGIAEEHLSRVFDPFFttKPVG------KGTGLGLS 73
                           90       100
                   ....*....|....*....|....*..
gi 1986385785  487 LVRELAELHGGSASAASEPGRGSVFTV 513
Cdd:cd16976     74 ISYGIVEEHGGRLSVANEEGAGARFTF 100
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
363-520 1.31e-11

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 66.18  E-value: 1.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  363 RLRAEYRATDLADYTWR--LASTFRSAAERAGLELVVETPPlsAPVYVDREMWE---KIVLNLLSNAVKFTAAGRVVVRI 437
Cdd:COG4585    110 RLVRGLRPPALDDLGLAaaLEELAERLLRAAGIRVELDVDG--DPDRLPPEVELalyRIVQEALTNALKHAGATRVTVTL 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  438 GADAGDAVLSVEDTGVGIPADQQPllfdrfhrvtgawarsheGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPF 517
Cdd:COG4585    188 EVDDGELTLTVRDDGVGFDPEAAP------------------GGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPL 249

                   ...
gi 1986385785  518 GTA 520
Cdd:COG4585    250 AAA 252
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
569-684 1.48e-11

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 65.05  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  569 PGRILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPI 645
Cdd:PRK10651     6 PATILLIDDHPMLRTGVKQLISMAPDitvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLR--EKSLSGRI 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1986385785  646 VVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRA 684
Cdd:PRK10651    84 VVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQ 122
envZ PRK09467
osmolarity sensor protein; Provisional
387-498 1.49e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 68.01  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  387 AAERAGLELVVET--PPLSAPVYVDREMWEKIVLNLLSNAVKFTAaGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLF 464
Cdd:PRK09467   304 IAAESGYEREIETalQPGPIEVPMNPIAIKRALANLVVNAARYGN-GWIKVSSGTEGKRAWFQVEDDGPGIPPEQLKHLF 382
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  465 DRFHRvtGAWARSHEGTGIGLALVRELAELHGGS 498
Cdd:PRK09467   383 QPFTR--GDSARGSSGTGLGLAIVKRIVDQHNGK 414
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
614-686 1.60e-11

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 65.21  E-value: 1.60e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  614 DLVLTDVMMPRLDGFGLIAALRadeRTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:PRK10529    47 DLIILDLGLPDGDGIEFIRDLR---QWSAIPVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVAL 116
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
380-514 1.67e-11

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: 63.03  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  380 LASTFRSAAERAGLELVVETPPlSAPVYVDREMWEKIVLNLLSNAVKFtAAGRVVVRIGADAGDAVLSVEDTGVGIPADQ 459
Cdd:cd16954      6 LCSALNKVYQRKGVSISLDISP-ELRFPGERNDLMELLGNLLDNACKW-CLEFVEVTARQTDGGLHLIVDDDGPGVPESQ 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  460 QPLLFDRFHRVTgawaRSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVR 514
Cdd:cd16954     84 RSKIFQRGQRLD----EQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVV 134
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
571-634 4.89e-11

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: 61.45  E-value: 4.89e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAAL 634
Cdd:COG2197      3 RVLIVDDHPLVREGLRALLEAEPDievVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK10336 PRK10336
two-component system response regulator QseB;
571-695 7.34e-11

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 63.38  E-value: 7.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHV-ARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLS 649
Cdd:PRK10336     2 RILLIEDDMLIGDGIkTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWR--EKGQREPVLILT 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDL--GQARRQI 695
Cdd:PRK10336    80 ARDALAERVEGLRLGADDYLCKPFALIEVAARLEALMRRtnGQASNEL 127
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
572-673 1.00e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 65.44  E-value: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRP-HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTrdVPIVVLSA 650
Cdd:PRK10365     8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPA--IPVLIMTA 85
                           90       100
                   ....*....|....*....|...
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKPF 673
Cdd:PRK10365    86 YSSVETAVEALKTGALDYLIKPL 108
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
572-672 1.12e-10

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: 59.47  E-value: 1.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVA-RLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPrlDGFGLIAALRADERTRDVPIVVLSA 650
Cdd:cd19926      1 VLVVDDEPDIRELLEiTLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLP--DGSGLELVQHIQQRLPQTPVAVITA 78
                           90       100
                   ....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKP 672
Cdd:cd19926     79 YGSLDTAIEALKAGAFDFLTKP 100
PRK15369 PRK15369
two component system response regulator;
571-739 1.69e-10

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 62.02  E-value: 1.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLR--PHWDVTTAV-DGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVV 647
Cdd:PRK15369     5 KILLVDDHELIINGIKNMLApyPRYKIVGQVdNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLH--QRWPAMNILV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  648 LSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRA----------NLDlgqarRQIISRLRGLVDTAAALNTVRTTaE 717
Cdd:PRK15369    83 LTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTvavgkryidpALN-----REAILALLNADDTNPPLLTPRER-Q 156
                          170       180
                   ....*....|....*....|..
gi 1986385785  718 VLDVAAQHVRAMTTAGRVVVSV 739
Cdd:PRK15369   157 ILKLITEGYTNRDIAEQLSISI 178
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
416-516 1.80e-10

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: 58.33  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSNAVKFTAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPllfdrfhrvtgawarshEGTGIGLALVRELAELH 495
Cdd:cd16917      4 IVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPP-----------------GGGGFGLLGMRERAELL 66
                           90       100
                   ....*....|....*....|.
gi 1986385785  496 GGSASAASEPGRGSVFTVRVP 516
Cdd:cd16917     67 GGTLTIGSRPGGGTRVTARLP 87
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
572-672 3.36e-10

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: 58.28  E-value: 3.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPrlDGFGLIAALRADERTRDVPIVVLSA 650
Cdd:cd19928      1 ILVADDDRAIRTVLTQALgRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMP--DENGLDLIPRIKKARPDLPIIVMSA 78
                           90       100
                   ....*....|....*....|..
gi 1986385785  651 RAGEESAVEGLGAGADDYLVKP 672
Cdd:cd19928     79 QNTLMTAVKAAERGAFEYLPKP 100
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
572-678 5.62e-10

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 58.15  E-value: 5.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHWDVTTAVD-GQAALELTRRGR-----------FDLVLTDVMMPRLDGFGLIAALRADER 639
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLRISSCRVTAVDsGKRALEFLGLEDeedssnfnepkVNMIITDYCMPGMTGYDLLKKVKESSA 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1986385785  640 TRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDL 678
Cdd:cd17581     81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADV 119
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
571-673 7.93e-10

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 57.13  E-value: 7.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLR-DHVARLLRPHWDVTTAVDGQAALELTRRGR-FDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVL 648
Cdd:cd18160      1 TILLADDEPSVRkFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREAR--KIDPDVKILFI 78
                           90       100
                   ....*....|....*....|....*
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPF 673
Cdd:cd18160     79 SGGAAAAPELLSDAVGDNATLKKPF 103
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
571-681 1.18e-09

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 57.25  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADL----RDHVARLlrPHWDVT-TAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVpI 645
Cdd:cd19925      2 NVLIVEDDPMVaeihRAYVEQV--PGFTVIgTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDV-I 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  646 VVLSARagEESAV-EGLGAGADDYLVKPFSARDLIAR 681
Cdd:cd19925     79 VVTAAN--DVETVrEALRLGVVDYLIKPFTFERLRQR 113
PRK13856 PRK13856
two-component response regulator VirG; Provisional
572-710 2.21e-09

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 59.44  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtrDVPIVVLS- 649
Cdd:PRK13856     4 VLVIDDDVAMRHLIVEYLTIHaFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATKS---DVPIIIISg 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL--------------------DLGQARRQIISRLRGLVD-TAAA 708
Cdd:PRK13856    81 DRLEEADKVVALELGATDFIAKPFGTREFLARIRVALrvrpnvvrtkdrrsfcfadwTLNLRQRRLISEAGGEVKlTAGE 160

                   ..
gi 1986385785  709 LN 710
Cdd:PRK13856   161 FN 162
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
572-683 3.05e-09

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: 55.82  E-value: 3.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHWDVTT---AVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVL 648
Cdd:cd19931      1 VLLIDDHPLLRKGIKQLIELDPDFTVvgeASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALR--EEGVSARIVIL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVR 683
Cdd:cd19931     79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALK 113
PRK15115 PRK15115
response regulator GlrR; Provisional
567-698 4.71e-09

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 60.24  E-value: 4.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  567 RRPGRILLADDNADLRDHVA-RLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPI 645
Cdd:PRK15115     3 RKPAHLLLVDDDPGLLKLLGmRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQ--KVQPGMPV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785  646 VVLSARAGEESAVEGLGAGADDYLVKP------FSARDLIARVRANLDLGQARRQIISR 698
Cdd:PRK15115    81 IILTAHGSIPDAVAATQQGVFSFLTKPvdrdalYKAIDDALEQSAPATDERWREAIVTR 139
PRK10766 PRK10766
two-component system response regulator TorR;
571-686 5.30e-09

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 57.74  E-value: 5.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRdhvARLL----RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAderTRDVPIV 646
Cdd:PRK10766     4 HILVVEDEPVTR---ARLQgyfeQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS---RSTVGII 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1986385785  647 VLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRaNL 686
Cdd:PRK10766    78 LVTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVK-NL 116
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
571-680 8.49e-09

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: 54.72  E-value: 8.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRpHW--DVT-TAVDGQAALELTRRGRFDLVLTDVMMP-RLDGfglIAALRADERTRDVPIV 646
Cdd:cd17534      2 KILIVEDEAIIALDLKEILE-SLgyEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDG---IEAAREIREKFDIPVI 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  647 VLSARAGE---ESAVEglgAGADDYLVKPFSARDLIA 680
Cdd:cd17534     78 FLTAYSDEetlERAKE---TNPYGYLVKPFNERELKA 111
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
420-519 1.02e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 58.88  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  420 LLSNAVKF-----TAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFhrvtgawARSHEGTGIGLALVRE-LAE 493
Cdd:COG2972    344 LVENAIEHgiepkEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEEL-------SSKGEGRGIGLRNVRErLKL 416
                           90       100
                   ....*....|....*....|....*...
gi 1986385785  494 LHGGSA--SAASEPGRGSVFTVRVPFGT 519
Cdd:COG2972    417 YYGEEYglEIESEPGEGTTVTIRIPLEE 444
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
406-516 1.25e-08

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: 58.97  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  406 VYVDREMWEKIVLNLLSNAVK-FTAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFhrvtgaWARSHEGTGIG 484
Cdd:COG5805    389 IYCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLKKLGEPF------FTTKEKGTGLG 462
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1986385785  485 LALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG5805    463 LMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
571-719 3.39e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 56.81  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLL--RPHWDVT-TAVDGQAALELTRRGRFDLVLTDVMMPRLDGfglIAALRADERTRDVPIVV 647
Cdd:PRK12555     2 RIGIVNDSPLAVEALRRALarDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDG---VEATRRIMAERPCPILI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  648 LSA--RAGEESAVEGLGAGADDYLVKPF---------SARDLIARVRanldlgQARRQIISRLRGLVDTAAALNTVRTTA 716
Cdd:PRK12555    79 VTSltERNASRVFEAMGAGALDAVDTPTlgigagleeYAAELLAKID------QIGRLLGRRLAPAAAPAAASAAPFRTT 152

                   ...
gi 1986385785  717 EVL 719
Cdd:PRK12555   153 PRL 155
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
354-887 3.57e-08

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 57.96  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  354 LDFSRLESGRLRaeyRATDLADYTW--RLASTFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAG 431
Cdd:COG3321    847 VDWSALYPGRGR---RRVPLPTYPFqrEDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAA 923
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  432 RVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVF 511
Cdd:COG3321    924 AALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALA 1003
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  512 TVRVPFGTAHLPADRVLPDGERIAPEFDARPYAEEAEHWWTGDEPVTLPLPPPAGRRPGRILLADDNADLRDHVARLLRP 591
Cdd:COG3321   1004 LLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAA 1083
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  592 HWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSARAGEESAVEGLGAGADDYLVK 671
Cdd:COG3321   1084 LALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAAL 1163
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  672 PFSARDLIARVRANLDLGQARRQIISRLRGLVDTAAALNTVRTTAEVLDVAAQHVRAMTTAGRVVVSVPGSRAEVDGGAA 751
Cdd:COG3321   1164 AAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAA 1243
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  752 PGTQPDSVLPLPDTSGATVGELRVWSPPDGALEPAVLIQLARLIGLRLENARLYEAEHRIAsTLQHSLLPQSLPRMPGTI 831
Cdd:COG3321   1244 AVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAA-AAAAAAAAAAAAAAAALA 1322
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1986385785  832 VASRYLAGSNEAEVGGDWYDVIAAPDEQLVLVIGDVVGKGVQAAAGMGQLRNALRA 887
Cdd:COG3321   1323 AALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALAL 1378
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-516 3.87e-08

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 52.54  E-value: 3.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  409 DREMWEKIVLNLLSNAVKFTAA-----GRVVVRIGADA-GDAVLSVEDTGVGIPADQQPLLFDRFhrVTgawaRSHEGTG 482
Cdd:cd16944      1 DTTQISQVLTNILKNAAEAIEGrpsdvGEVRIRVEADQdGRIVLIVCDNGKGFPREMRHRATEPY--VT----TRPKGTG 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1986385785  483 IGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16944     75 LGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
fixJ PRK09390
response regulator FixJ; Provisional
570-692 4.50e-08

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 54.62  E-value: 4.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  570 GRILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTrdVPIVVL 648
Cdd:PRK09390     4 GVVHVVDDDEAMRDSLAFLLdSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSP--LPVIVM 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQAR 692
Cdd:PRK09390    82 TGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEA 125
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
614-672 5.21e-08

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: 51.99  E-value: 5.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785  614 DLVLTDVMMPRLDGFGLIAALRADERTRDVPIVVLSARAGEESAVEGLGAGADDYLVKP 672
Cdd:cd17602     44 DLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
416-517 8.32e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 56.46  E-value: 8.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSN---AVKFTAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTGawarshEGTGIGLALVRELA 492
Cdd:PRK11086   437 ILGNLIENaleAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTKG------SNRGVGLYLVKQSV 510
                           90       100
                   ....*....|....*....|....*
gi 1986385785  493 ELHGGSASAASEPGRGSVFTVRVPF 517
Cdd:PRK11086   511 ENLGGSIAVESEPGVGTQFFVQIPW 535
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
570-694 1.16e-07

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 51.98  E-value: 1.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  570 GRILLADDNADLRDHVARLLRPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLS 649
Cdd:cd17596      1 PTILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVR--ERWPEVVRIIIS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1986385785  650 ARAGEESAVEGL-GAGADDYLVKPFSARDLIARVRANLDLGQARRQ 694
Cdd:cd17596     79 GYTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRE 124
PRK11173 PRK11173
two-component response regulator; Provisional
593-686 1.33e-07

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 53.87  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  593 WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADertRDVPIVVLSARAGEESAVEGLGAGADDYLVKP 672
Cdd:PRK11173    28 YDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQ---ANVALMFLTGRDNEVDKILGLEIGADDYITKP 104
                           90
                   ....*....|....
gi 1986385785  673 FSARDLIARVRaNL 686
Cdd:PRK11173   105 FNPRELTIRAR-NL 117
PRK10693 PRK10693
two-component system response regulator RssB;
598-683 1.44e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 54.61  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  598 AVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFsaRD 677
Cdd:PRK10693     3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLR--NRGDQTPVLVISATENMADIAKALRLGVQDVLLKPV--KD 78

                   ....*.
gi 1986385785  678 LiARVR 683
Cdd:PRK10693    79 L-NRLR 83
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
304-516 1.48e-07

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: 55.26  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  304 VSHEFRTPLTLILGPLEdVLDDPRLPALQRERLLPMQRNGL-RLLKLVNTVLDFSRLESGRLraeyRATDLADYTWRLAS 382
Cdd:COG5806    208 IAHEVRNPLTVVRGFIQ-LLQEPELSDEKRKQYIRIALEELdRAEAIITDYLTFAKPQPEKL----EKIDVSEELEHVID 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  383 TFRSAAERAGLELVVETPPlSAPVYVDREMWEKIVLNLLSNAVKFTA-AGRVVVRIGADAGDAVLSVEDTGVGIPADQQP 461
Cdd:COG5806    283 VLSPYANMNNVEIQTELEP-GLYIEGDRQKLQQCLINIIKNGIEAMPnGGTLTIDVSIDKNKVIISIKDTGVGMTKEQLE 361
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1986385785  462 LLFDRFHRVTGawarshEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:COG5806    362 RLGEPYFSTKE------KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLP 410
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
367-516 1.49e-07

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 55.30  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  367 EYRATDLADYTWRLASTFRSAAERAGLELVVETPPLSAPVyvdremwEK-----IVLN-LLSNAVKF----TAAGRVVVR 436
Cdd:COG3920    355 DWEGVDLRDYLRELLEPLRDSYGGRGIRIELDGPDVELPA-------DAavplgLILNeLVTNALKHaflsGEGGRIRVS 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  437 IGADAGDAVLSVEDTGVGIPADQQPllfdrfhrvtgawarsHEGTGIGLALVRELAELHGGSASAASEPgrGSVFTVRVP 516
Cdd:COG3920    428 WRREDGRLRLTVSDNGVGLPEDVDP----------------PARKGLGLRLIRALVRQLGGTLELDRPE--GTRVRITFP 489
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
300-497 1.59e-07

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 54.97  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  300 FFSNVSHEFRTPLTLILGPLE--------DVldDP---RLPALQR--ERLLPMQRNGLRL-------LKLVNTVLDFSRL 359
Cdd:PRK10755   140 FTADVAHELRTPLAGIRLHLEllekqhhiDV--APliaRLDQMMHtvEQLLQLARAGQSFssghyqtVKLLEDVILPSQD 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  360 EsgrlraeyratdladytwrlastFRSAAERAGLELVVETPPLSAPVYVDREMWEKIVLNLLSNAVKFTAAG-RVVVRIG 438
Cdd:PRK10755   218 E-----------------------LSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGsTITIKLS 274
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785  439 ADAGDAVLSVEDTGVGIPADQQPLLFDRFHRVTgawaRSHEGTGIGLALVRELAELHGG 497
Cdd:PRK10755   275 QEDGGAVLAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHG 329
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
571-686 1.77e-07

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 53.49  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRAderTRDVPIVVLS 649
Cdd:PRK10701     3 KIVFVEDDAEVGSLIAAYLAKHdIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRP---KWQGPIVLLT 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1986385785  650 ARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:PRK10701    80 SLDSDMNHILALEMGACDYILKTTPPAVLLARLRLHL 116
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
571-678 1.97e-07

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: 50.86  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGR--FDLVLTDVMMPRLDGFGLIAALRADERTRDVP-IV 646
Cdd:cd19933      2 KVLLVDDNAVNRMVTKGLLeKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPlIV 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1986385785  647 VLSARAGEESAVEGLGAGADDYLVKPFSARDL 678
Cdd:cd19933     82 ALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
572-682 2.12e-07

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: 50.72  E-value: 2.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHW--DVTTAVDGQAALELTRRGRFDLVLTDVMM-PRLDGFGLIAALRADERTRDVPIVVL 648
Cdd:cd17589      1 FLIVDDQPTFRSMLKSMLRSLGvtRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELRHKKLISPSTVFIM 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1986385785  649 ----SARAGEESAVEglgAGADDYLVKPFSARDLIARV 682
Cdd:cd17589     81 vtgeSSRAMVLSALE---LEPDDYLLKPFTVSELRERL 115
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
568-694 4.71e-07

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 53.72  E-value: 4.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  568 RPGRILLADDNADLRDHVARLL-RPHWDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRadERTRDVPIV 646
Cdd:PRK10923     2 QRGIVWVVDDDSSIRWVLERALaGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIK--QRHPMLPVI 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1986385785  647 VLSARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANLDLGQARRQ 694
Cdd:PRK10923    80 IMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQ 127
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
572-673 5.06e-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: 49.27  E-value: 5.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRG-RFDLVLTDVMMPR-LDGFGLIAALRAdeRTRDVPIVVL 648
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLEDLgYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARR--RRPDLKVLLT 78
                           90       100
                   ....*....|....*....|....*
gi 1986385785  649 SARAGEESAVEGLGAGAdDYLVKPF 673
Cdd:cd18161     79 SGYAENAIEGGDLAPGV-DVLSKPF 102
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
569-691 6.78e-07

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 51.39  E-value: 6.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  569 PGRILLADDNADLRDHVARLLR--PHWDVTT-AVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRDVPI 645
Cdd:PRK10403     6 PFQVLIVDDHPLMRRGVRQLLEldPGFEVVAeAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIII 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1986385785  646 VVLSARAGEESAVegLGAGADDYLVKPFSARDLIARVRANLDLGQA 691
Cdd:PRK10403    86 LTVSDASSDVFAL--IDAGADGYLLKDSDPEVLLEAIRAGAKGSKV 129
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
414-516 2.64e-06

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 47.37  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  414 EKIVLNLLSNAVK-FTAAGRVVVRIGADAGDA---------------VLSVEDTGVGIPADQQPLLFDRFHRVTGAwars 477
Cdd:cd16919      2 ELAILNLAVNARDaMPEGGRLTIETSNQRVDAdyalnyrdlipgnyvCLEVSDTGSGMPAEVLRRAFEPFFTTKEV---- 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1986385785  478 HEGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:cd16919     78 GKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
PRK11697 PRK11697
two-component system response regulator BtsR;
571-686 3.19e-06

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 49.84  E-value: 3.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  571 RILLADDNADLRDHVARLLRPHWDVTtaVDGQA-----ALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADERTRdvpI 645
Cdd:PRK11697     3 KVLIVDDEPLAREELRELLQEEGDIE--IVGECsnaieAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPEHMPY---I 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1986385785  646 VVLSA------RAGEESAVeglgagadDYLVKPFSARDL---IARVRANL 686
Cdd:PRK11697    78 VFVTAfdeyaiKAFEEHAF--------DYLLKPIDPARLaktLARLRQER 119
PLN03029 PLN03029
type-a response regulator protein; Provisional
572-678 3.48e-06

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 49.26  E-value: 3.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLR-PHWDVTTAVDGQAALELT--------------------RRGRFDLVLTDVMMPRLDGFGL 630
Cdd:PLN03029    11 VLAVDDSLIDRKLIEKLLKtSSYQVTTVDSGSKALKFLglheddrsnpdtpsvspnshQEVEVNLIITDYCMPGMTGYDL 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1986385785  631 IAALRADERTRDVPIVVLSARAGEESAVEGLGAGADDYLVKPFSARDL 678
Cdd:PLN03029    91 LKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
419-526 1.27e-05

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 49.25  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  419 NLLSNAVKFTAAgrvVVRIGADAGDAVLS--VEDTGVGIPADQQPLLFDRFHRVTgawaRSHEGTGIGLALVRELAELHG 496
Cdd:PRK10815   385 NVLDNACKYCLE---FVEISARQTDEHLHivVEDDGPGIPESKRELIFDRGQRAD----TLRPGQGLGLSVAREITEQYE 457
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785  497 GSASAASEPGRGSvfTVRVPFGTAHLPADR 526
Cdd:PRK10815   458 GKISAGDSPLGGA--RMEVIFGRQHSTPKD 485
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
1077-1167 1.95e-05

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: 44.67  E-value: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1077 DDVFDLTVAVSEAAANAIEHPVDPVEPVITVEAslvDGAVVITVRDSGR--------------WRETAAEGF-RGRGLAL 1141
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAGEITVTLSE---GGELTLTVEDNGIgippedlprifepfSTADKRGGGgTGLGLSI 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1986385785 1142 IGALSELS------VSRSDSGTSVTLRRPLSI 1167
Cdd:pfam02518   78 VRKLVELLggtitvESEPGGGTTVTLTLPLAQ 109
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
1049-1161 1.99e-05

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 46.07  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1049 LRLPAEPGRLSVLRrrledfLTGNGVPD------DDVFDLTVAVSEAAANAIEHPVDPVEP-VITVEASLVDGAVVITVR 1121
Cdd:PRK04069    10 MKIPAKAEYVSIIR------LTLSGVANrmgfsyDDIEDMKIAVSEACTNAVQHAYKEDEVgEIHIRFEIYEDRLEIVVA 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1986385785 1122 DSG------RWRETAA------------EGfrGRGLALIGAL-SELSVsRSDSGTSVTL 1161
Cdd:PRK04069    84 DNGvsfdyeTLKSKLGpydiskpiedlrEG--GLGLFLIETLmDDVTV-YKDSGVTVSM 139
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1085-1166 3.68e-05

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.18  E-value: 3.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  1085 AVSEAAANAIEHPvdPVEPVITVEASLVDGAVVITVRDSGR------------------WRETAAEGFrGRGLALIGALS 1146
Cdd:smart00387    9 VLSNLLDNAIKYT--PEGGRITVTLERDGDHVEITVEDNGPgippedlekifepffrtdKRSRKIGGT-GLGLSIVKKLV 85
                            90       100
                    ....*....|....*....|....*.
gi 1986385785  1147 E-----LSV-SRSDSGTSVTLRRPLS 1166
Cdd:smart00387   86 ElhggeISVeSEPGGGTTFTITLPLE 111
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
572-672 4.15e-05

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 43.80  E-value: 4.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPHWD---VTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtRDVPIVVL 648
Cdd:cd17565      1 FYIVDDDKNIIKILSDIIEDDDLgevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTG--SNGKFIMI 78
                           90       100
                   ....*....|....*....|....
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKP 672
Cdd:cd17565     79 SQVSDKEMIGKAYQAGIEFFINKP 102
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
570-686 4.38e-05

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: 44.08  E-value: 4.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  570 GRILLADDNADLRDHVARLLRPH-WDVTTAVDGQAALELTRRGRFDLVLTDVMMPRLDGFGLIAALRADErtRDVPIVVL 648
Cdd:cd17553      1 EKILIVDDQYGIRILLNEVFNKEgYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVID--ENIRVIIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1986385785  649 SARAGEESAVEGLGAGADDYLVKPFSARDLIARVRANL 686
Cdd:cd17553     79 TAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-498 8.28e-05

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: 42.83  E-value: 8.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  409 DREMWEKIVLNLLSNAVKFTAAGRVV-VRIGADAGDAVLSVEDTGVGIPADQQPLLFDRFHR-VTGAWARSHegTGIGLA 486
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGGTVsISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRdDTSRRSGGH--YGMGLY 78
                           90
                   ....*....|..
gi 1986385785  487 LVRELAELHGGS 498
Cdd:cd16975     79 IAKNLVEKHGGS 90
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
295-526 1.69e-04

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 46.08  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  295 QAKTNFFSNVSHEFRTPLTlILGPLEDVLDDPRLPALQRERLLPMQRNGLRLLKLVNTVLDFSRLESGRLRAE---YRAT 371
Cdd:PRK10618   448 QARKAFLQNIGDELKQPLQ-SLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEqelFSLQ 526
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  372 DLADytwRLASTFRSAAERAGLELVVETPPLSAPVYV-DREMWEKIVLNLLSNAVKFTAAGRVVVRIGADAGDA---VLS 447
Cdd:PRK10618   527 DLID---EVLPEVLPAIKRKGLQLLIHNHLKAEQLRIgDRDALRKILLLLLNYAITTTAYGKITLEVDQDESSPdrlTIR 603
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  448 VEDTGVGIPADQQ---------PLLFDRFHRvtgawarsheGTGIGLALVRELAELHGGSASAASEPGRGSVFTVRVPFG 518
Cdd:PRK10618   604 ILDTGAGVSIKELdnlhfpflnQTQGDRYGK----------ASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKML 673

                   ....*...
gi 1986385785  519 TAHLPADR 526
Cdd:PRK10618   674 AADPEVEE 681
glnL PRK11073
nitrogen regulation protein NR(II);
305-516 1.84e-04

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 45.07  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  305 SHEFRTPLTLILGP---LEDVLDDP--------------RLPALQrERLLPMQRNGLRLLKLVNTVLD-FSRLESgrLRA 366
Cdd:PRK11073   138 AHEIKNPLGGLRGAaqlLSKALPDPalteytkviieqadRLRNLV-DRLLGPQRPGTHVTESIHKVAErVVQLVS--LEL 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  367 EYRATDLADYTWRLastfrsaaeraglelvvetPPLSapvyVDREMWEKIVLNLLSNAV------------------KFT 428
Cdd:PRK11073   215 PDNVRLIRDYDPSL-------------------PELA----HDPDQIEQVLLNIVRNALqalgpeggtitlrtrtafQLT 271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  429 AAG---RVVVRIgadagdavlSVEDTGVGIPADQQPLLFdrFHRVTGawarsHEG-TGIGLALVRELAELHGGSASAASE 504
Cdd:PRK11073   272 LHGeryRLAARI---------DIEDNGPGIPPHLQDTLF--YPMVSG-----REGgTGLGLSIARNLIDQHSGKIEFTSW 335
                          250
                   ....*....|..
gi 1986385785  505 PGRgSVFTVRVP 516
Cdd:PRK11073   336 PGH-TEFSVYLP 346
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
416-516 3.92e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 40.89  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  416 IVLNLLSNAV-KFTAAGRVVVRIGADAGDAVLSVEDTGVGIPADQQPLLfdrfhrvtgaWARSHEGTGIGLALVRE-LAE 493
Cdd:cd16924      9 LVENAIQHGLsPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNIL----------GKKPKEGNGIGLYNVHQrLIL 78
                           90       100
                   ....*....|....*....|....*
gi 1986385785  494 LHGGSA--SAASEPGRGSVFTVRVP 516
Cdd:cd16924     79 LFGEDYgiHIASEPDKGTRITFTIP 103
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
1092-1165 5.43e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 43.85  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1092 NAIEHPVDPVEP--VITVEASLVDGAVVITVRDSG---------RWRETAAEGFRGRGLALI----------GALSELSV 1150
Cdd:COG2972    347 NAIEHGIEPKEGggTIRISIRKEGDRLVITVEDNGvgmpeekleKLLEELSSKGEGRGIGLRnvrerlklyyGEEYGLEI 426
                           90
                   ....*....|....*.
gi 1986385785 1151 -SRSDSGTSVTLRRPL 1165
Cdd:COG2972    427 eSEPGEGTTVTIRIPL 442
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
1078-1166 7.31e-04

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 43.30  E-value: 7.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1078 DVFDLTVAVSEAAANAIEH--PVDPVEPVITVEASLVDGAVVITVRDSG-------RWR------ETAAEGFRGRGLALI 1142
Cdd:COG3290    278 SDTDLVTILGNLLDNAIEAveKLPEEERRVELSIRDDGDELVIEVEDSGpgipeelLEKifergfSTKLGEGRGLGLALV 357
                           90       100       110
                   ....*....|....*....|....*....|
gi 1986385785 1143 GALSE-----LSV-SRSDSGTSVTLRRPLS 1166
Cdd:COG3290    358 KQIVEkyggtIEVeSEEGEGTVFTVRLPKE 387
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
1077-1124 7.55e-04

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980 [Multi-domain]  Cd Length: 137  Bit Score: 41.06  E-value: 7.55e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1986385785 1077 DDVFDLTVAVSEAAANAIEHPVDP-VEPVITVEASLVDGAVVITVRDSG 1124
Cdd:TIGR01925   35 EELTDIKTAVSEAVTNAIIHGYEEnCEGVVYISATIEDHEVYITVRDEG 83
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
1077-1124 9.67e-04

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 40.60  E-value: 9.67e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1986385785 1077 DDVFDLTVAVSEAAANAIEHPVDPVEP-VITVEASLVDGAVVITVRDSG 1124
Cdd:cd16942     34 DELTEIKTVVSEAVTNAIIHGYNNDPNgIVSISVIIEDGVVHLTVRDEG 82
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
393-516 1.18e-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: 41.03  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  393 LELVVEtpplSAPVYVDREMWEKIV---LNLLSNAV-------------KFTAAGRVVVRIGADAGDAVLSVEDTGVGI- 455
Cdd:cd16916     20 VELVVE----GEDTELDKSVLEKLAdplTHLLRNAVdhgieapeerlaaGKPPEGTITLRAEHQGNQVVIEVSDDGRGId 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  456 --------------PADQQPLLFDR------FHR--VTGAWARSHEGTGIGLALVRELAELHGGSASAASEPGRGSVFTV 513
Cdd:cd16916     96 rekirekaiergliTADEAATLSDDevlnliFAPgfSTAEQVTDVSGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTI 175

                   ...
gi 1986385785  514 RVP 516
Cdd:cd16916    176 RLP 178
PRK10430 PRK10430
two-component system response regulator DcuR;
613-675 1.80e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 41.25  E-value: 1.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986385785  613 FDLVLTDVMMPRLDGFGLIAALRADERTRDVpiVVLSARAGEESAVEGLGAGADDYLVKPFSA 675
Cdd:PRK10430    50 IDLILLDIYMQQENGLDLLPVLHEAGCKSDV--IVISSAADAATIKDSLHYGVVDYLIKPFQA 110
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
405-516 1.93e-03

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 42.13  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  405 PVYVDREMWEKIVLNLLSNA----VKFTAAGRVVVRIGADAGD-AVLSVEDTGVGIPADQQPLLFDRfhrvtGAWARSHE 479
Cdd:PRK15053   425 PPGLDSTEFAAIVGNLLDNAfeasLRSDEGNKIVELFLSDEGDdVVIEVADQGCGVPESLRDKIFEQ-----GVSTRADE 499
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1986385785  480 GT--GIGLALVRELAELHGGSASAASEPGRGSVFTVRVP 516
Cdd:PRK15053   500 PGehGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
572-672 3.44e-03

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 38.86  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  572 ILLADDNADLRDHVARLLRPH----WDVTTAVDGQAAL----ELTRRGR-FDLVLTDVMMPRLDGFGLIAalRADERTRD 642
Cdd:cd17595      3 ILTVDDDPQVLRAVARDLRRQygkdYRVLRADSGAEALdalkELKLRGEaVALFLVDQRMPEMDGVEFLE--KAMELFPE 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1986385785  643 VPIVVLSARAGEESAVEGLG-AGADDYLVKP 672
Cdd:cd17595     81 AKRVLLTAYADTDAAIRAINdVQLDYYLLKP 111
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
993-1165 6.90e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 39.60  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785  993 RIGIDSGLADLTADAAKPAEHVEDLLDdLLAKAVRRTRRddiALLALQVTEPSEFVLRlpaepgrlSVLRRRLEDFLTGN 1072
Cdd:COG4585     73 KLQLEAARRLLDADPEAAREELEEIRE-LAREALAELRR---LVRGLRPPALDDLGLA--------AALEELAERLLRAA 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986385785 1073 GVP-------DDDVFDLTVA------VSEAAANAIEH-PVDPVepviTVEASLVDGAVVITVRDSGRWRETAAEGFRGRG 1138
Cdd:COG4585    141 GIRveldvdgDPDRLPPEVElalyriVQEALTNALKHaGATRV----TVTLEVDDGELTLTVRDDGVGFDPEAAPGGGLG 216
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1986385785 1139 L-------ALIGAlsELSV-SRSDSGTSVTLRRPL 1165
Cdd:COG4585    217 LrgmreraEALGG--TLTIgSAPGGGTRVRATLPL 249
 
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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