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Conserved domains on  [gi|2256105915|ref|WP_252039484|]
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response regulator [Vibrio sp. SCSIO 43133]

Protein Classification

sensor histidine kinase family protein( domain architecture ID 1001650)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
467-1099 1.10e-137

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 441.60  E-value: 1.10e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  467 LAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGK 546
Cdd:PRK11107   279 LDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGK 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  547 LDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITADNL 626
Cdd:PRK11107   359 LVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRAL 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  627 ENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINM 706
Cdd:PRK11107   439 SNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPL 518
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  707 KRSQVLETKPIVVpTSLNHLNILIVDDNASARLIVEDILQSLNFNVRSAngvdSAIDALNHaaqsdSAFDVVITDWQMPG 786
Cdd:PRK11107   519 DLNPNPIIDGLPT-DCLAGKRLLYVEPNSAAAQATLDILSETPLEVTYS----PTLSQLPE-----AHYDILLLGLPVTF 588
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  787 KDGVELIHA-IQQSESLNPKILMLTAYDRQLLADSVQERGLIvpSILDKPVTASHLFDAIvglydIENHRSSRDELEQQT 865
Cdd:PRK11107   589 REPLTMLHErLAKAKSMTDFLILALPCHEQVLAEQLKQDGAD--ACLSKPLSHTRLLPAL-----LEPCHHKQPPLLPPT 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  866 HlANVQHLAgahLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTL 945
Cdd:PRK11107   662 D-ESRLPLT---VMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLP 737
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  946 NDRAIPIIAMTADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLARWITSPQREigsevstssSDSNVNTQPVKLPDINt 1025
Cdd:PRK11107   738 HNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFT---------SRVVAPEPPEPVHFPN- 807
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2256105915 1026 ITLSQGLA--RANNNHQLYRRLLQRFYEHYSD-LSQVREQLANAASSDLKRYIHSLKGVSGNIGANELFELCSALES 1099
Cdd:PRK11107   808 ATLDWQLAlrQAAGKPDLARDMLQMLLDFLPEvRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ 884
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
467-1099 1.10e-137

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 441.60  E-value: 1.10e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  467 LAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGK 546
Cdd:PRK11107   279 LDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGK 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  547 LDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITADNL 626
Cdd:PRK11107   359 LVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRAL 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  627 ENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINM 706
Cdd:PRK11107   439 SNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPL 518
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  707 KRSQVLETKPIVVpTSLNHLNILIVDDNASARLIVEDILQSLNFNVRSAngvdSAIDALNHaaqsdSAFDVVITDWQMPG 786
Cdd:PRK11107   519 DLNPNPIIDGLPT-DCLAGKRLLYVEPNSAAAQATLDILSETPLEVTYS----PTLSQLPE-----AHYDILLLGLPVTF 588
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  787 KDGVELIHA-IQQSESLNPKILMLTAYDRQLLADSVQERGLIvpSILDKPVTASHLFDAIvglydIENHRSSRDELEQQT 865
Cdd:PRK11107   589 REPLTMLHErLAKAKSMTDFLILALPCHEQVLAEQLKQDGAD--ACLSKPLSHTRLLPAL-----LEPCHHKQPPLLPPT 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  866 HlANVQHLAgahLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTL 945
Cdd:PRK11107   662 D-ESRLPLT---VMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLP 737
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  946 NDRAIPIIAMTADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLARWITSPQREigsevstssSDSNVNTQPVKLPDINt 1025
Cdd:PRK11107   738 HNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFT---------SRVVAPEPPEPVHFPN- 807
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2256105915 1026 ITLSQGLA--RANNNHQLYRRLLQRFYEHYSD-LSQVREQLANAASSDLKRYIHSLKGVSGNIGANELFELCSALES 1099
Cdd:PRK11107   808 ATLDWQLAlrQAAGKPDLARDMLQMLLDFLPEvRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ 884
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
468-845 7.57e-78

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: 277.43  E-value: 7.57e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  468 AIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKL 547
Cdd:TIGR02956  451 AKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHL 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  548 DIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITAdnle 627
Cdd:TIGR02956  531 SISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL---- 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  628 NDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSstTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMK 707
Cdd:TIGR02956  607 NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT 684
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  708 RSQVLETKPIVVPTSLNHLNILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGK 787
Cdd:TIGR02956  685 RGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECF-----HQHAFDLALLDINLPDG 759
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2256105915  788 DGVELIHAIQQSESLNPKILMLtAYDRQLLADSV-QERGLIVPSILDKPVTASHLFDAI 845
Cdd:TIGR02956  760 DGVTLLQQLRAIYGAKNEVKFI-AFSAHVFNEDVaQYLAAGFDGFLAKPVVEEQLTAMI 817
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
379-704 6.14e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 248.67  E-value: 6.14e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  379 LTQYLALFEQLFTQKQAIAQQSSALDNAYLKAFKVIEPDFEHQQNIVENSSQISFYLAIGGIIFMSTIVFIVLLANKSHA 458
Cdd:COG0642      8 LVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  459 ALEKSADKLAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLaLKTDLTKAQRNYIQKVKLSADTLLGLINDILD 538
Cdd:COG0642     88 LLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLEL-LLEELDEEQREYLETILRSADRLLRLINDLLD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  539 FSKIEAGKLDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTaLYGDPLRLGQILTNLANNAVKFTEQGEvK 618
Cdd:COG0642    167 LSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGG-T 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  619 ITITadnLENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSttRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGS 698
Cdd:COG0642    245 VTVS---VRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                   ....*.
gi 2256105915  699 TFEFTI 704
Cdd:COG0642    320 TFTVTL 325
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
597-706 7.85e-56

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 188.86  E-value: 7.85e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQGEVKITITADNLENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAI 676
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2256105915  677 SKELCLLMGGDIEVRSQFGEGSTFEFTINM 706
Cdd:cd16922     81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
592-704 2.04e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 127.76  E-value: 2.04e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915   592 GDPLRLGQILTNLANNAVKFTEQGeVKITITADnLENDDVTLRfaVSDTGIGMTPEQTQKLFNKFTQADSsTTRKYGGTG 671
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVTLE-RDGDHVEIT--VEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGTG 75
                            90       100       110
                    ....*....|....*....|....*....|...
gi 2256105915   672 LGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:smart00387   76 LGLSIVKKLVELHGGEISVESEPGGGTTFTITL 108
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
592-708 1.06e-31

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 119.78  E-value: 1.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  592 GDPLRLGQILTNLANNAVKFT-EQGEVKITITADNlenddvTLRFAVSDTGIGMTPEQTQKLFNKFTQADSsttRKYGGT 670
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSEGG------ELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGT 71
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2256105915  671 GLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKR 708
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
484-717 1.38e-31

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 130.53  E-value: 1.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  484 FLANMSHEIRTPMNAIigmsylALKTDLTKAQRNYIQ-KVKLSADTLLG-------LINDILDFSKIEAG--KLDIEHVD 553
Cdd:NF040691   274 FVSDVSHELRTPLTTI------RMAADVIHDSRDDFDpATARSAELLHTeldrfesLLSDLLEISRFDAGaaELDVEPVD 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  554 FR--LENVLDNISNLvglkASEQGLELLIHTSkDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITADnleNDDV 631
Cdd:NF040691   348 LRplVRRVVDALRQL----AERAGVELRVDAP-GTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQD---DTAV 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  632 TLrfAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKRSQV 711
Cdd:NF040691   420 AV--TVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAGDR 497

                   ....*.
gi 2256105915  712 LETKPI 717
Cdd:NF040691   498 LTTSPL 503
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
479-688 6.94e-24

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 106.45  E-value: 6.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  479 QAKSDFLANMSHEIRTPMnAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDIEHVDFRLEN 558
Cdd:NF012163   238 QMRRDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVP 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  559 VLDNISNLVGLKASEQGLEllIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEvKITITAdnlENDDVTLRFAVS 638
Cdd:NF012163   317 LLEVEGGAFRERFASAGLE--LEVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHISA---SQRPKEVTLTVA 390
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2256105915  639 DTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDI 688
Cdd:NF012163   391 DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
467-1099 1.10e-137

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 441.60  E-value: 1.10e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  467 LAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGK 546
Cdd:PRK11107   279 LDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGK 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  547 LDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITADNL 626
Cdd:PRK11107   359 LVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRAL 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  627 ENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINM 706
Cdd:PRK11107   439 SNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPL 518
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  707 KRSQVLETKPIVVpTSLNHLNILIVDDNASARLIVEDILQSLNFNVRSAngvdSAIDALNHaaqsdSAFDVVITDWQMPG 786
Cdd:PRK11107   519 DLNPNPIIDGLPT-DCLAGKRLLYVEPNSAAAQATLDILSETPLEVTYS----PTLSQLPE-----AHYDILLLGLPVTF 588
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  787 KDGVELIHA-IQQSESLNPKILMLTAYDRQLLADSVQERGLIvpSILDKPVTASHLFDAIvglydIENHRSSRDELEQQT 865
Cdd:PRK11107   589 REPLTMLHErLAKAKSMTDFLILALPCHEQVLAEQLKQDGAD--ACLSKPLSHTRLLPAL-----LEPCHHKQPPLLPPT 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  866 HlANVQHLAgahLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTL 945
Cdd:PRK11107   662 D-ESRLPLT---VMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLP 737
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  946 NDRAIPIIAMTADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLARWITSPQREigsevstssSDSNVNTQPVKLPDINt 1025
Cdd:PRK11107   738 HNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFT---------SRVVAPEPPEPVHFPN- 807
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2256105915 1026 ITLSQGLA--RANNNHQLYRRLLQRFYEHYSD-LSQVREQLANAASSDLKRYIHSLKGVSGNIGANELFELCSALES 1099
Cdd:PRK11107   808 ATLDWQLAlrQAAGKPDLARDMLQMLLDFLPEvRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ 884
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
468-845 7.57e-78

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: 277.43  E-value: 7.57e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  468 AIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKL 547
Cdd:TIGR02956  451 AKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHL 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  548 DIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITAdnle 627
Cdd:TIGR02956  531 SISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL---- 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  628 NDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSstTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMK 707
Cdd:TIGR02956  607 NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT 684
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  708 RSQVLETKPIVVPTSLNHLNILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGK 787
Cdd:TIGR02956  685 RGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECF-----HQHAFDLALLDINLPDG 759
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2256105915  788 DGVELIHAIQQSESLNPKILMLtAYDRQLLADSV-QERGLIVPSILDKPVTASHLFDAI 845
Cdd:TIGR02956  760 DGVTLLQQLRAIYGAKNEVKFI-AFSAHVFNEDVaQYLAAGFDGFLAKPVVEEQLTAMI 817
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
379-704 6.14e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 248.67  E-value: 6.14e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  379 LTQYLALFEQLFTQKQAIAQQSSALDNAYLKAFKVIEPDFEHQQNIVENSSQISFYLAIGGIIFMSTIVFIVLLANKSHA 458
Cdd:COG0642      8 LVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  459 ALEKSADKLAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLaLKTDLTKAQRNYIQKVKLSADTLLGLINDILD 538
Cdd:COG0642     88 LLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLEL-LLEELDEEQREYLETILRSADRLLRLINDLLD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  539 FSKIEAGKLDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTaLYGDPLRLGQILTNLANNAVKFTEQGEvK 618
Cdd:COG0642    167 LSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGG-T 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  619 ITITadnLENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSttRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGS 698
Cdd:COG0642    245 VTVS---VRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                   ....*.
gi 2256105915  699 TFEFTI 704
Cdd:COG0642    320 TFTVTL 325
PRK15347 PRK15347
two component system sensor kinase;
454-1104 1.21e-69

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 252.64  E-value: 1.21e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  454 NKSHAALEKSADK----LAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTL 529
Cdd:PRK15347   367 NEQYDTLENKVAErtqaLAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSL 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  530 LGLINDILDFSKIEAGKLDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAV 609
Cdd:PRK15347   447 LAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAV 526
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  610 KFTEQGEVKITITAdnlENDdvTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTtrkyGGTGLGLAISKELCLLMGGDIE 689
Cdd:PRK15347   527 KFTETGGIRLRVKR---HEQ--QLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELT 597
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  690 VRSQFGEGSTFEFTINMKRSQVLET--KPIVVPTSLnhlnilivddnasarlivedilqslnfnvrsangvdsaidalnH 767
Cdd:PRK15347   598 LFSTPGVGSCFSLVLPLNEYAPPEPlkGELSAPLAL-------------------------------------------H 634
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  768 AAqsdsafdvvITDWqmpgkdGVELIHAIQQSESLNPKILMLTAYDRQLLADSVQErglivpsildkpvtashlfdaivg 847
Cdd:PRK15347   635 RQ---------LSAW------GITCQPGHQNPALLDPELAYLPGRLYDLLQQIIQG------------------------ 675
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  848 lydienhrssrDELEQQTHLaNVQHLAgAHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDC 927
Cdd:PRK15347   676 -----------APNEPVINL-PLQPWQ-LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDI 742
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  928 QMPVLDGYSATEIIRNTLN--DRAIPIIAMTADVMERDRERAYQSGMNDIIAKPIDVGimfsTLARWItspqreigSEVS 1005
Cdd:PRK15347   743 RMPGLDGLETTQLWRDDPNnlDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLA----QLARAL--------ELAA 810
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915 1006 TSSSDSNVNTQPvklpdiNTITLSQGLARANNnhqlyrRLLQRFYEHYSDLSQVREQlANAASSDLKRYIHSLKGVSGNI 1085
Cdd:PRK15347   811 EYQLLRGIELSP------QDSSCSPLLDTDDM------ALNSKLYQSLLLLLAQIEQ-AVENQEVLSQLLHTLKGCAGQA 877
                          650
                   ....*....|....*....
gi 2256105915 1086 GANELFELCSALESDINNE 1104
Cdd:PRK15347   878 GLTELQCAVIDLENALETG 896
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
460-990 2.33e-63

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 233.71  E-value: 2.33e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  460 LEKSADKLAIArdeADYANQAKSDFLANMSHEIRTPMNAIIGMSYLaLKTD--------LTKAQRNyiqkvklSADTLLG 531
Cdd:PRK10841   429 MEESLQEMAQA---AEQASQSKSMFLATVSHELRTPLYGIIGNLDL-LQTKelpkgvdrLVTAMNN-------SSSLLLK 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  532 LINDILDFSKIEAGKLDIEHVDFRLENVLDNI-SNLVGLKASEQgLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVK 610
Cdd:PRK10841   498 IISDILDFSKIESEQLKIEPREFSPREVINHItANYLPLVVKKR-LGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIK 576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  611 FTEQGEVKITITADnlendDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEV 690
Cdd:PRK10841   577 FTDTGCIVLHVRVD-----GDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISV 651
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  691 RSQFGEGSTFEFTINMKRSQVlETKPIVvpTSLNHLNILIVDDNASarliVEDILQSLnfnvRSANGvdsaIDALNHAAQ 770
Cdd:PRK10841   652 DSEPGMGSQFTIRIPLYGAQY-PQKKGV--EGLQGKRCWLAVRNAS----LEQFLETL----LQRSG----IQVQRYEGQ 716
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  771 SDSAFDVVITDwqmpgkdgveliHAIQQSESLNPKILMLTAYdrqllADSVQER--GLIVPSildkPVTASHLFDAIVGL 848
Cdd:PRK10841   717 EPTPEDVLITD------------DPVQKKWQGRAVITFCRRH-----IGIPLEIapGEWVHS----TATPHELPALLARI 775
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  849 YDIENHrSSRDELEQQTHLANVQHLAGAHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQ 928
Cdd:PRK10841   776 YRIELE-SDDSANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVN 854
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2256105915  929 MPVLDGYSATEIIRNTlnDRAIPIIAMTADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLA 990
Cdd:PRK10841   855 MPNMDGYRLTQRLRQL--GLTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLT 914
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
341-704 4.08e-62

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 217.50  E-value: 4.08e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  341 IAEQIEGTIKESQQRLADLIPHISDATQQQTLGKIKGQLTQYLALFEQLFTQKQAIAQQSSALDNAYLKAFKVIEPDFEH 420
Cdd:COG5002     27 LLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  421 QQNIVENSSQISFYLAIGGIIFMSTIVFIVLLANKSHAALEKSADKLAIARDEAdyANQAKSDFLANMSHEIRTPMNAII 500
Cdd:COG5002    107 LLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELER--LEQMRREFVANVSHELRTPLTSIR 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  501 GMSYLAL--KTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDIEHVDFRLENVLDNISNLVGLKASEQGLEL 578
Cdd:COG5002    185 GYLELLLdgAADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIEL 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  579 LIHTSKDvPTALYGDPLRLGQILTNLANNAVKFTEQGEvKITITADNLENddvTLRFAVSDTGIGMTPEQTQKLFNKFTQ 658
Cdd:COG5002    265 ELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTPEGG-TITVSLREEDD---QVRISVRDTGIGIPEEDLPRIFERFYR 339
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2256105915  659 ADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:COG5002    340 VDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
466-704 4.72e-62

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 211.69  E-value: 4.72e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  466 KLAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALK--TDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIE 543
Cdd:COG2205      1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  544 AGKLDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTaLYGDPLRLGQILTNLANNAVKFTEQGeVKITITA 623
Cdd:COG2205     81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSPPG-GTITISA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  624 dnlENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSstTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFT 703
Cdd:COG2205    159 ---RREGDGVRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVT 233

                   .
gi 2256105915  704 I 704
Cdd:COG2205    234 L 234
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
470-869 3.51e-61

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 224.82  E-value: 3.51e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  470 ARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDI 549
Cdd:PRK11091   272 YQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQL 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  550 EH--VDFrlENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITADnlE 627
Cdd:PRK11091   352 DNqpIDF--TDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYE--E 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  628 NDDvtLRFAVSDTGIGMTPEQTQKLFNKFTQA-DSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINM 706
Cdd:PRK11091   428 GDM--LTFEVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHA 505
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  707 KRS-QVLETKPIVVPTSLNHLNILIVDDNASARLIVEDILQSLnfnvrsANGVDSAI---DALNHAAqsDSAFDVVITDW 782
Cdd:PRK11091   506 PAVaEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKL------GNSVDVAMtgkEALEMFD--PDEYDLVLLDI 577
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  783 QMPGKDGVEL---IHAIQQSESLNPkILMLTAydrQLLADSVQERGLIVPSILDKPVTASHLFDAIVGLYDIENHRSSRD 859
Cdd:PRK11091   578 QLPDMTGLDIareLRERYPREDLPP-LVALTA---NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTV 653
                          410
                   ....*....|
gi 2256105915  860 ELEQQTHLAN 869
Cdd:PRK11091   654 TTEESSKANE 663
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
597-706 7.85e-56

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 188.86  E-value: 7.85e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQGEVKITITADNLENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAI 676
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2256105915  677 SKELCLLMGGDIEVRSQFGEGSTFEFTINM 706
Cdd:cd16922     81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
470-845 4.69e-54

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 205.14  E-value: 4.69e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  470 ARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDI 549
Cdd:PRK11466   433 ARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGKNV 512
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  550 EHVD--FRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITAdnle 627
Cdd:PRK11466   513 SVSDepFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRT---- 588
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  628 nDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQAdsstTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMK 707
Cdd:PRK11466   589 -DGEQWLVEVEDSGCGIDPAKLAEIFQPFVQV----SGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLR 663
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  708 RSQVLETKPIVVPTSLNHLNILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaQSDSAFDVVITDWQMPGK 787
Cdd:PRK11466   664 VATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETL----QNSEPFAAALVDFDLPDY 739
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  788 DGVELihaIQQSESLNPKiLMLTAYDRQLLADSVQER--GLIVpSILDKPVTASHLFDAI 845
Cdd:PRK11466   740 DGITL---ARQLAQQYPS-LVLIGFSAHVIDETLRQRtsSLFR-GIIPKPVPREVLGQLL 794
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
467-811 1.22e-44

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 176.85  E-value: 1.22e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  467 LAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQR-NYIQKVKLSADTLLGLINDILDFSKIEAG 545
Cdd:PRK09959   698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESG 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  546 KLDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITADN 625
Cdd:PRK09959   778 NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGH 857
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  626 LENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQadSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTIN 705
Cdd:PRK09959   858 IDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  706 MKRSQ---VLETK---PIVVPtslNHLNILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAQSDsaFDVVI 779
Cdd:PRK09959   936 VEISQqvaTVEAKaeqPITLP---EKLSILIADDHPTNRLLLKRQLNLLGYDVDEAT---DGVQALHKVSMQH--YDLLI 1007
                          330       340       350
                   ....*....|....*....|....*....|..
gi 2256105915  780 TDWQMPGKDGVELIHAIQQSESLNPkILMLTA 811
Cdd:PRK09959  1008 TDVNMPNMDGFELTRKLREQNSSLP-IWGLTA 1038
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
878-989 4.87e-44

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: 154.93  E-value: 4.87e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNT-LNDRAIPIIAMT 956
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeGGGRRTPIIALT 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKPIDVGIMFSTL 989
Cdd:cd17546     81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
258-704 3.29e-43

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 165.34  E-value: 3.29e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  258 MQQHIAAQIDSAGEEFTRASVVLRTSLQKELAAYQQELNDIQQQTNVKLSTTAQLLTLRSLFSDTTQYERDFSLVQTLNE 337
Cdd:COG4251     59 LALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLE 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  338 QQDIAEQIEGTIKESQQRLADLIPHISDATQQQTLGKIKGQLTQYLALFEQLFTQKQAIAQQSSALDNAYLKAFKVIEPD 417
Cdd:COG4251    139 ELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELL 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  418 FEHQQNIVENSSQISFYLAIGGIIFMSTIVFIVLLANKSHAALEKSADKLAIARDEADYANQAKSDFLANMSHEIRTPMN 497
Cdd:COG4251    219 LSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLR 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  498 AIIGMSYL---ALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDIEHVDfrLENVLDNISNLVGLKASEQ 574
Cdd:COG4251    299 KISGFSQLleeDYGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQELEFEPVD--LNELLEEVLEDLEPRIEER 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  575 GLELLIHtskDVPTaLYGDPLRLGQILTNLANNAVKFTEQGEV-KITITADNLENDdvtLRFAVSDTGIGMTPEQTQKLF 653
Cdd:COG4251    377 GAEIEVG---PLPT-VRGDPTLLRQVFQNLISNAIKYSRPGEPpRIEIGAEREGGE---WVFSVRDNGIGIDPEYAEKIF 449
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2256105915  654 NKFTQADSSttRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:COG4251    450 EIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTL 498
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
872-998 1.10e-41

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: 148.85  E-value: 1.10e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  872 HLAGAHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIP 951
Cdd:COG0784      2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIP 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2256105915  952 IIAMTADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLARWITSPQR 998
Cdd:COG0784     82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
463-704 7.04e-35

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


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 136.57  E-value: 7.04e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  463 SADKLAIARD--EADYANQAKSDFLANMSHEIRTPMNAIIGmsYL----ALKTDLTKAQRNYIQKVKLSADTLLGLINDI 536
Cdd:TIGR02966   94 EEQKLLVARDvtRLRRLEQMRRDFVANVSHELRTPLTVLRG--YLetlaDGPDEDPEEWNRALEIMLEQSQRMQSLVEDL 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  537 LDFSKIEAGKLDIEHVDFRLENVLDNISNLvgLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFT-EQG 615
Cdd:TIGR02966  172 LTLSRLESAASPLEDEPVDMPALLDHLRDE--AEALSQGKNHQITFEIDGGVDVLGDEDELRSAFSNLVSNAIKYTpEGG 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  616 EVKITITADnleNDDVtlRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFG 695
Cdd:TIGR02966  250 TITVRWRRD---GGGA--EFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELG 324

                   ....*....
gi 2256105915  696 EGSTFEFTI 704
Cdd:TIGR02966  325 KGSTFSFIF 333
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
459-704 1.76e-34

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: 138.95  E-value: 1.76e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  459 ALEKSaDKLAIArdeadyanqakSDFLANMSHEIRTPMNAIIGMSYLaLKTDLTKAQRNYIQKVKLSADTLLGLINDILD 538
Cdd:COG5809    260 LLRKS-EKLSVV-----------GELAAGIAHEIRNPLTSLKGFIQL-LKDTIDEEQKTYLDIMLSELDRIESIISEFLV 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  539 FSKIEAGKldIEHVDFR--LENVLDnisnLVGLKASEQGLELLIHTSKDVPTaLYGDPLRLGQILTNLANNAVKFTEQGe 616
Cdd:COG5809    327 LAKPQAIK--YEPKDLNtlIEEVIP----LLQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMPEG- 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  617 VKITITADNLENDDVTLRfaVSDTGIGMTPEQTQKLFNKFTqadsstTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGE 696
Cdd:COG5809    399 GNITIETKAEDDDKVVIS--VTDEGCGIPEERLKKLGEPFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGK 470

                   ....*...
gi 2256105915  697 GSTFEFTI 704
Cdd:COG5809    471 GTTFSITL 478
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
592-704 2.04e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 127.76  E-value: 2.04e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915   592 GDPLRLGQILTNLANNAVKFTEQGeVKITITADnLENDDVTLRfaVSDTGIGMTPEQTQKLFNKFTQADSsTTRKYGGTG 671
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVTLE-RDGDHVEIT--VEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGTG 75
                            90       100       110
                    ....*....|....*....|....*....|...
gi 2256105915   672 LGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:smart00387   76 LGLSIVKKLVELHGGEISVESEPGGGTTFTITL 108
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
592-708 1.06e-31

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 119.78  E-value: 1.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  592 GDPLRLGQILTNLANNAVKFT-EQGEVKITITADNlenddvTLRFAVSDTGIGMTPEQTQKLFNKFTQADSsttRKYGGT 670
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSEGG------ELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGT 71
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2256105915  671 GLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKR 708
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
484-717 1.38e-31

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 130.53  E-value: 1.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  484 FLANMSHEIRTPMNAIigmsylALKTDLTKAQRNYIQ-KVKLSADTLLG-------LINDILDFSKIEAG--KLDIEHVD 553
Cdd:NF040691   274 FVSDVSHELRTPLTTI------RMAADVIHDSRDDFDpATARSAELLHTeldrfesLLSDLLEISRFDAGaaELDVEPVD 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  554 FR--LENVLDNISNLvglkASEQGLELLIHTSkDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITADnleNDDV 631
Cdd:NF040691   348 LRplVRRVVDALRQL----AERAGVELRVDAP-GTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQD---DTAV 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  632 TLrfAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKRSQV 711
Cdd:NF040691   420 AV--TVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAGDR 497

                   ....*.
gi 2256105915  712 LETKPI 717
Cdd:NF040691   498 LTTSPL 503
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
486-704 1.57e-31

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 127.61  E-value: 1.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  486 ANMSHEIRTPMNAIIGMSYLA---LKTDLTKAQ-RNYIQKVKLSADTLLGLINDILDFSKieAGKLDIEHVDfrLENVLD 561
Cdd:COG4191    147 AGIAHEINNPLAAILGNAELLrrrLEDEPDPEElREALERILEGAERAAEIVRSLRAFSR--RDEEEREPVD--LNELID 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  562 NISNLVGLKASEQGLELLIHTSKDVPtALYGDPLRLGQILTNLANNAVK-FTEQGEVKITITADnLENDDVTLRfaVSDT 640
Cdd:COG4191    223 EALELLRPRLKARGIEVELDLPPDLP-PVLGDPGQLEQVLLNLLINAIDaMEEGEGGRITISTR-REGDYVVIS--VRDN 298
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  641 GIGMTPEQTQKLFNKFTqadssTTRKYG-GTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:COG4191    299 GPGIPPEVLERIFEPFF-----TTKPVGkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
876-992 1.61e-31

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 121.94  E-value: 1.61e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAM 955
Cdd:COG3706      2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPIDVGIMFS---TLARW 992
Cdd:COG3706     82 TALDDEEDRARALEAGADDYLTKPFDPEELLArvdLVARY 121
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
879-991 2.28e-31

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 119.18  E-value: 2.28e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTAD 958
Cdd:cd17548      3 LIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALTAY 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  959 VMERDRERAYQSGMNDIIAKPIDVGIMFSTLAR 991
Cdd:cd17548     83 AMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
488-711 1.43e-28

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: 120.07  E-value: 1.43e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  488 MSHEIRTPMNAIIGMSYLaLKTDLTKAQRNYIQKVKLSADT-------LLGLINDILDFSKIEAGKLdiEHVDfrLENVL 560
Cdd:COG5000    208 IAHEIKNPLTPIQLSAER-LRRKLADKLEEDREDLERALDTiirqvdrLKRIVDEFLDFARLPEPQL--EPVD--LNELL 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  561 DNISNLVGLKASEQGLELLIHTSKDVPTaLYGDPLRLGQILTNLANNAVKFTEQ-GEVKITITadnLENDDVTLRfaVSD 639
Cdd:COG5000    283 REVLALYEPALKEKDIRLELDLDPDLPE-VLADRDQLEQVLINLLKNAIEAIEEgGEIEVSTR---REDGRVRIE--VSD 356
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2256105915  640 TGIGMTPEQTQKLFNKFTqadssTTRKyGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKRSQV 711
Cdd:COG5000    357 NGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEAE 422
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
486-710 1.07e-27

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 116.10  E-value: 1.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  486 ANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKL---DIEHVdfrLENVLDN 562
Cdd:COG3852    140 AGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPERepvNLHEV---LERVLEL 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  563 ISNLVGlkaseQGLELLIHTSKDVPtALYGDPLRLGQILTNLANNAVK-FTEQGEVKITITADNLENDDVT-----LRFA 636
Cdd:COG3852    217 LRAEAP-----KNIRIVRDYDPSLP-EVLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVERQVTLGGLrprlyVRIE 290
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2256105915  637 VSDTGIGMTPEQTQKLFNKFTqadssTTRKyGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKRSQ 710
Cdd:COG3852    291 VIDNGPGIPEEILDRIFEPFF-----TTKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAE 358
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
428-704 1.56e-26

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: 113.81  E-value: 1.56e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  428 SSQISFYLAIGGIIFMSTIVFIVLLANKSHAALE-----KSADKLAIArdeadyanqakSDFLANMSHEIRTPMNAIIGM 502
Cdd:COG5806    154 ISELLDFILYFIIIQLLAMLIAVYLIENLIENILlrkelQRAEKLEVV-----------SELAASIAHEVRNPLTVVRGF 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  503 SYLALKTDLTKA-QRNYIQkvkLSADTL---LGLINDILDFSKIEAGKLDIEHVDFRLENVLDNISNLvglkASEQGLEl 578
Cdd:COG5806    223 IQLLQEPELSDEkRKQYIR---IALEELdraEAIITDYLTFAKPQPEKLEKIDVSEELEHVIDVLSPY----ANMNNVE- 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  579 lIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQ-GEVKITITADNlenDDVTLRfaVSDTGIGMTPEQTQKLFNKFT 657
Cdd:COG5806    295 -IQTELEPGLYIEGDRQKLQQCLINIIKNGIEAMPNgGTLTIDVSIDK---NKVIIS--IKDTGVGMTKEQLERLGEPYF 368
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2256105915  658 qadsSTTRKygGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:COG5806    369 ----STKEK--GTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITL 409
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
876-1021 3.70e-26

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 107.35  E-value: 3.70e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAM 955
Cdd:COG0745      2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRA--RPSDIPIIML 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPIDVGIMFST---LARWITSPQREIGSEVSTSSSDSNVNTQPVKLP 1021
Cdd:COG0745     80 TARDDEEDRVRGLEAGADDYLTKPFDPEELLARiraLLRRRAAEVLRVGDLLDLAAREVTRDGEPVELT 148
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
876-993 6.29e-25

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 104.48  E-value: 6.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAM 955
Cdd:COG3437      7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFL 86
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLARWI 993
Cdd:COG3437     87 TALADPEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
721-845 7.91e-25

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: 100.70  E-value: 7.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  721 TSLNHLNILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSE 800
Cdd:COG0784      1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAE---DGAEALELLRAGP--PDLILLDINMPGMDGLELLRRIRALP 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2256105915  801 SL-NPKILMLTAYDRQLLADSVQERGliVPSILDKPVTASHLFDAI 845
Cdd:COG0784     76 RLpDIPIIALTAYADEEDRERALEAG--ADDYLTKPVDPEELLEAL 119
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
489-845 2.01e-24

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 110.54  E-value: 2.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  489 SHEIRTPMNAIIGMSYLAL-KTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKieagKLDIEHVDFRLENVLDNISNLv 567
Cdd:PRK13837   458 AHNFNNILGAILGYAEMALnKLARHSRAARYIDEIISAGARARLIIDQILAFGR----KGERNTKPFDLSELVTEIAPL- 532
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  568 gLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVK-FTEQGEVKITI------TADNLENDDVT----LRFA 636
Cdd:PRK13837   533 -LRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLsraklrAPKVLSHGVLPpgryVLLR 611
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  637 VSDTGIGMTPEQTQKLFNKFTqadssTTRKyGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMkRSQV----- 711
Cdd:PRK13837   612 VSDTGAGIDEAVLPHIFEPFF-----TTRA-GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPP-SSKVpvapq 684
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  712 LETKPIVVPTSlNHLNILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHAAQsdsAFDVVITDwqMPGKDGVE 791
Cdd:PRK13837   685 AFFGPGPLPRG-RGETVLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKGPE---RFDLVLVD--DRLLDEEQ 758
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2256105915  792 LIHAIqqsESLNPKILMLTAyDRQLLADSVQERGLIVPSILDKPVTASHLFDAI 845
Cdd:PRK13837   759 AAAAL---HAAAPTLPIILG-GNSKTMALSPDLLASVAEILAKPISSRTLAYAL 808
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
879-981 2.90e-24

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: 98.76  E-value: 2.90e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMTAD 958
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTAH 79
                           90       100
                   ....*....|....*....|...
gi 2256105915  959 VMERDRERAYQSGMNDIIAKPID 981
Cdd:pfam00072   80 GDEDDAVEALEAGADDFLSKPFD 102
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
479-688 6.94e-24

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 106.45  E-value: 6.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  479 QAKSDFLANMSHEIRTPMnAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDIEHVDFRLEN 558
Cdd:NF012163   238 QMRRDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVP 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  559 VLDNISNLVGLKASEQGLEllIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEvKITITAdnlENDDVTLRFAVS 638
Cdd:NF012163   317 LLEVEGGAFRERFASAGLE--LEVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHISA---SQRPKEVTLTVA 390
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2256105915  639 DTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDI 688
Cdd:NF012163   391 DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
879-979 2.02e-23

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 95.76  E-value: 2.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMTAD 958
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE--LPPDIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 2256105915  959 VMERDRERAYQSGMNDIIAKP 979
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-704 1.70e-22

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 93.16  E-value: 1.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQGEVK-ITITADNLENddvTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTtrKYGGTGLGLA 675
Cdd:cd16921      1 LGQVLTNLLGNAIKFRRPRRPPrIEVGAEDVGE---EWTFYVRDNGIGIDPEYAEKVFGIFQRLHSRE--EYEGTGVGLA 75
                           90       100
                   ....*....|....*....|....*....
gi 2256105915  676 ISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16921     76 IVRKIIERHGGRIWLESEPGEGTTFYFTL 104
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
728-845 1.22e-21

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: 90.99  E-value: 1.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSESLN--PK 805
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAE---NGQEALELLKEEP--FDLVLMDLQMPVMDGLEATRRIRELEGGGrrTP 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2256105915  806 ILMLTAYDRQLLADSVQERGLIvpSILDKPVTASHLFDAI 845
Cdd:cd17546     76 IIALTANALEEDREKCLEAGMD--DYLSKPVKLDQLKEVL 113
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
484-712 2.01e-21

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 100.43  E-value: 2.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  484 FLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDIEHVDFRLENVLdni 563
Cdd:PRK11360   393 LVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQPVSLNALVEEVL--- 469
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  564 sNLVGLKASEQGLELLIHTSKDVPTAlYGDPLRLGQILTNLANNAVKfTEQGEVKITITADNLENDDVTLrfAVSDTGIG 643
Cdd:PRK11360   470 -QLFQTAGVQARVDFETELDNELPPI-WADPELLKQVLLNILINAVQ-AISARGKIRIRTWQYSDGQVAV--SIEDNGCG 544
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2256105915  644 MTPEQTQKLFNKFTqadsstTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKRSQVL 712
Cdd:PRK11360   545 IDPELLKKIFDPFF------TTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQGNQ 607
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
482-703 1.20e-20

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: 96.69  E-value: 1.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  482 SDFLANMSHEIRTPMNAIIGMSYLALKTDLTkaQRNYIQKVKLSADTLLGL---INDILDFSKIEAGKLDIEHVDFRLEN 558
Cdd:TIGR01386  242 SQFSADLAHELRTPLTNLLGQTQVALSQPRT--GEEYREVLESNLEELERLsrmVSDMLFLARADNGQLALERVRLDLAA 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  559 VLDNISNLVGLKASEQGLELLIHTSKDVPtalyGDPLRLGQILTNLANNAVKFTEQGEvKITItadNLENDDVTLRFAVS 638
Cdd:TIGR01386  320 ELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGG-TITV---RIERRSDEVRVSVS 391
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  639 DTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEgSTFEFT 703
Cdd:TIGR01386  392 NPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILR 455
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
593-688 1.58e-20

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 87.90  E-value: 1.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  593 DPLRLGQILTNLANNAVKFTEQGEvKITITAdnlENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGL 672
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRA---AQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                           90
                   ....*....|....*.
gi 2256105915  673 GLAISKELCLLMGGDI 688
Cdd:cd16946     77 GLAICHNIALAHGGTI 92
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
480-704 2.58e-20

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 95.08  E-value: 2.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  480 AKSDFLANMSHEIRTPMNAIIGmsYLALKTD--LTKAQRN-YIQKVKLSADTLLGLINDILDFSKIEAGKldieHVDfrL 556
Cdd:PRK11006   203 ARRNFFANVSHELRTPLTVLQG--YLEMMQDqpLEGALREkALHTMREQTQRMEGLVKQLLTLSKIEAAP----TID--L 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  557 ENVLDNISNLVGLKASEQGLELLIHTSK-DVPTAL--YGDPLRLGQILTNLANNAVKFTEQGeVKITITadnLENDDVTL 633
Cdd:PRK11006   275 NEKVDVPMMLRVLEREAQTLSQGKHTITfEVDNSLkvFGNEDQLRSAISNLVYNAVNHTPEG-THITVR---WQRVPQGA 350
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2256105915  634 RFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:PRK11006   351 EFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVL 421
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
877-980 9.08e-20

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: 85.63  E-value: 9.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMT 956
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKPI 980
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
879-979 2.49e-19

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: 84.00  E-value: 2.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIAMTAD 958
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 2256105915  959 VMERDRERAYQSGMNDIIAKP 979
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
878-980 5.28e-19

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: 83.33  E-value: 5.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTA 957
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                           90       100
                   ....*....|....*....|...
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPI 980
Cdd:cd19920     81 LTDTEDKVKGFELGAVDYITKPF 103
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
593-704 6.09e-19

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: 83.31  E-value: 6.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  593 DPLRLGQILTNLANNAVKFT-EQGEVKITITADNLENDDVTlrfaVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTG 671
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTpDGGRIRCILEKFRLNRFLLT----VSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTG 76
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  672 LGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16925     77 LGLSIVKEFVELHGGTVTVSDAPGGGALFQVEL 109
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
479-676 1.25e-18

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 90.46  E-value: 1.25e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  479 QAKSDFLANMSHEIRTPMnAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDiehvdFRLEN 558
Cdd:PRK10549   238 QMRRDFMADISHELRTPL-AVLRGELEAIQDGVRKFTPESVASLQAEVGTLTKLVDDLHQLSLSDEGALA-----YRKTP 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  559 VldNISNLVGLKASE-----QGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEvKITITAdNLENDDVTL 633
Cdd:PRK10549   312 V--DLVPLLEVAGGAfrerfASRGLTLQLSLPDSATVFGDPDRLMQLFNNLLENSLRYTDSGG-SLHISA-EQRDKTLRL 387
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2256105915  634 RFAvsDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAI 676
Cdd:PRK10549   388 TFA--DSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAI 428
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
879-981 2.26e-18

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: 81.74  E-value: 2.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTAD 958
Cdd:cd17580      2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTGY 81
                           90       100
                   ....*....|....*....|...
gi 2256105915  959 VMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17580     82 GQPEDRERALEAGFDAHLVKPVD 104
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
486-700 2.42e-18

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 89.46  E-value: 2.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  486 ANMSHEIRTPMNAIIGMS-YLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKieAGKLDIEHVDfrLENVLDNIS 564
Cdd:PRK10364   242 AGVAHEIRNPLSSIKGLAkYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVK--PTHLALQAVD--LNDLINHSL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  565 NLVGLKASEQGLELLIHTSKDVPtALYGDPLRLGQILTNLANNAVKFTEQGEVkITITADNlENDDVTLRfaVSDTGIGM 644
Cdd:PRK10364   318 QLVSQDANSREIQLRFTANDTLP-EIQADPDRLTQVLLNLYLNAIQAIGQHGV-ISVTASE-SGAGVKIS--VTDSGKGI 392
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2256105915  645 TPEQTQKLFnkftqaDSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTF 700
Cdd:PRK10364   393 AADQLEAIF------TPYFTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATF 442
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
725-845 6.02e-18

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: 82.65  E-value: 6.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  725 HLNILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSESL-N 803
Cdd:COG3706      1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAA---DGEEALELLQEHR--PDLILLDLEMPDMDGLELCRRLRADPRTaD 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2256105915  804 PKILMLTAYDRQLLADSVQERGLIvpSILDKPVTASHLFDAI 845
Cdd:COG3706     76 IPIIFLTALDDEEDRARALEAGAD--DYLTKPFDPEELLARV 115
PRK10490 PRK10490
sensor protein KdpD; Provisional
448-717 6.03e-18

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 89.71  E-value: 6.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  448 FIVLLANkshaALEK-----SAD--KLAIARDeadyanQAKSDFLANMSHEIRTPMNAIIGMSYLaLKTDLTKAQRNYIQ 520
Cdd:PRK10490   634 FTLLIAN----ALERltltaSEEqaRLASERE------QLRNALLAALSHDLRTPLTVLFGQAEI-LTLDLASEGSPHAR 702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  521 KVKLSADTLLG---LINDILDFSKIEAGKLDIehvdfRLE-NVLDNI--SNLVGLKASEQGLELLIHTSKDVpTALYGDP 594
Cdd:PRK10490   703 QASEIRQQVLNttrLVNNLLDMARIQSGGFNL-----RKEwLTLEEVvgSALQMLEPGLSGHPINLSLPEPL-TLIHVDG 776
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  595 LRLGQILTNLANNAVKFT-EQGEVKITITAdnlENDdvTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTrkYGGTGLG 673
Cdd:PRK10490   777 PLFERVLINLLENAVKYAgAQAEIGIDAHV---EGE--RLQLDVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLG 849
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2256105915  674 LAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKRSQVLETKPI 717
Cdd:PRK10490   850 LAICRAIVEVHGGTIWAENRPEGGACFRVTLPLETPPELEEFHE 893
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
876-981 1.08e-17

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: 80.18  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLES-QNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIA 954
Cdd:cd17551      1 MRILIVDDNPTNLLLLEALLRSaGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                           90       100
                   ....*....|....*....|....*..
gi 2256105915  955 MTADVMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17551     81 ITADTDREVRLRALEAGATDFLTKPFD 107
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
726-875 2.50e-17

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: 82.52  E-value: 2.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSESL-NP 804
Cdd:COG3437      7 PTVLIVDDDPENLELLRQLLRTLGYDVVTA---ESGEEALELLLEAP--PDLILLDVRMPGMDGFELLRLLRADPSTrDI 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2256105915  805 KILMLTAYDRQLLADSVQERGliVPSILDKPVTASHLFDAIVGLYDIENHRSSRDELEQQTHLANVQHLAG 875
Cdd:COG3437     82 PVIFLTALADPEDRERALEAG--ADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLHDIG 150
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
466-706 2.90e-17

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 87.68  E-value: 2.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  466 KLAIARDEADYANQAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAG 545
Cdd:PRK10618   435 KLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQ 514
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  546 KLDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGevKITITADN 625
Cdd:PRK10618   515 DWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYG--KITLEVDQ 592
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  626 LENDDVTLRFAVSDTGIGMTPEQTQKLFNKF---TQADssttrKYG-GTGLGLAISKELCLLMGGDIEVRSQFGEGSTFE 701
Cdd:PRK10618   593 DESSPDRLTIRILDTGAGVSIKELDNLHFPFlnqTQGD-----RYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYS 667

                   ....*
gi 2256105915  702 FTINM 706
Cdd:PRK10618   668 IHLKM 672
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
729-835 3.53e-17

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: 78.04  E-value: 3.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  729 LIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAaqSDSAFDVVITDWQMPGKDGVELIHAIQQSESlNPKILM 808
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTA---ADGEEALELL--REERPDLVLLDLMMPGMDGLELLRKLRELPP-DIPVIV 74
                           90       100
                   ....*....|....*....|....*..
gi 2256105915  809 LTAYDRQLLADSVQERGLIvpSILDKP 835
Cdd:cd00156     75 LTAKADEEDAVRALELGAD--DYLVKP 99
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
480-545 5.70e-17

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 76.07  E-value: 5.70e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2256105915   480 AKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAG 545
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
480-545 1.00e-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: 75.33  E-value: 1.00e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2256105915  480 AKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAG 545
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
594-700 1.22e-16

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 76.69  E-value: 1.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  594 PLRLGQILTNLANNAVKFTEqGEVKITI-TADnlenDDVTLRFAVSDTGIGMTPEQTQKLFNKFTqadssTTRKYG-GTG 671
Cdd:cd16943      1 PSQLNQVLLNLLVNAAQAME-GRGRITIrTWA----HVDQVLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTG 70
                           90       100
                   ....*....|....*....|....*....
gi 2256105915  672 LGLAISKELCLLMGGDIEVRSQFGEGSTF 700
Cdd:cd16943     71 LGLSLSYRIIQKHGGTIRVASVPGGGTRF 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
727-845 1.35e-16

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: 83.86  E-value: 1.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQsESLNPKI 806
Cdd:COG2204      4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALL-----REEPPDLVLLDLRMPGMDGLELLRELRA-LDPDLPV 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2256105915  807 LMLTAYDRQLLADSVQERGLIvpSILDKPVTASHLFDAI 845
Cdd:COG2204     78 ILLTGYGDVETAVEAIKAGAF--DYLTKPFDLEELLAAV 114
PRK09303 PRK09303
histidine kinase;
479-704 1.59e-16

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 83.08  E-value: 1.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  479 QAKSDFLANMSHEIRTPMNAiigmSYLALKTdltkAQRNYIQKVKLSADTLLG---------------LINDILDFSKIE 543
Cdd:PRK09303   149 KFKDRVLAMLAHDLRTPLTA----ASLALET----LELGQIDEDTELKPALIEqlqdqarrqleeierLITDLLEVGRTR 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  544 AGKLDIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSKDVPTaLYGDPLRLGQILTNLANNAVKFT-EQGEVKITIt 622
Cdd:PRK09303   221 WEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPS-VYADQERIRQVLLNLLDNAIKYTpEGGTITLSM- 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  623 adnLENDDVTLRFAVSDTGIGMTPEQTQKLF-NKFT-QADSSTTrkygGTGLGLAISKELCLLMGGDIEVRSQFGEGSTF 700
Cdd:PRK09303   299 ---LHRTTQKVQVSICDTGPGIPEEEQERIFeDRVRlPRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCF 371

                   ....
gi 2256105915  701 EFTI 704
Cdd:PRK09303   372 HFTL 375
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
876-991 3.15e-16

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: 82.70  E-value: 3.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAM 955
Cdd:COG2204      3 ARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVILL 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLAR 991
Cdd:COG2204     81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVER 116
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
877-981 3.50e-16

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: 76.30  E-value: 3.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNI--QVTVAQNGQVAID-LYKQMTFDG------ILMDCQMPVLDGYSATEIIRNTLND 947
Cdd:cd17557      1 TILLVEDNPGDAELIQEAFKEAGVpnELHVVRDGEEALDfLRGEGEYADaprpdlILLDLNMPRMDGFEVLREIKADPDL 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2256105915  948 RAIPIIAMTADVMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17557     81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVD 114
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
249-1123 3.51e-16

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


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 83.94  E-value: 3.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  249 RNLKLVTAPMQQHIAAQIDSAGEEFTRASVVLRTSLQKELAAYQQELNDIQQQTNVKLSTTAQLLTLRSLFSDTTQYERD 328
Cdd:COG2198      1 LALLLLALLLLLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  329 FSLVQTLNEQQDIAEQIEGTIKESQQRLADLIPHISDATQQQTLGKIKGQLTQYLALFEQLFTQKQAIAQQSSALDNAYL 408
Cdd:COG2198     81 ELLLLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  409 KAFKVIEPDFEHQQNIVENSSQISFYLAIGGIIFMSTIVFIVLLANKSHAALEKSADKLAIARDEADYANQAKSDFLANM 488
Cdd:COG2198    161 LLLALLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  489 SHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDIEHVDFRLENVLDNISNLVG 568
Cdd:COG2198    241 LAALLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  569 LKASEQGLELLIHTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQGEVKITITADNLENDDVTLRFAVSDTGIGMTPEQ 648
Cdd:COG2198    321 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  649 TQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKRSQVLETKPIVVPTSLNHLNI 728
Cdd:COG2198    401 LLLLSLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  729 LIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHAAQSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPKILM 808
Cdd:COG2198    481 LLLLLLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLAL 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  809 LTAYDRQLLADSVQERGLIVPSILDKPVTASHLFDAIVGLYDIENHRSSRDELEQQTHLANVQHLAGAHLLLVEDNEINQ 888
Cdd:COG2198    561 LLGLGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLL 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  889 ELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTADVMERDRERAY 968
Cdd:COG2198    641 LLLLLLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAA 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  969 QSGMNDIIAKPIDVGIMFSTLARWITSPQREIGSEVSTSSSDSNVntqpvklpdintitlsQGLARANNNHQLYRRLLQR 1048
Cdd:COG2198    721 ALLAALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLDL----------------EALRRLGGDPELLRELLEL 784
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2256105915 1049 FYEHY-SDLSQVREQLANAASSDLKRYIHSLKGVSGNIGANELFELCSALESDINNEQLQK--KLLNALNQTTEAIRE 1123
Cdd:COG2198    785 FLEELpELLAELRQALAAGDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARAGDLEEaeELLAELEAELERVLA 862
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
878-979 7.86e-16

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: 74.04  E-value: 7.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQN--IQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAM 955
Cdd:COG4753      2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE--LDPDTKIIIL 79
                           90       100
                   ....*....|....*....|....
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKP 979
Cdd:COG4753     80 SGYSDFEYAQEAIKLGADDYLLKP 103
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
727-825 1.33e-15

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: 73.65  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLN--FNVRSANgvdSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQsESLNP 804
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAE---NGEEALELLEEHK--PDLVITDINMPGMDGLELLEAIRE-LDPDT 74
                           90       100
                   ....*....|....*....|.
gi 2256105915  805 KILMLTAYDRQLLADSVQERG 825
Cdd:COG4753     75 KIIILSGYSDFEYAQEAIKLG 95
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
592-697 2.39e-15

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 73.21  E-value: 2.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  592 GDPLRLGQILTNLANNAVKFTEQGEVkITITadnLENDDVTLrFAVSDTGIGMTPEQTQKLFNKFTQADSSTtrkYGGTG 671
Cdd:cd16940      9 GDALLLFLLLRNLVDNAVRYSPQGSR-VEIK---LSADDGAV-IRVEDNGPGIDEEELEALFERFYRSDGQN---YGGSG 80
                           90       100
                   ....*....|....*....|....*.
gi 2256105915  672 LGLAISKELCLLMGGDIEVRSQFGEG 697
Cdd:cd16940     81 LGLSIVKRIVELHGGQIFLGNAQGGG 106
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
601-704 3.23e-15

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: 72.62  E-value: 3.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  601 LTNLANNAVKFT-EQGEVKITITADnlendDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKE 679
Cdd:cd16952      5 FSNLVSNAVKYTpPSDTITVRWSQE-----ESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKH 79
                           90       100
                   ....*....|....*....|....*
gi 2256105915  680 LCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16952     80 VMSRHDARLLIASELGKGSRFTCLF 104
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
728-815 5.08e-15

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: 74.99  E-value: 5.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSESLNPkIL 807
Cdd:COG0745      4 ILVVEDDPDIRELLADALEREGYEVDTA---ADGEEALELLEEER--PDLILLDLMLPGMDGLEVCRRLRARPSDIP-II 77

                   ....*...
gi 2256105915  808 MLTAYDRQ 815
Cdd:COG0745     78 MLTARDDE 85
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
343-703 5.63e-15

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: 79.39  E-value: 5.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  343 EQIEGTIKESQQRLADLIPHISDA-TQQQTLGKIKGQLTQYLALFE---QLFTQKQAIAQQSSALDNAYLKAFKVIEPDF 418
Cdd:COG5805    146 KKIEEILQEQEERLQTLIENSPDLiCVIDTDGRILFINESIERLFGaprEELIGKNLLELLHPCDKEEFKERIESITEVW 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  419 ehQQNIVENSsqisFYLAIGGIIFMSTIVFIVLLANKSHAALeksadkLAIARDEADYANQ----AKSDFL-------AN 487
Cdd:COG5805    226 --QEFIIERE----IITKDGRIRYFEAVIVPLIDTDGSVKGI------LVILRDITEKKEAeelmARSEKLsiagqlaAG 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  488 MSHEIRTPMNAIIGMSYLaLKTDLTKaQRNYIQKVKLSADTLLGLINDILDFSKIEAgkldiehVDFRLENVLDNISNLV 567
Cdd:COG5805    294 IAHEIRNPLTSIKGFLQL-LQPGIED-KEEYFDIMLSELDRIESIISEFLALAKPQA-------VNKEKENINELIQDVV 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  568 GL---KASEQGLELLIHTSKDVPTaLYGDPLRLGQILTNLANNAVKFTEQ-GEVKITITAdnlENDDVTLRfaVSDTGIG 643
Cdd:COG5805    365 TLletEAILHNIQIRLELLDEDPF-IYCDENQIKQVFINLIKNAIEAMPNgGTITIHTEE---EDNSVIIR--VIDEGIG 438
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  644 MTPEQTQKLFNKFTqadsstTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFT 703
Cdd:COG5805    439 IPEERLKKLGEPFF------TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTIT 492
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
728-845 9.10e-15

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: 71.41  E-value: 9.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQsESLNPKIL 807
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEA---DDGKEALELLKEER--PDLILLDINMPGMDGLELLKRIRR-RDPTTPVI 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2256105915  808 MLTAYDrqllADSVQERGLIV--PSILDKPVTASHLFDAI 845
Cdd:pfam00072   75 ILTAHG----DEDDAVEALEAgaDDFLSKPFDPDELLAAI 110
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
727-813 1.35e-14

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: 71.32  E-value: 1.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSL-NFNVRSANgvdSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSESL-NP 804
Cdd:cd17551      2 RILIVDDNPTNLLLLEALLRSAgYLEVVSFT---DPREALAWCRENP--PDLILLDYMMPGMDGLEFIRRLRALPGLeDV 76

                   ....*....
gi 2256105915  805 KILMLTAYD 813
Cdd:cd17551     77 PIVMITADT 85
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
487-691 1.47e-14

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 77.58  E-value: 1.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  487 NMSHEIRTPMNAIIGMSYLaLKTDLTKAQR-NYIQKVKLSADTLLGLINDILDFSKIEAGKlDIEHVD-FRLENVLDNIS 564
Cdd:PRK11100   262 TLTHELKSPLAAIRGAAEL-LQEDPPPEDRaRFTGNILTQSARLQQLIDRLLELARLEQRQ-ELEVLEpVALAALLEELV 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  565 NLVGLKASEQGLELLIHTSkdvPTALYGDPLRLGQILTNLANNAVKFT-EQGEVKITitadnLENDDVTLRFAVSDTGIG 643
Cdd:PRK11100   340 EAREAQAAAKGITLRLRPD---DARVLGDPFLLRQALGNLLDNAIDFSpEGGTITLS-----AEVDGEQVALSVEDQGPG 411
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2256105915  644 MtPEQTQ-KLFNKF-TQADSSTTRKygGTGLGLAISKELCLLMGGDIEVR 691
Cdd:PRK11100   412 I-PDYALpRIFERFySLPRPANGRK--STGLGLAFVREVARLHGGEVTLR 458
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
469-692 2.14e-14

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 77.12  E-value: 2.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  469 IARDEADYANQAksDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLG-LINDILDFSKIEAGKL 547
Cdd:PRK09835   252 IERIEDVFTRQS--NFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAkMVSDMLFLAQADNNQL 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  548 DIEHVDFRLENVLDNISNLVGLKASEQGLELLIHTSkdvPTALYGDPLRLGQILTNLANNAVKFTEQGEvkiTITADNLE 627
Cdd:PRK09835   330 IPEKKMLDLADEVGKVFDFFEAWAEERGVELRFVGD---PCQVAGDPLMLRRAISNLLSNALRYTPAGE---AITVRCQE 403
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  628 NDDvTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRS 692
Cdd:PRK09835   404 VDH-QVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTS 467
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
879-993 2.24e-14

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 71.15  E-value: 2.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNI--QVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMT 956
Cdd:COG4565      7 LIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDVDVIVIT 84
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLARWI 993
Cdd:COG4565     85 AARDPETVREALRAGVVDYLIKPFTFERLREALERYL 121
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
729-826 2.65e-14

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: 69.74  E-value: 2.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  729 LIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSESlNPKILM 808
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTA---ADGEEALELAREEQ--PDLIILDVMLPGMDGFEVCRRLREKGS-DIPIIM 74
                           90
                   ....*....|....*...
gi 2256105915  809 LTAYDrqllADSVQERGL 826
Cdd:cd17574     75 LTAKD----EEEDKVLGL 88
PRK10604 PRK10604
sensor protein RstB; Provisional
487-702 3.45e-14

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 76.18  E-value: 3.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  487 NMSHEIRTPmnaIIGMSY-LALKTDLTKAQRnyiQKVKLSADTLLGLINDILDFSKIEAGKLDIEHVDFRLENVLDniSN 565
Cdd:PRK10604   218 GIAHELRTP---LVRLRYrLEMSDNLSAAES---QALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLS--TH 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  566 LVGLKASEQGLELLIHTSkdvPTALYG--DPLRLGQILTNLANNAVKFTEQgEVKITITadnLENDDVTLRfaVSDTGIG 643
Cdd:PRK10604   290 LADIQAVTPEKTVRLDTP---HQGDYGalDMRLMERVLDNLLNNALRYAHS-RVRVSLL---LDGNQACLI--VEDDGPG 360
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2256105915  644 MTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEF 702
Cdd:PRK10604   361 IPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-703 6.22e-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: 69.24  E-value: 6.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNlannAVKFTEQGEvKITItadNLENDDVTLRFAVSDTGIGMTPEQTQKLFNK-FTQADSSTTRKygGTGLGLA 675
Cdd:cd16948     10 IGQIVSN----ALKYSKQGG-KIEI---YSETNEQGVVLSIKDFGIGIPEEDLPRVFDKgFTGENGRNFQE--STGMGLY 79
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  676 ISKELCLLMGGDIEVRSQFGEGSTFEFT 703
Cdd:cd16948     80 LVKKLCDKLGHKIDVESEVGEGTTFTIT 107
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
478-541 6.78e-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: 67.24  E-value: 6.78e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  478 NQAKSDFLANMSHEIRTPMNAIIGM-SYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSK 541
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGAlELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-697 2.29e-13

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 67.09  E-value: 2.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTeQGEVKITItadnlENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSttRKYGGTGLGLAI 676
Cdd:cd16950      1 LKRVLSNLVDNALRYG-GGWVEVSS-----DGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAI 72
                           90       100
                   ....*....|....*....|.
gi 2256105915  677 SKELCLLMGGDIEVRSQFGEG 697
Cdd:cd16950     73 VQRISDAHGGSLTLANRAGGG 93
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
878-979 2.49e-13

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 67.02  E-value: 2.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVeDNEINQELAVEL-LESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMT 956
Cdd:cd19927      1 ILLV-DDDPGIRLAVKDyLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLT 79
                           90       100
                   ....*....|....*....|...
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKP 979
Cdd:cd19927     80 AKGMTSDRIKGYNAGCDGYLSKP 102
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-703 3.47e-13

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 66.68  E-value: 3.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQgEVKITITADnlendDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAI 676
Cdd:cd16939      1 MARALDNLLRNALRYAHR-TVRIALLVS-----GGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  677 SKELCLLMGGDIEV-RSQFGeGSTFEFT 703
Cdd:cd16939     75 VHRVALWHGGHVECdDSELG-GACFRLT 101
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
878-980 4.66e-13

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: 66.65  E-value: 4.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQ--MTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIP-IIA 954
Cdd:cd19933      3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaeHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPlIVA 82
                           90       100
                   ....*....|....*....|....*.
gi 2256105915  955 MTADVMERDRERAYQSGMNDIIAKPI 980
Cdd:cd19933     83 LTANTDDSTREKCLSLGMNGVITKPV 108
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
485-676 8.55e-13

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 72.27  E-value: 8.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  485 LANMSHEIRTPMnaiigmSYLALKTDLtkAQR-----NYIQKVKLSADTLLGLINDILDFSKIEAgKLDIEHVDFRLENV 559
Cdd:PRK09470   247 LSDISHELRTPL------TRLQLATAL--LRRrqgesKELERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  560 LDNISNLVGLKASEQGLELLIhTSKDVPTALYGDPLRLGQILTNLANNAVKFTEQgEVKITITADNlenDDVTLRfaVSD 639
Cdd:PRK09470   318 WSEVLEDAKFEAEQMGKSLTV-SAPPGPWPINGNPNALASALENIVRNALRYSHT-KIEVAFSVDK---DGLTIT--VDD 390
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2256105915  640 TGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAI 676
Cdd:PRK09470   391 DGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAI 427
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
728-815 1.06e-12

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: 65.56  E-value: 1.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAAqsDSAFDVVITDWQMPGKDGVELIHAIQQSESL-NPKI 806
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEGAEVTTA---HSGEEALEAAQ--RFRPDVILSDIGMPGMDGYELARRLRELPWLaNTPA 75
                           90
                   ....*....|...
gi 2256105915  807 LMLTAY----DRQ 815
Cdd:cd17580     76 IALTGYgqpeDRE 88
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
879-981 1.19e-12

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 65.71  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMTAD 958
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTAL 78
                           90       100
                   ....*....|....*....|...
gi 2256105915  959 VMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17625     79 DAVEDRVKGLDLGADDYLPKPFS 101
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
489-709 1.28e-12

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 71.03  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  489 SHEIRTPMNAIIGMsylaLKTDLTKAQRNYIQKVklsADTLLGLINDILDFSKieagkldiehvdfrlENVLDNISNLVG 568
Cdd:COG3290    197 RHDFRNHLHTISGL----LQLGEYDEALEYIDEI---SEELQELIDSLLSRIG---------------NPVLAALLLGKA 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  569 LKASEQGLELLIHTSKDVPTALYGDPLrLGQILTNLANNA---VKFTEQGEVKITITADNLENDdvtLRFAVSDTGIGMT 645
Cdd:COG3290    255 ARARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAieaVEKLPEEERRVELSIRDDGDE---LVIEVEDSGPGIP 330
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  646 PEQTQKLFNK-FTqadsstTRKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTINMKRS 709
Cdd:COG3290    331 EELLEKIFERgFS------TKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
599-704 1.53e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 65.11  E-value: 1.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  599 QILTNLANNAVKFTEQGEVK---ITITadNLENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTqadsstTRKYGGTGLGLA 675
Cdd:cd16920      3 QVLINLVRNGIEAMSEGGCErreLTIR--TSPADDRAVTISVKDTGPGIAEEVAGQLFDPFY------TTKSEGLGMGLS 74
                           90       100
                   ....*....|....*....|....*....
gi 2256105915  676 ISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16920     75 ICRSIIEAHGGRLSVESPAGGGATFQFTL 103
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
728-812 1.75e-12

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: 64.99  E-value: 1.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHAAQsdsafDVVITDWQMPGKDGVELIHAIQQSESLNPKIL 807
Cdd:cd19919      3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQP-----DVLISDIRMPGMDGLALLAQIKQRHPDLPVII 77

                   ....*
gi 2256105915  808 MlTAY 812
Cdd:cd19919     78 M-TAH 81
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
878-979 1.87e-12

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: 65.09  E-value: 1.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQM---------TFDGILMDCQMPVLDGYSATEIIRNTLNDR 948
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlskELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2256105915  949 AIPIIAMTADVMERDRERAYQSGMNDIIAKP 979
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-707 1.87e-12

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: 65.23  E-value: 1.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQGEVkITITadnLENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAI 676
Cdd:cd16947     21 LQRILKNLISNAIKYGSDGKF-LGMT---LREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNGLGLTI 96
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2256105915  677 SKELCLLMGGDIEVRSQFGEGSTfeFTINMK 707
Cdd:cd16947     97 TKRLAESMGGSIYVNSKPYEKTV--FTVTLK 125
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
728-810 2.11e-12

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: 65.01  E-value: 2.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSA-NGVDsaidALNHAAQSdsAFDVVITDWQMPGKDGVELIHAI-QQSESLNPK 805
Cdd:cd17562      3 ILAVDDSASIRQMVSFTLRGAGYEVVEAaDGRD----ALSKAQSK--KFDLIITDQNMPNMDGIELIKELrKLPAYKFTP 76

                   ....*
gi 2256105915  806 ILMLT 810
Cdd:cd17562     77 ILMLT 81
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
728-845 3.17e-12

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: 64.46  E-value: 3.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLN-FN-VRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIqQSESLNPK 805
Cdd:cd17535      1 VLIVDDHPLVREGLRRLLESEPdIEvVGEAADGEEALALL-----RELRPDVVLMDLSMPGMDGIEALRRL-RRRYPDLK 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2256105915  806 ILMLTAYDRQLLADSVQERGliVPSILDKPVTASHLFDAI 845
Cdd:cd17535     75 VIVLTAHDDPEYVLRALKAG--AAGYLLKDSSPEELIEAI 112
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-688 3.43e-12

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


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 63.88  E-value: 3.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQgEVKITITADNlenDDVTLRfaVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAI 676
Cdd:cd16949      1 LARALENVLRNALRYSPS-KILLDISQDG---DQWTIT--ITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAI 74
                           90
                   ....*....|..
gi 2256105915  677 SKELCLLMGGDI 688
Cdd:cd16949     75 AERAIEQHGGKI 86
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
726-811 4.38e-12

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 64.28  E-value: 4.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNF-NVRSA-NGVDsAIDALNHAAqsdsaFDVVITDWQMPGKDGVELIHAIQQSESLN 803
Cdd:cd19923      1 MKVLVVDDFSTMRRIIKNLLKELGFnNVEEAeDGVD-ALEKLKAGG-----FDFVITDWNMPNMDGLELLKTIRADGALS 74
                           90
                   ....*....|
gi 2256105915  804 --PkILMLTA 811
Cdd:cd19923     75 hlP-VLMVTA 83
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
728-817 8.60e-12

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: 63.31  E-value: 8.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaQSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNP-KI 806
Cdd:cd17544      3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVL----EQHPDIKLVITDYNMPEMDGFELVREIRKKYSRDQlAI 78
                           90
                   ....*....|.
gi 2256105915  807 LMLTAYDRQLL 817
Cdd:cd17544     79 IGISASGDNAL 89
PRK13557 PRK13557
histidine kinase; Provisional
593-835 9.39e-12

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 68.93  E-value: 9.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  593 DPLRLGQILTNLANNAVKFTEQGEVkITITADNLENDD--------------VTLrfAVSDTGIGMTPEQTQKLFNKFTq 658
Cdd:PRK13557   274 DPTQAEVALLNVLINARDAMPEGGR-VTIRTRNVEIEDedlamyhglppgryVSI--AVTDTGSGMPPEILARVMDPFF- 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  659 adssTTRKYG-GTGLGLAISKELCLLMGGDIEVRSQFGEGSTFE--FTINMKRSQVLETKPIVVPTSLNHLNILIVDDNA 735
Cdd:PRK13557   350 ----TTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRlyFPASDQAENPEQEPKARAIDRGGTETILIVDDRP 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  736 SARLIVEDILQSLNFNVRSANGVDSAIDALnhaaQSDSAFDVVITDWQMPGK-DGVELIHAIQQsesLNPKI--LMLTAY 812
Cdd:PRK13557   426 DVAELARMILEDFGYRTLVASNGREALEIL----DSHPEVDLLFTDLIMPGGmNGVMLAREARR---RQPKIkvLLTTGY 498
                          250       260
                   ....*....|....*....|....*.
gi 2256105915  813 drqllADSVQERGLIVPS---ILDKP 835
Cdd:PRK13557   499 -----AEASIERTDAGGSefdILNKP 519
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
878-981 1.00e-11

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 63.11  E-value: 1.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTA 957
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100
                   ....*....|....*....|....
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYD 104
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
877-981 1.01e-11

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 62.95  E-value: 1.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLES-QNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAM 955
Cdd:cd17552      3 RILVIDDEEDIREVVQACLEKlAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILL 82
                           90       100
                   ....*....|....*....|....*.
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17552     83 TAKAQPSDRQRFASLGVAGVIAKPFD 108
PRK10610 PRK10610
chemotaxis protein CheY;
726-841 1.28e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 63.07  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNFNvrSANGVDSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSESLNP- 804
Cdd:PRK10610     6 LKFLVVDDFSTMRRIVRNLLKELGFN--NVEEAEDGVDALNKLQAGG--FGFVISDWNMPNMDGLELLKTIRADGAMSAl 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2256105915  805 KILMLTAYDRQ---LLADSVQERGLIVpsildKPVTASHL 841
Cdd:PRK10610    82 PVLMVTAEAKKeniIAAAQAGASGYVV-----KPFTAATL 116
envZ PRK09467
osmolarity sensor protein; Provisional
485-678 1.33e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 68.01  E-value: 1.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  485 LANMSHEIRTPMNAIigmsylALKTDLTKAQRNYIqkvklsADtllGLINDILDFSKIEAGKLDIEHVDFRLENVLDNIS 564
Cdd:PRK09467   233 MAGVSHDLRTPLTRI------RLATEMMSEEDGYL------AE---SINKDIEECNAIIEQFIDYLRTGQEMPMEMADLN 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  565 NLVG-LKASEQGLELLIHTS-KDVPTALYGDPLRLGQILTNLANNAVKFTEqGEVKITiTADNLEnddvTLRFAVSDTGI 642
Cdd:PRK09467   298 ALLGeVIAAESGYEREIETAlQPGPIEVPMNPIAIKRALANLVVNAARYGN-GWIKVS-SGTEGK----RAWFQVEDDGP 371
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2256105915  643 GMTPEQTQKLFNKFTQADssTTRKYGGTGLGLAISK 678
Cdd:PRK09467   372 GIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVK 405
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
877-930 1.72e-11

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 60.27  E-value: 1.72e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2256105915   877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMP 930
Cdd:smart00448    2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
723-863 1.75e-11

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 63.06  E-value: 1.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  723 LNHLNILIVDDNASARLIVEDILQSLNF--NVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQsE 800
Cdd:COG4565      1 MKMIRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALL-----AEHRPDLILLDIYLPDGDGLELLRELRA-R 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2256105915  801 SLNPKILMLTAYDRQLLADSVQERGLIvpSILDKPVTASHLFDAivglydIENHRSSRDELEQ 863
Cdd:COG4565     75 GPDVDVIVITAARDPETVREALRAGVV--DYLIKPFTFERLREA------LERYLEYRRLLRE 129
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-704 2.20e-11

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: 61.63  E-value: 2.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQgEVKITITADnLENDDVTLRFAvsDTGIGMTPEQTQKLFNKFTQADSSttRKYGGTGLGLAI 676
Cdd:cd16923      1 LQRVFSNLLSNAIKYSPE-NTRIYITSF-LTDDVVNIMFK--NPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSI 74
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  677 SKELCLLMGGDIEVRSQfGEGSTFEFTI 704
Cdd:cd16923     75 AKAIIELHGGSASAEYD-DNHDLFKVRL 101
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
726-813 2.28e-11

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 65.22  E-value: 2.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNFN--VRSANGVDSAIDALNhaaqsDSAFDVVITDWQMPGKDGVELIHAIQQSESlN 803
Cdd:COG3279      2 MKILIVDDEPLARERLERLLEKYPDLevVGEASNGEEALELLE-----EHKPDLVFLDIQMPGLDGFELARQLRELDP-P 75
                           90
                   ....*....|
gi 2256105915  804 PKILMLTAYD 813
Cdd:COG3279     76 PPIIFTTAYD 85
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
879-979 2.36e-11

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: 62.02  E-value: 2.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQ-NIQV-TVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTlndRAIPIIAMT 956
Cdd:cd17541      4 LIVDDSAVMRKLLSRILESDpDIEVvGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE---RPTPVVMVS 80
                           90       100
                   ....*....|....*....|....*.
gi 2256105915  957 ADVmERDRE---RAYQSGMNDIIAKP 979
Cdd:cd17541     81 SLT-EEGAEitlEALELGAVDFIAKP 105
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
878-985 5.10e-11

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: 60.76  E-value: 5.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAMTA 957
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN---VPIIFISS 77
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPIDVGIM 985
Cdd:cd18159     78 RDDNMDQVMAINMGGDDYITKPFDLDVL 105
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
879-982 5.65e-11

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: 60.75  E-value: 5.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTAD 958
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100
                   ....*....|....*....|....
gi 2256105915  959 VMERDRERAYQSGMNDIIAKPIDV 982
Cdd:cd19937     81 GEEFDKVLGLELGADDYITKPFSP 104
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
726-906 9.08e-11

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 62.28  E-value: 9.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNFNVrsANGVDSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQsESLNPk 805
Cdd:COG3707      4 LRVLVVDDEPLRRADLREGLREAGYEV--VAEAADGEDAVELVRELK--PDLVIVDIDMPDRDGLEAARQISE-ERPAP- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  806 ILMLTAYDRQLLADSVQERGliVPSILDKPVTASHLFDAI-VGLYDIENHRSSRDELEQ-QTHLANVQHLAGAHLLLVED 883
Cdd:COG3707     78 VILLTAYSDPELIERALEAG--VSAYLVKPLDPEDLLPALeLALARFRELRALRRELAKlREALEERKLIERAKGILMER 155
                          170       180
                   ....*....|....*....|....*
gi 2256105915  884 NEINQELAVELL--ESQNIQVTVAQ 906
Cdd:COG3707    156 RGLSEDEAYRLLrkQAMDRRVKLAE 180
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
728-835 1.03e-10

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 59.70  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHaaqsdSAFDVVITDWQMPGKDGVELIHAIQQSESLN--PK 805
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQ-----YIPDLIISDIIMPGVDGYSLLGKLRKNADFDtiPV 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 2256105915  806 ILmLTAydRQLLADSVQERGLIVPSILDKP 835
Cdd:cd19927     76 IF-LTA--KGMTSDRIKGYNAGCDGYLSKP 102
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
600-704 1.11e-10

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 59.61  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  600 ILTNLANNAVKF---TEQGEVKITITAdNLENDDVTLRfaVSDTGIGMTPEQTQKLFNKftqadSSTTRKYGGTGLGLAI 676
Cdd:cd16915      4 IVGNLIDNALDAlaaTGAPNKQVEVFL-RDEGDDLVIE--VRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLAL 75
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  677 SKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16915     76 VRQSVERLGGSITVESEPGGGTTFSIRI 103
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
727-845 1.96e-10

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: 59.21  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNV--RSANGVDSAIDALNHAAqsdsafDVVITDWQMPGKDGVELIHAIQQSESlNP 804
Cdd:cd17542      2 KVLIVDDAAFMRMMLKDILTKAGYEVvgEAANGEEAVEKYKELKP------DLVTMDITMPEMDGIEALKEIKKIDP-NA 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2256105915  805 KILMLTAYDRQ-LLADSVQE--RGLIVpsildKPVTASHLFDAI 845
Cdd:cd17542     75 KVIMCSAMGQEeMVKEAIKAgaKDFIV-----KPFQPERVLEAV 113
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
894-991 3.62e-10

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: 58.70  E-value: 3.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  894 LLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMTADVMERDRERAYQSGMN 973
Cdd:cd17593     20 LPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPV--EQLETKVIVVSGDVQPEAKERVLELGAL 97
                           90
                   ....*....|....*...
gi 2256105915  974 DIIAKPIDVGIMFSTLAR 991
Cdd:cd17593     98 AFLKKPFDPEKLAQLLEE 115
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
879-990 6.85e-10

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: 59.97  E-value: 6.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQV-TVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRntlNDRAIPIIAMTA 957
Cdd:COG3707      7 LVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQIS---EERPAPVILLTA 83
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPIDVGIMFSTLA 990
Cdd:COG3707     84 YSDPELIERALEAGVSAYLVKPLDPEDLLPALE 116
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-706 9.71e-10

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: 57.20  E-value: 9.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQGEVKITITADNLENddvTLRFAVSDTGIGMTPEQTQKLFNKFtQADSSTTRKYG-GTGLGLA 675
Cdd:cd16953      1 LGQVLRNLIGNAISFSPPDTGRITVSAMPTGK---MVTISVEDEGPGIPQEKLESIFDRF-YTERPANEAFGqHSGLGLS 76
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  676 ISKELCLLMGGDI--EVRSQFGEGSTFEFTINM 706
Cdd:cd16953     77 ISRQIIEAHGGISvaENHNQPGQVIGARFTVQL 109
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
726-837 1.04e-09

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 57.41  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNFNVRSangVDSAIDALNHAAQSDSAFDVVITDWQMPGKDGVELIHAIQQ--SESLN 803
Cdd:cd19933      1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTT---VSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKlfGRRER 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2256105915  804 PKILMLTAydrqLLADSVQERGLI--VPSILDKPVT 837
Cdd:cd19933     78 PLIVALTA----NTDDSTREKCLSlgMNGVITKPVS 109
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
727-825 1.11e-09

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 57.11  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSA-NGVDsAIDALNhaaqsDSAFDVVITDWQMPGKDGVELIHAIQQSESlNPK 805
Cdd:COG5803      4 KILIVDDQAGIRMLLKEVLKKEGYEVFQAaNGKE-ALEKVK-----ELKPDLVLLDMKMPGMDGIEILKEIKEIDP-DIP 76
                           90       100
                   ....*....|....*....|
gi 2256105915  806 ILMLTAYDRQLLADSVQERG 825
Cdd:COG5803     77 VIMMTAYGELDMVEEAKELG 96
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
728-808 1.21e-09

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: 57.12  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNhaaqsDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPKIL 807
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIK-----ERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIM 75

                   .
gi 2256105915  808 M 808
Cdd:cd17550     76 I 76
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
878-982 2.02e-09

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 61.40  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMTA 957
Cdd:PRK11361     7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRS--HETRTPVILMTA 84
                           90       100
                   ....*....|....*....|....*
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPIDV 982
Cdd:PRK11361    85 YAEVETAVEALRCGAFDYVIKPFDL 109
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
728-808 2.46e-09

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: 56.10  E-value: 2.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAQSDSAFDVVITDWQMPGKDGVELIHAIQQSESLnPKIL 807
Cdd:cd17584      1 VLVVDDDPTCLAILKRMLLRCGYQVTTCT---DAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRLEMDL-PVIM 76

                   .
gi 2256105915  808 M 808
Cdd:cd17584     77 M 77
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
728-826 2.95e-09

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 55.52  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNV-RSANGvdsaIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQSESLNPkI 806
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLTEEGYAVdVAYDG----EDGLHLALTNE--YDLIILDVMLPGLDGLEVLRRLRAAGKQTP-V 73
                           90       100
                   ....*....|....*....|..
gi 2256105915  807 LMLTAydrqllADSVQER--GL 826
Cdd:cd19935     74 LMLTA------RDSVEDRvkGL 89
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
599-702 3.15e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 55.54  E-value: 3.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  599 QILTNLANNAVKFTEQGEV-KITITADnLENDDVTLRfaVSDTGIGMTPEQTQKLFNKFTqadssTTRKYG-GTGLGLAI 676
Cdd:cd16976      3 QVLMNLLQNALDAMGKVENpRIRIAAR-RLGGRLVLV--VRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGLSI 74
                           90       100
                   ....*....|....*....|....*.
gi 2256105915  677 SKELCLLMGGDIEVRSQFGEGSTFEF 702
Cdd:cd16976     75 SYGIVEEHGGRLSVANEEGAGARFTF 100
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
728-813 3.88e-09

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 55.81  E-value: 3.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDIL--QSLNFNV--RSANGVDsAIDALNHaaqsdSAFDVVITDWQMPGKDGVELIHAIQQsESLN 803
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIdwEELGFEVvgEAENGEE-ALELIEE-----HKPDIVITDIRMPGMDGLELIEKIRE-LYPD 73
                           90
                   ....*....|
gi 2256105915  804 PKILMLTAYD 813
Cdd:cd17536     74 IKIIILSGYD 83
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
878-991 4.27e-09

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: 55.46  E-value: 4.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraiPIIAMTA 957
Cdd:cd17622      3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG---PILLLTA 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPIDVGIMfstLAR 991
Cdd:cd17622     80 LDSDIDHILGLELGADDYVVKPVEPAVL---LAR 110
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
727-811 5.36e-09

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: 55.33  E-value: 5.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNhaaqsDSAFDVVITDWQMPGKDGVELIHAIQQSESLN--P 804
Cdd:cd17618      2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIV-----EPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRdiP 76

                   ....*..
gi 2256105915  805 kILMLTA 811
Cdd:cd17618     77 -IIMLTA 82
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
878-989 5.92e-09

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: 55.11  E-value: 5.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTV-AQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRntlNDRAIPIIAMT 956
Cdd:cd19932      3 VLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT---SENIAPIVLLT 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKPIDVGIMFSTL 989
Cdd:cd19932     80 AYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
877-983 6.02e-09

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: 55.15  E-value: 6.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYsatEIIRNTLNDRAIPIIAMT 956
Cdd:cd17594      1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGL---DLLRTIRARSDVPIIIIS 77
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  957 ADVM-ERDRERAYQSGMNDIIAKPIDVG 983
Cdd:cd17594     78 GDRRdEIDRVVGLELGADDYLAKPFGLR 105
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
489-692 6.45e-09

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 60.09  E-value: 6.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  489 SHEIRTPMNAIIGMSY---LALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKieagKLDIEHVDFRLENVLDNISN 565
Cdd:COG4192    441 AHELNQPLNAMSMYLFsakKALEQENYAQLPTSLDKIEGLIERMDKIIKSLRQFSR----KSDTPLQPVDLRQVIEQAWE 516
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  566 LVGLKASEQGLELLIHTSKDVPtalyGDPLRLGQILTNLANNAVkftEQGEVKITITADNLENDDvTLRFAVSDTGIGMt 645
Cdd:COG4192    517 LVESRAKPQQITLHIPDDLMVQ----GDQVLLEQVLVNLLVNAL---DAVATQPQISVDLLSNAE-NLRVAISDNGNGW- 587
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2256105915  646 pEQTQKLFNKFTqadsstTRKYGGTGLGLAISKELCLLMGGDIEVRS 692
Cdd:COG4192    588 -PLVDKLFTPFT------TTKEVGLGLGLSICRSIMQQFGGDLYLAS 627
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
876-980 6.65e-09

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: 54.90  E-value: 6.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIAM 955
Cdd:cd17555      1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPD--TPVIVV 78
                           90       100
                   ....*....|....*....|....*
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPI 980
Cdd:cd17555     79 SGAGVMSDAVEALRLGAWDYLTKPI 103
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
482-704 7.63e-09

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: 60.14  E-value: 7.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  482 SDFLANMS----HEIRTPMnAIIGMSYLALKT-DLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKLDIEHVDFRL 556
Cdd:TIGR03785  482 THYLENMSsrlsHELRTPV-AVVRSSLENLELqALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDL 560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  557 ENVLDNISNLVGLKASEQGLELLIHTSkdvPTALYGDPLRLGQILTNLANNAVKFT-EQGEVKITITadnlENDDVTLRF 635
Cdd:TIGR03785  561 SEVLSGCMQGYQMTYPPQRFELNIPET---PLVMRGSPELIAQMLDKLVDNAREFSpEDGLIEVGLS----QNKSHALLT 633
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  636 aVSDTGIGMTPEQTQKLFNKFTQADSSTTRKYGGTGLGLAISKELCLLMGGDIEVRSQF-GEGSTFEFTI 704
Cdd:TIGR03785  634 -VSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISL 702
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
876-991 8.62e-09

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: 54.56  E-value: 8.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAM 955
Cdd:cd17618      1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPidvgimFST---LAR 991
Cdd:cd17618     81 TARGEEEDKVRGLEAGADDYITKP------FSPrelVAR 113
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
728-813 8.92e-09

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: 54.04  E-value: 8.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAAQsdSAFDVVITDWQMPGKDGVELIHAIQQSESLN--Pk 805
Cdd:cd17538      2 ILVVDDEPANRELLEALLSAEGYEVLTA---DSGQEALALAEE--ELPDLILLDVMMPGMDGFEVCRRLKEDPETRhiP- 75

                   ....*...
gi 2256105915  806 ILMLTAYD 813
Cdd:cd17538     76 VIMITALD 83
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
727-823 1.14e-08

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 54.33  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNasarlivEDILQSLN-------FNVRSANgvdSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQs 799
Cdd:cd17569      2 TILLVDDE-------PNILKALKrllrregYEVLTAT---SGEEALEILKQEP--VDVVISDQRMPGMDGAELLKRVRE- 68
                           90       100
                   ....*....|....*....|....*..
gi 2256105915  800 esLNPKI--LMLTAY-DRQLLADSVQE 823
Cdd:cd17569     69 --RYPDTvrILLTGYaDLDAAIEAINE 93
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
890-979 1.20e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 58.35  E-value: 1.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  890 LAVELL-----ESQNIQVT-VAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATeiiRNTLNDRAIPIIAMTADVmERD 963
Cdd:PRK12555    11 LAVEALrralaRDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEAT---RRIMAERPCPILIVTSLT-ERN 86
                           90
                   ....*....|....*....
gi 2256105915  964 RERAYQS---GMNDIIAKP 979
Cdd:PRK12555    87 ASRVFEAmgaGALDAVDTP 105
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
727-812 1.51e-08

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: 55.69  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQsesLNP-- 804
Cdd:COG4567      6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALL-----EQAPPDYAVLDLRLGDGSGLDLIEALRE---RDPda 77

                   ....*...
gi 2256105915  805 KILMLTAY 812
Cdd:COG4567     78 RIVVLTGY 85
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
877-979 1.63e-08

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: 53.92  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAMT 956
Cdd:cd19938      1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSD---VPIIMVT 77
                           90       100
                   ....*....|....*....|...
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKP 979
Cdd:cd19938     78 ARVEEIDRLLGLELGADDYICKP 100
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
728-845 1.63e-08

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: 53.75  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRsanGVDSAIDALNHAaqSDSAFDVVITDWQMPGKDGVELIHAIQQSESlNPKIL 807
Cdd:cd17537      3 VYVVDDDEAVRDSLAFLLRSVGLAVK---TFTSASAFLAAA--PPDQPGCLVLDVRMPGMSGLELQDELLARGS-NIPII 76
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2256105915  808 MLTAY-DRQLLADSVQeRGLIvpSILDKPVTASHLFDAI 845
Cdd:cd17537     77 FITGHgDVPMAVEAMK-AGAV--DFLEKPFRDQVLLDAI 112
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
597-700 2.16e-08

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: 53.54  E-value: 2.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQGEvKITITADNLENDDVT------------LRFAVSDTGIGMTPEQTQKLFNKFTqadssTT 664
Cdd:cd16919      1 LELAILNLAVNARDAMPEGG-RLTIETSNQRVDADYalnyrdlipgnyVCLEVSDTGSGMPAEVLRRAFEPFF-----TT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2256105915  665 RKYG-GTGLGLAISKELCLLMGGDIEVRSQFGEGSTF 700
Cdd:cd16919     75 KEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTV 111
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
728-836 2.68e-08

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: 52.73  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaQSDSAFDVVITDWQMPGK-DGVELihaIQQSESLNPKI 806
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLL----ESGPDIDLLVTDVIMPGGmNGSQL---AEEARRRRPDL 73
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2256105915  807 --LMLTAYDRQLLADSVQERGLIVpsiLDKPV 836
Cdd:cd18161     74 kvLLTSGYAENAIEGGDLAPGVDV---LSKPF 102
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
878-979 2.72e-08

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: 53.16  E-value: 2.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIAMTA 957
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGND--LPILVLTA 78
                           90       100
                   ....*....|....*....|..
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKP 979
Cdd:cd17627     79 RDSVSDRVAGLDAGADDYLVKP 100
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
728-808 3.06e-08

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 53.26  E-value: 3.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARlivEDILQSLN---FNVRSAngvDSAIDALnhAAQSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNP 804
Cdd:cd17549      1 VLLVDDDADVR---EALQQTLElagFRVRAF---ADAEEAL--AALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLP 72

                   ....
gi 2256105915  805 KILM 808
Cdd:cd17549     73 VILI 76
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
728-835 3.54e-08

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: 52.50  E-value: 3.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaQSDSAFDVVITDWQMPGKDGVELIHAIQQsesLNP--K 805
Cdd:cd18160      2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKL----QQGKDIDIVVTDIVMPEMDGIELAREARK---IDPdvK 74
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  806 ILMLTAYDR---QLLADSVQERGlivpsILDKP 835
Cdd:cd18160     75 ILFISGGAAaapELLSDAVGDNA-----TLKKP 102
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
878-979 4.13e-08

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 52.20  E-value: 4.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPvldGYSATEIIRNTLNDRAIPIIAMTA 957
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLP---GLSGTEVCRQLRARSNVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKP 979
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
728-811 4.37e-08

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 52.69  E-value: 4.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHaaqsdSAFDVVITDWQMPGKDGVELIHAIQQSESLnpKIL 807
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLE-----GSPDLVVLDVMLPKMNGLDVLKELRKTSQV--PVL 73

                   ....
gi 2256105915  808 MLTA 811
Cdd:cd17623     74 MLTA 77
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
593-688 4.52e-08

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: 52.46  E-value: 4.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  593 DPLRLGQILTNLANNAVKFT-EQGEVKITItadnlENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTQADSSTTRKyGGTG 671
Cdd:cd16975      1 DTLLLSRALINIISNACQYApEGGTVSISI-----YDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GHYG 74
                           90
                   ....*....|....*..
gi 2256105915  672 LGLAISKELCLLMGGDI 688
Cdd:cd16975     75 MGLYIAKNLVEKHGGSL 91
pleD PRK09581
response regulator PleD; Reviewed
728-981 4.56e-08

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 57.22  E-value: 4.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAQSDSafDVVITDWQMPGKDGVELIHAIQQseslNPK-- 805
Cdd:PRK09581     5 ILVVDDIPANVKLLEAKLLAEYYTVLTAS---SGAEAIAICEREQP--DIILLDVMMPGMDGFEVCRRLKS----DPAtt 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  806 ---ILMLTAYDRqlLADSVqeRGLIVPS--ILDKPVTASHLFDAIVGLYDIenhRSSRDELEQQ---THLANVQHL---- 873
Cdd:PRK09581    76 hipVVMVTALDD--PEDRV--RGLEAGAddFLTKPINDVALFARVKSLTRL---KMVIDELRLRastNAEIGVTALmima 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  874 -----AGAHLLLVEDNEINQELAVELLeSQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDR 948
Cdd:PRK09581   149 yankdEDGRILLVDDDVSQAERIANIL-KEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTR 227
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2256105915  949 AIPIIAMtADVMERDR-ERAYQSGMNDIIAKPID 981
Cdd:PRK09581   228 YVPILLL-VDEDDDPRlVKALELGVNDYLMRPID 260
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
726-785 4.91e-08

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: 50.64  E-value: 4.91e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915   726 LNILIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAAQSDsaFDVVITDWQMP 785
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLEKEGYEVDEA---TDGEEALELLKEEK--PDLILLDIMMP 55
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
878-979 5.94e-08

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: 52.04  E-value: 5.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAMTA 957
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSN---VPIIMLTA 77
                           90       100
                   ....*....|....*....|..
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKP 979
Cdd:cd17614     78 KDSEVDKVLGLELGADDYVTKP 99
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
879-979 6.06e-08

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: 52.52  E-value: 6.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMT-FDGILMDCQMPVLDGYSATEIIRNTLNDRAIPII---- 953
Cdd:cd17544      4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIgisa 83
                           90       100       110
                   ....*....|....*....|....*....|
gi 2256105915  954 ----AMTAdvmerdreRAYQSGMNDIIAKP 979
Cdd:cd17544     84 sgdnALSA--------RFIKAGANDFLTKP 105
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
876-957 6.08e-08

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: 52.22  E-value: 6.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTlnDRAIPIIAM 955
Cdd:cd17554      1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK--KPDLPVIIC 78

                   ..
gi 2256105915  956 TA 957
Cdd:cd17554     79 TA 80
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
728-808 6.90e-08

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: 52.37  E-value: 6.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSangVDSAIDAL---------NHAAQSDSAFDVVITDWQMPGKDGVELIHAIQQ 798
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLRISSCRVTA---VDSGKRALeflgledeeDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKE 77
                           90
                   ....*....|..
gi 2256105915  799 SESLN--PKILM 808
Cdd:cd17581     78 SSALKeiPVVIM 89
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
571-704 7.34e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 56.46  E-value: 7.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  571 ASEQGLELLIHTSKDVPTAlyGDP---LRLGQILTNLANN---AVKFTEQGEVKITitadnLENDDVTLRFAVSDTGIGM 644
Cdd:PRK11086   407 ARELGITLIISEDSQLPDS--GDEdqvHELITILGNLIENaleAVGGEEGGEISVS-----LHYRNGWLHCEVSDDGPGI 479
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  645 TPEQTQKLFNKftqaDSSTtrKYGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:PRK11086   480 APDEIDAIFDK----GYST--KGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
878-979 8.43e-08

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 51.90  E-value: 8.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDN-EINQELAVELLESQNiQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMT 956
Cdd:cd19934      1 LLLVEDDaLLAAQLKEQLSDAGY-VVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRS--EGRATPVLILT 77
                           90       100
                   ....*....|....*....|...
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKP 979
Cdd:cd19934     78 ARDSWQDKVEGLDAGADDYLTKP 100
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
726-845 8.68e-08

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 51.65  E-value: 8.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNFNV--RSANGVDSAIDALNHAAqsdsafDVVITDWQMPGKDGVELIHAIQQsESLN 803
Cdd:cd19932      1 VRVLIAEDEALIRMDLREMLEEAGYEVvgEASDGEEAVELAKKHKP------DLVIMDVKMPRLDGIEAAKIITS-ENIA 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2256105915  804 PkILMLTAYDRQLLADSVQERGliVPSILDKPVTASHLFDAI 845
Cdd:cd19932     74 P-IVLLTAYSQQDLVERAKEAG--AMAYLVKPFSESDLIPAI 112
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
727-813 8.88e-08

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: 51.45  E-value: 8.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPkI 806
Cdd:cd17554      2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKL-----ESEDPDLVILDIKMPGMDGLETLRKIREKKPDLP-V 75

                   ....*..
gi 2256105915  807 LMLTAYD 813
Cdd:cd17554     76 IICTAYS 82
fixJ PRK09390
response regulator FixJ; Provisional
727-808 9.32e-08

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 53.85  E-value: 9.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSangVDSAIDALNHAAqsDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPKI 806
Cdd:PRK09390     5 VVHVVDDDEAMRDSLAFLLDSAGFEVRL---FESAQAFLDALP--GLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVI 79

                   ..
gi 2256105915  807 LM 808
Cdd:PRK09390    80 VM 81
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
878-981 1.27e-07

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: 51.15  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAMTA 957
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQ---VPVLMLTA 77
                           90       100
                   ....*....|....*....|....
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17623     78 RGDDIDRILGLELGADDYLPKPFN 101
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
593-691 1.36e-07

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 50.92  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  593 DPLRLGQILTNLANNAVKFT-EQGEVKITITADNlenDDVTLRfaVSDTGIGMTPEQTQKLFNKFTqadsSTTRKYGG-- 669
Cdd:cd16945      1 DPFLLRQAINNLLDNAIDFSpEGGLIALQLEADT---EGIELL--VFDEGSGIPDYALNRVFERFY----SLPRPHSGqk 71
                           90       100
                   ....*....|....*....|...
gi 2256105915  670 -TGLGLAISKELCLLMGGDIEVR 691
Cdd:cd16945     72 sTGLGLAFVQEVAQLHGGRITLR 94
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
877-979 1.49e-07

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 51.22  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGysaTEIIRNTLNDRAIPIIAMT 956
Cdd:cd19939      1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDG---LTVCREVREHSHVPILMLT 77
                           90       100
                   ....*....|....*....|...
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKP 979
Cdd:cd19939     78 ARTEEMDRVLGLEMGADDYLCKP 100
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
1044-1123 1.59e-07

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


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 50.04  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915 1044 RLLQRFY-EHYSDLSQVREQLANAASSDLKRYIHSLKGVSGNIGANELFELCSALESDINNEQLQK--KLLNALNQTTEA 1120
Cdd:pfam01627    1 ELLELFLeEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGELPLdpELLEALRDLLEA 80

                   ...
gi 2256105915 1121 IRE 1123
Cdd:pfam01627   81 LRA 83
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
593-704 1.80e-07

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 50.61  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  593 DPLRLGQILTNLANNAVKFTE-----QGEVKITITADNLENDDVTlrfaVSDTGIGMTPEQTQKLFnkftqaDSSTTRKY 667
Cdd:cd16944      1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRVEADQDGRIVLI----VCDNGKGFPREMRHRAT------EPYVTTRP 70
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2256105915  668 GGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16944     71 KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
878-982 1.89e-07

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: 50.56  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMTA 957
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTA 78
                           90       100
                   ....*....|....*....|....*
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPIDV 982
Cdd:cd17624     79 RDGVDDRVAGLDAGADDYLVKPFAL 103
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
728-825 2.66e-07

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 50.07  E-value: 2.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHAAQSDSA----FDVVITDWQMPGKDGVELIHAIQQSESL- 802
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGNDlskeLDLIITDIEMPKMDGYELTFELRDDPRLa 80
                           90       100
                   ....*....|....*....|...
gi 2256105915  803 NPKILMLTAYDRQLLADSVQERG 825
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVG 103
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
879-981 4.03e-07

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 49.97  E-value: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTV-AQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSAT-EIIRNTLNDRAIPIIAMT 956
Cdd:cd17542      4 LIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALkEIKKIDPNAKVIMCSAMG 83
                           90       100
                   ....*....|....*....|....*
gi 2256105915  957 ADVMERDrerAYQSGMNDIIAKPID 981
Cdd:cd17542     84 QEEMVKE---AIKAGAKDFIVKPFQ 105
ompR PRK09468
osmolarity response regulator; Provisional
875-979 5.70e-07

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 51.90  E-value: 5.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  875 GAHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIA 954
Cdd:PRK09468     5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNP--TPIIM 82
                           90       100
                   ....*....|....*....|....*
gi 2256105915  955 MTADVMERDRERAYQSGMNDIIAKP 979
Cdd:PRK09468    83 LTAKGEEVDRIVGLEIGADDYLPKP 107
glnL PRK11073
nitrogen regulation protein NR(II);
479-704 6.04e-07

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 53.16  E-value: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  479 QAKSDFLANMSHEIRTPMNAIIGMSYLALKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKieAGKldieHVDFRLEN 558
Cdd:PRK11073   128 VAARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLLGPQR--PGT----HVTESIHK 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  559 VLDNISNLVGLKASEQgleLLIHTSKDvPT--ALYGDPLRLGQILTNLANNAVKFTEQGEVKITI---TADNLENDDVTL 633
Cdd:PRK11073   202 VAERVVQLVSLELPDN---VRLIRDYD-PSlpELAHDPDQIEQVLLNIVRNALQALGPEGGTITLrtrTAFQLTLHGERY 277
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  634 RFA----VSDTGIGMTPEQTQKLFNKFTQAdssttrKYGGTGLGLAISKELCLLMGGDIEVRSQfgEGSTfEFTI 704
Cdd:PRK11073   278 RLAaridIEDNGPGIPPHLQDTLFYPMVSG------REGGTGLGLSIARNLIDQHSGKIEFTSW--PGHT-EFSV 343
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
876-991 6.28e-07

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: 49.22  E-value: 6.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAM 955
Cdd:cd17562      1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPIDVGIMFSTLAR 991
Cdd:cd17562     81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKK 116
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
726-841 6.33e-07

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 49.36  E-value: 6.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNF-NVRSANGVDSAIDALNHAAQsdsafDVVITDWQMPGKDGVELIHAIQQSESLNP 804
Cdd:cd17530      1 LRVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAP-----DIIICDLKMPDMDGIEFLRHLAESHSNAA 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2256105915  805 KILMlTAYD---RQLLADSVQERGLIVPSILDKPVTASHL 841
Cdd:cd17530     76 VILM-SGLDggiLESAETLAGANGLNLLGTLSKPFSPEEL 114
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
902-979 6.38e-07

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: 49.26  E-value: 6.38e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2256105915  902 VTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTADVMERDRERAYQSGMNDIIAKP 979
Cdd:cd19923     28 VEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKP 105
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
727-812 6.77e-07

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: 48.98  E-value: 6.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQsesLNP-- 804
Cdd:cd17563      2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALA-----REEKPDYAVLDLRLGGDSGLDLIPPLRA---LQPda 73

                   ....*...
gi 2256105915  805 KILMLTAY 812
Cdd:cd17563     74 RIVVLTGY 81
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
728-813 7.23e-07

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: 48.60  E-value: 7.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHaaqsdSAFDVVITDWQMPGKDGVELIHAIQQSESLnpKIL 807
Cdd:cd19936      1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNA-----RPPDLAILDIKMPRMDGMELLQRLRQKSTL--PVI 73

                   ....*.
gi 2256105915  808 MLTAYD 813
Cdd:cd19936     74 FLTSKD 79
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
728-813 7.50e-07

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: 48.92  E-value: 7.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPkIL 807
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVI-----SGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLP-IL 74

                   ....*.
gi 2256105915  808 MLTAYD 813
Cdd:cd17627     75 VLTARD 80
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
727-845 7.56e-07

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: 49.34  E-value: 7.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNF--NVRSA-NGVDsAIDALNHAAQSDSAF--DVVITDWQMPGKDGVELIHAIQQSES 801
Cdd:cd17557      1 TILLVEDNPGDAELIQEAFKEAGVpnELHVVrDGEE-ALDFLRGEGEYADAPrpDLILLDLNMPRMDGFEVLREIKADPD 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2256105915  802 LN--PkILMLTAYDRQ---LLADSVQERGLIVpsildKPVTASHLFDAI 845
Cdd:cd17557     80 LRriP-VVVLTTSDAEediERAYELGANSYIV-----KPVDFEEFVEAI 122
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
876-979 7.97e-07

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: 49.01  E-value: 7.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRntlNDRAIPIIAM 955
Cdd:cd17626      1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR---AESGVPIVML 77
                           90       100
                   ....*....|....*....|....
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKP 979
Cdd:cd17626     78 TAKSDTVDVVLGLESGADDYVAKP 101
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
878-979 8.41e-07

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: 48.76  E-value: 8.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDN-EINQELAVELLESQNIQVT-VAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAM 955
Cdd:cd17561      4 VLIADDNrEFVQLLEEYLNSQPDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIML 83
                           90       100
                   ....*....|....*....|....
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKP 979
Cdd:cd17561     84 TAFGQEDITQRAVELGASYYILKP 107
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
879-981 9.76e-07

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: 48.56  E-value: 9.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVT-VAQNGQVAIDLYKQMTFDGILMDCQMP-VLDGYSATEIIRNTLNdraIPIIAMT 956
Cdd:cd17534      4 LIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD---IPVIFLT 80
                           90       100
                   ....*....|....*....|....*
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17534     81 AYSDEETLERAKETNPYGYLVKPFN 105
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
727-815 1.02e-06

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: 48.93  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSL-NFNVrsangVDSA---IDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQQsesL 802
Cdd:cd17541      2 RVLIVDDSAVMRKLLSRILESDpDIEV-----VGTArdgEEALEKIKELK--PDVITLDIEMPVMDGLEALRRIMA---E 71
                           90
                   ....*....|....
gi 2256105915  803 NP-KILMLTAYDRQ 815
Cdd:cd17541     72 RPtPVVMVSSLTEE 85
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
728-811 1.06e-06

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 48.53  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHAAQsdsafDVVITDWQMPGKDGVELIHAIQQSESLnpKIL 807
Cdd:cd19938      2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPP-----DLILLDLMLPGTDGLTLCREIRRFSDV--PII 74

                   ....
gi 2256105915  808 MLTA 811
Cdd:cd19938     75 MVTA 78
PRK11517 PRK11517
DNA-binding response regulator HprR;
878-979 1.23e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 50.67  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYsatEIIRNTLNDRAIPIIAMTA 957
Cdd:PRK11517     3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGW---QILQTLRTAKQTPVICLTA 79
                           90       100
                   ....*....|....*....|..
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKP 979
Cdd:PRK11517    80 RDSVDDRVRGLDSGANDYLVKP 101
pleD PRK09581
response regulator PleD; Reviewed
876-981 1.38e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 52.21  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINqelaVELLE----SQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIP 951
Cdd:PRK09581     3 ARILVVDDIPAN----VKLLEakllAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIP 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 2256105915  952 IIAMTADVMERDRERAYQSGMNDIIAKPID 981
Cdd:PRK09581    79 VVMVTALDDPEDRVRGLEAGADDFLTKPIN 108
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
879-982 1.43e-06

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: 48.39  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDL--YKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAMT 956
Cdd:cd17584      2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMlrENKDEFDLVITDVHMPDMDGFEFLELIRLEMD---LPVIMMS 78
                           90       100
                   ....*....|....*....|....*.
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKPIDV 982
Cdd:cd17584     79 ADGSTSTVMKGLAHGACDYLLKPVSI 104
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
591-689 1.53e-06

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


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 48.04  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  591 YGDPLRLGQILTNLANNAVKFT--EQG--EVKITITADNLENDD--VTLRFAVSDTGIGMTPEQTQKLFNKftqaDSSTT 664
Cdd:cd16932      1 YGDQIRLQQVLADFLLNAVRFTpsPGGwvEIKVSPTKKQIGDGVhvIHLEFRITHPGQGLPEELVQEMFEE----NQWTT 76
                           90       100
                   ....*....|....*....|....*
gi 2256105915  665 RKyggtGLGLAISKELCLLMGGDIE 689
Cdd:cd16932     77 QE----GLGLSISRKLVKLMNGDVR 97
ompR PRK09468
osmolarity response regulator; Provisional
728-811 1.55e-06

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 50.74  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSA-NGvdsaiDALNHAAQSDSaFDVVITDWQMPGKDGVELIHAIQQSESLNPkI 806
Cdd:PRK09468     8 ILVVDDDMRLRALLERYLTEQGFQVRSAaNA-----EQMDRLLTRES-FHLMVLDLMLPGEDGLSICRRLRSQNNPTP-I 80

                   ....*
gi 2256105915  807 LMLTA 811
Cdd:PRK09468    81 IMLTA 85
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
878-979 1.56e-06

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 50.49  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTA 957
Cdd:PRK10161     5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                           90       100
                   ....*....|....*....|..
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKP 979
Cdd:PRK10161    85 RGEEEDRVRGLETGADDYITKP 106
PRK10337 PRK10337
sensor protein QseC; Provisional
484-705 2.08e-06

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 51.57  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  484 FLANMSHEIRTPMNAIIGMSYLA-LKTDLTKAQRNYIQKVKLSADTLLGLINDILDFSKIEAGKL--DIEHVDFR--LEN 558
Cdd:PRK10337   240 FTSDAAHELRSPLAALKVQTEVAqLSDDDPQARKKALLQLHAGIDRATRLVDQLLTLSRLDSLDNlqDVAEIPLEdlLQS 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  559 VLDNISNlvglKASEQGLELLIHTSkDVPTALYGDPLRLGQILTNLANNAVKFTEQG-EVKITITADnlenddvtlRFAV 637
Cdd:PRK10337   320 AVMDIYH----TAQQAGIDVRLTLN-AHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGsVVDVTLNAR---------NFTV 385
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  638 SDTGIGMTPEQTQKLFNKFTQADSSTTRkygGTGLGLAISKELCLLMGgdieVRSQFG--EGSTFEFTIN 705
Cdd:PRK10337   386 RDNGPGVTPEALARIGERFYRPPGQEAT---GSGLGLSIVRRIAKLHG----MNVSFGnaPEGGFEAKVS 448
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
727-864 2.25e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 51.80  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPKI 806
Cdd:PRK10923     5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEAL-----ASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVI 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  807 LMlTAYdrqlladsvqerglivpSILDKPVTASH--LFDAIVGLYDIEN-----HRSSRDELEQQ 864
Cdd:PRK10923    80 IM-TAH-----------------SDLDAAVSAYQqgAFDYLPKPFDIDEavalvERAISHYQEQQ 126
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
879-981 2.44e-06

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: 47.51  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQN-IQVtVAQ--NGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIAM 955
Cdd:cd17535      2 LIVDDHPLVREGLRRLLESEPdIEV-VGEaaDGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPD--LKVIVL 78
                           90       100
                   ....*....|....*....|....*.
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17535     79 TAHDDPEYVLRALKAGAAGYLLKDSS 104
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
727-845 2.52e-06

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: 47.40  E-value: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVrsANGVDSAIDALNHAAQSDSafDVVITDWQMPGK-DGVELIHAIQqsESLNPK 805
Cdd:cd17534      2 KILIVEDEAIIALDLKEILESLGYEV--VGIADSGEEAIELAEENKP--DLILMDINLKGDmDGIEAAREIR--EKFDIP 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2256105915  806 ILMLTAY-DRQLL--ADSVQERGLIVpsildKPVTASHLFDAI 845
Cdd:cd17534     76 VIFLTAYsDEETLerAKETNPYGYLV-----KPFNERELKAAI 113
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
878-979 2.54e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 50.07  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAMTA 957
Cdd:PRK10710    13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSD---IPIVMVTA 89
                           90       100
                   ....*....|....*....|..
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKP 979
Cdd:PRK10710    90 KIEEIDRLLGLEIGADDYICKP 111
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
878-981 2.64e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 49.80  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQmTFDGILMDCQMPVLDGYSATEIIRNTlndRAIPIIAMTA 957
Cdd:PRK10955     4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQT---HQTPVIMLTA 79
                           90       100
                   ....*....|....*....|....
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPID 981
Cdd:PRK10955    80 RGSELDRVLGLELGADDYLPKPFN 103
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
881-979 2.85e-06

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: 46.98  E-value: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  881 VEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTADVM 960
Cdd:cd17602      4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDG 83
                           90
                   ....*....|....*....
gi 2256105915  961 ERDRERAYQSGMNDIIAKP 979
Cdd:cd17602     84 LVDRIRAKMAGASGYLTKP 102
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
586-704 3.13e-06

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


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 47.84  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  586 VPTALYGDPLRLGQILTNLANNAVKFTEQG---EVKITITADNLE--------------NDDVTLRFAVSDTGIGmtpEQ 648
Cdd:cd16938      1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGgniTFRVFLEGGSEDrsdrdwgpwrpsmsDESVEIRFEVEINDSG---SP 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  649 TQKLFNKFtqadSSTTRKYG----GTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16938     78 SIESASMR----NSLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
728-812 3.37e-06

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 46.76  E-value: 3.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPkIL 807
Cdd:cd19926      1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELL-----ASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTP-VA 74

                   ....*
gi 2256105915  808 MLTAY 812
Cdd:cd19926     75 VITAY 79
orf27 CHL00148
Ycf27; Reviewed
877-979 4.23e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 49.33  E-value: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAMT 956
Cdd:CHL00148     8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESD---VPIIMLT 84
                           90       100
                   ....*....|....*....|...
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKP 979
Cdd:CHL00148    85 ALGDVSDRITGLELGADDYVVKP 107
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
726-796 4.83e-06

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: 47.19  E-value: 4.83e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2256105915  726 LNILIVDDNASARLIVEDILQSL-NFNV-RSANGVDSAIDALNHAAqsdsaFDVVITDWQMPGKDGVELIHAI 796
Cdd:COG2197      2 IRVLIVDDHPLVREGLRALLEAEpDIEVvGEAADGEEALELLEELR-----PDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
728-824 5.68e-06

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: 46.32  E-value: 5.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNasaRLIVEDILQSLNFNVRSANGVDSAIDALnhAAQSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPkIL 807
Cdd:cd17624      1 ILLVEDD---ALLGDGLKTGLRKAGYAVDWVRTGAEAE--AALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLP-VL 74
                           90
                   ....*....|....*..
gi 2256105915  808 MLTAYDRqlladsVQER 824
Cdd:cd17624     75 ILTARDG------VDDR 85
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
728-813 7.05e-06

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 46.38  E-value: 7.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNfNVRSANGVDSAIDALNhaAQSDSAFDVVITDWQMPGKDGVELIHAIQQSESLnPKIL 807
Cdd:cd17532      1 ALIVDDEPLAREELRYLLEEHP-DIEIVGEAENGEEALE--AIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKP-PLIV 76

                   ....*.
gi 2256105915  808 MLTAYD 813
Cdd:cd17532     77 FVTAYD 82
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
893-979 7.11e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 49.76  E-value: 7.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  893 ELLESQ-NIQVT-VAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIrntLNDRAIPII---AMTadvmERDRE-- 965
Cdd:PRK00742    21 EILNSDpDIEVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKI---MRLRPTPVVmvsSLT----ERGAEit 93
                           90
                   ....*....|....*
gi 2256105915  966 -RAYQSGMNDIIAKP 979
Cdd:PRK00742    94 lRALELGAVDFVTKP 108
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
878-997 9.30e-06

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 49.64  E-value: 9.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRnTLNDrAIPIIAMTA 957
Cdd:PRK10365     8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK-ALNP-AIPVLIMTA 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKPIDVGIMFSTLARWITSPQ 997
Cdd:PRK10365    86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTH 125
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
728-812 1.04e-05

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: 46.04  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqSDSAFDVVITDWQMPGKDGVELIHAIQQsESLNPKIL 807
Cdd:cd17572      1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFL-----SDQPPDVVLLDLKLPDMSGMEILKWIQE-RSLPTSVI 74

                   ....*
gi 2256105915  808 MLTAY 812
Cdd:cd17572     75 VITAH 79
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
728-809 1.11e-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: 45.34  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSlNFNVRSANGVDSAIDALNHAAQSDSafDVVITDWQMPGKDGVELIHAIQQSESlNPKIL 807
Cdd:cd17565      1 FYIVDDDKNIIKILSDIIED-DDLGEVVGEADNGAQAYDEILFLQP--DIVLIDLLMPGMDGIQLVRKLKDTGS-NGKFI 76

                   ..
gi 2256105915  808 ML 809
Cdd:cd17565     77 MI 78
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
895-982 1.12e-05

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: 45.73  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  895 LESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIAMTAdvmERDRERA---YQSG 971
Cdd:cd19919     20 LAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPD--LPVIIMTA---HSDLDSAvsaYQGG 94
                           90
                   ....*....|.
gi 2256105915  972 MNDIIAKPIDV 982
Cdd:cd19919     95 AFEYLPKPFDI 105
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
728-814 1.48e-05

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: 45.35  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNAsarLIVEDILQSLNfnvRSANGVDSAIDALNHAAQSDS-AFDVVITDWQMPGKDGVELIHAIQQSESLNPkI 806
Cdd:cd19934      1 LLLVEDDA---LLAAQLKEQLS---DAGYVVDVAEDGEEALFQGEEePYDLVVLDLGLPGMDGLSVLRRWRSEGRATP-V 73

                   ....*...
gi 2256105915  807 LMLTAYDR 814
Cdd:cd19934     74 LILTARDS 81
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
879-979 1.50e-05

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: 44.85  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAMTAD 958
Cdd:cd17620      2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA---VPVIVLSAR 78
                           90       100
                   ....*....|....*....|.
gi 2256105915  959 VMERDRERAYQSGMNDIIAKP 979
Cdd:cd17620     79 DEESDKIAALDAGADDYLTKP 99
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
878-957 1.70e-05

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: 45.41  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTV---AQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIA 954
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIDWEELGFEVvgeAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPD--IKIII 78

                   ...
gi 2256105915  955 MTA 957
Cdd:cd17536     79 LSG 81
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
729-824 1.95e-05

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: 44.90  E-value: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  729 LIVDDNASARLIVEDILQSLNFNVRSANGVDSAIdalnHAAQSDsAFDVVITDWQMPGKDGVELIHAIQQSESLNPkILM 808
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGL----EYALSG-IYDLIILDIMLPGMDGLEVLKSLREEGIETP-VLL 74
                           90
                   ....*....|....*.
gi 2256105915  809 LTAydrqllADSVQER 824
Cdd:cd17625     75 LTA------LDAVEDR 84
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
728-816 2.05e-05

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 45.06  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVeDILQSLNFNVRSANGVDSAIDALNHAAQsdsafDVVITDWQMPGKDGVELIHAIQQSESLnpKIL 807
Cdd:cd17622      4 LLVEDDPKLARLIA-DFLESHGFNVVVEHRGDRALEVIAREKP-----DAVLLDIMLPGIDGLTLCRDLRPKYQG--PIL 75

                   ....*....
gi 2256105915  808 MLTAYDRQL 816
Cdd:cd17622     76 LLTALDSDI 84
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
879-979 2.22e-05

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: 45.04  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEIN-QELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIAMTA 957
Cdd:cd17615      2 VLVVDDEPNiTELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPD--VPVLFLTA 79
                           90       100
                   ....*....|....*....|..
gi 2256105915  958 DVMERDRERAYQSGMNDIIAKP 979
Cdd:cd17615     80 KDSVEDRIAGLTAGGDDYVTKP 101
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
728-806 2.32e-05

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: 44.88  E-value: 2.32e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHaaqsdSAFDVVITDWQMPGKDGVELIHAIQQSESLNPKI 806
Cdd:cd17555      3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRS-----EQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVI 76
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
560-704 2.37e-05

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: 45.32  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  560 LDNISNLVGLKASEQGLELLIHTSKDVptALYGDPLRLGQILTNLANNAVKFTEQgevKITITADNLENDdvtLRFAVSD 639
Cdd:cd16954      3 LDSLCSALNKVYQRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCLE---FVEVTARQTDGG---LHLIVDD 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  640 TGIGMTPEQTQKLFNKFTQADSSTTrkygGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16954     75 DGPGVPESQRSKIFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
878-956 2.95e-05

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: 44.03  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQ-MTFDGILMDCQMPVLDGYSATEIIRNTlnDRAIPIIAMT 956
Cdd:cd18160      2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQgKDIDIVVTDIVMPEMDGIELAREARKI--DPDVKILFIS 79
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
879-957 2.97e-05

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 46.73  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLES-QNIQ-VTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMT 956
Cdd:COG3279      5 LIVDDEPLARERLERLLEKyPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRE--LDPPPPIIFTT 82

                   .
gi 2256105915  957 A 957
Cdd:COG3279     83 A 83
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
726-812 3.06e-05

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 48.10  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAaqSDSAFDVVITDWQMPGKDGVELIHAIQqseSLNPK 805
Cdd:PRK10365     6 IDILVVDDDISHCTILQALLRGWGYNVALAN---SGRQALEQV--REQVFDLVLCDVRMAEMDGIATLKEIK---ALNPA 77

                   ....*....
gi 2256105915  806 I--LMLTAY 812
Cdd:PRK10365    78 IpvLIMTAY 86
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
728-811 3.25e-05

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 46.64  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHAAQsdsafDVVITDWQMPGKDGVELI-HAIQQSESLNPKI 806
Cdd:PRK10161     5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWP-----DLILLDWMLPGGSGIQFIkHLKRESMTRDIPV 79

                   ....*
gi 2256105915  807 LMLTA 811
Cdd:PRK10161    80 VMLTA 84
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
876-981 3.51e-05

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: 44.30  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNdraIPIIAM 955
Cdd:cd17619      1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE---VGIILV 77
                           90       100
                   ....*....|....*....|....*.
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPID 981
Cdd:cd17619     78 TGRDDEVDRIVGLEIGADDYVTKPFN 103
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
729-811 4.47e-05

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: 43.80  E-value: 4.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  729 LIVDDNasarlivEDILQSLNFNVRSA-NGVDSAID---ALNHAAQSDsaFDVVITDWQMPGKDGVELIHAI-QQSESLN 803
Cdd:cd19937      1 LVVDDE-------EDIVELLKYNLEKEgYEVVTAYDgeeALKRAKDEK--PDLIILDLMLPGIDGLEVCRILrSDPKTSS 71

                   ....*...
gi 2256105915  804 PKILMLTA 811
Cdd:cd19937     72 IPIIMLTA 79
PRK15115 PRK15115
response regulator GlrR; Provisional
727-845 5.56e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 47.14  E-value: 5.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  727 NILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHaaqsdSAFDVVITDWQMPGKDGVELIHAIQQSESLNPkI 806
Cdd:PRK15115     7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNR-----EKVDLVISDLRMDEMDGMQLFAEIQKVQPGMP-V 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2256105915  807 LMLTAYDRQLLADSVQERGliVPSILDKPVTASHLFDAI 845
Cdd:PRK15115    81 IILTAHGSIPDAVAATQQG--VFSFLTKPVDRDALYKAI 117
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-696 5.97e-05

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: 43.54  E-value: 5.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFT--EQGEVKI-TITADNL----ENDDVTLRFAVSDTGIGMTPEQTQKLFNKFTqadsstTRKYGG 669
Cdd:cd16918      1 LIQVFLNLVRNAAQALagSGGEIILrTRTQRQVtlghPRHRLALRVSVIDNGPGIPPDLQDTIFYPMV------SGRENG 74
                           90       100
                   ....*....|....*....|....*..
gi 2256105915  670 TGLGLAISKELCLLMGGDIEVRSQFGE 696
Cdd:cd16918     75 TGLGLAIAQNIVSQHGGVIECDSQPGH 101
PRK15115 PRK15115
response regulator GlrR; Provisional
876-981 6.49e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 46.75  E-value: 6.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSA-TEIIRntlNDRAIPIIA 954
Cdd:PRK15115     6 AHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLfAEIQK---VQPGMPVII 82
                           90       100
                   ....*....|....*....|....*..
gi 2256105915  955 MTADVMERDRERAYQSGMNDIIAKPID 981
Cdd:PRK15115    83 LTAHGSIPDAVAATQQGVFSFLTKPVD 109
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
880-980 6.64e-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: 43.03  E-value: 6.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  880 LVEDNEINQELAVELLESQNIQ--VTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGysaTEIIRNTLNDRAIPIIAMTA 957
Cdd:cd17565      3 IVDDDKNIIKILSDIIEDDDLGevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDG---IQLVRKLKDTGSNGKFIMIS 79
                           90       100
                   ....*....|....*....|....
gi 2256105915  958 DVMERD-RERAYQSGMNDIIAKPI 980
Cdd:cd17565     80 QVSDKEmIGKAYQAGIEFFINKPI 103
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
877-941 7.82e-05

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: 43.73  E-value: 7.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2256105915  877 HLLLVEDNEINQELAVELLESQ-NIQV-TVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEII 941
Cdd:COG2197      3 RVLIVDDHPLVREGLRALLEAEpDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK10693 PRK10693
two-component system response regulator RssB;
903-980 8.54e-05

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 46.14  E-value: 8.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2256105915  903 TVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIAMTADVMERDRERAYQSGMNDIIAKPI 980
Cdd:PRK10693     1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQ--TPVLVISATENMADIAKALRLGVQDVLLKPV 76
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
728-824 8.79e-05

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: 43.11  E-value: 8.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIdalnhAAQSDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPkIL 807
Cdd:cd17615      2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEAL-----AAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVP-VL 75
                           90
                   ....*....|....*..
gi 2256105915  808 MLTAydrqllADSVQER 824
Cdd:cd17615     76 FLTA------KDSVEDR 86
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
728-811 9.77e-05

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: 42.84  E-value: 9.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnHAAQSDsafdVVITDWQMPGKDGVELIHAIQQsESLNPkIL 807
Cdd:cd17626      3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAF-REVRPD----LVLLDLMLPGIDGIEVCRQIRA-ESGVP-IV 75

                   ....
gi 2256105915  808 MLTA 811
Cdd:cd17626     76 MLTA 79
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
484-686 1.18e-04

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 45.73  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  484 FLANMSHEIRTPMNAIigmsylALKTDLTkAQRNYIQKVKLSA--DTLLGLINDILDFSKIE----AGKLD----IEHVD 553
Cdd:PRK10755   140 FTADVAHELRTPLAGI------RLHLELL-EKQHHIDVAPLIArlDQMMHTVEQLLQLARAGqsfsSGHYQtvklLEDVI 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  554 FRLENVLDNIsnlvgLKASEQGLELlihtsKDVPTALY--GDPLRLGQILTNLANNAVKFTEQGEvKITITadnLENDDV 631
Cdd:PRK10755   213 LPSQDELSEM-----LEQRQQTLLL-----PESAADITvqGDATLLRLLLRNLVENAHRYSPEGS-TITIK---LSQEDG 278
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2256105915  632 TLRFAVSDTGIGMTPEQTQKLFNKFTQADSsttrKYGGTGLGLAISKELCLLMGG 686
Cdd:PRK10755   279 GAVLAVEDEGPGIDESKCGELSKAFVRMDS----RYGGIGLGLSIVSRITQLHHG 329
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
597-704 1.29e-04

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 41.77  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  597 LGQILTNLANNAVKFTEQGEVKITITADNlenDDVTLRfaVSDTGIGmtpeqtqklfnkFTQADSSttrkyGGTGLGLAI 676
Cdd:cd16917      1 LYRIVQEALTNALKHAGASRVRVTLSYTA---DELTLT--VVDDGVG------------FDGPAPP-----GGGGFGLLG 58
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  677 SKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:cd16917     59 MRERAELLGGTLTIGSRPGGGTRVTARL 86
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
1040-1099 1.31e-04

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


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 41.85  E-value: 1.31e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2256105915  1040 QLYRRLLQRFYEHY-SDLSQVREQLANAASSDLKRYIHSLKGVSGNIGANELFELCSALES 1099
Cdd:smart00073    4 ELFREELAEFLQSLeEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLEN 64
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
728-812 1.42e-04

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: 42.54  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNV-RSANGVdSAIDALNHAAQsdsafDVVITDWQMPGKDGVELIHAIQQSESlNPKI 806
Cdd:cd17553      3 ILIVDDQYGIRILLNEVFNKEGYQTfQAANGL-QALDIVTKERP-----DLVLLDMKIPGMDGIEILKRMKVIDE-NIRV 75

                   ....*.
gi 2256105915  807 LMLTAY 812
Cdd:cd17553     76 IIMTAY 81
PLN03029 PLN03029
type-a response regulator protein; Provisional
877-980 1.69e-04

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 44.25  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDL--------------------YKQMTFDGILMDCQMPVLDGYS 936
Cdd:PLN03029    10 HVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFlglheddrsnpdtpsvspnsHQEVEVNLIITDYCMPGMTGYD 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2256105915  937 ATEIIRNTLNDRAIPIIAMTADVMERDRERAYQSGMNDIIAKPI 980
Cdd:PLN03029    90 LLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPV 133
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
878-957 1.71e-04

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 42.00  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTF--DGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAM 955
Cdd:cd17582      1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80

                   ..
gi 2256105915  956 TA 957
Cdd:cd17582     81 SS 82
PRK15479 PRK15479
transcriptional regulator TctD;
878-982 2.00e-04

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 44.33  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNeinQELAVEL---LESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIA 954
Cdd:PRK15479     3 LLLAEDN---RELAHWLekaLVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRK--RGQTLPVLL 77
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  955 MTADVMERDRERAYQSGMNDIIAKPIDV 982
Cdd:PRK15479    78 LTARSAVADRVKGLNVGADDYLPKPFEL 105
orf27 CHL00148
Ycf27; Reviewed
728-813 2.78e-04

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 43.94  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAQSDSafDVVITDWQMPGKDGVELIHAIqQSESLNPkIL 807
Cdd:CHL00148     9 ILVVDDEAYIRKILETRLSIIGYEVITAS---DGEEALKLFRKEQP--DLVILDVMMPKLDGYGVCQEI-RKESDVP-II 81

                   ....*.
gi 2256105915  808 MLTAYD 813
Cdd:CHL00148    82 MLTALG 87
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
879-980 2.82e-04

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 41.97  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  879 LLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDL-----------YKQMTFDGILMDCQMPVLDGYSATEIIRNTLND 947
Cdd:cd17581      2 LAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFlgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVKESSAL 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2256105915  948 RAIPIIAMTAD-VMERDReRAYQSGMNDIIAKPI 980
Cdd:cd17581     82 KEIPVVIMSSEnIPTRIS-RCLEEGAEDFLLKPV 114
PRK13856 PRK13856
two-component response regulator VirG; Provisional
877-979 3.08e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 43.65  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYsatEIIRNTLNDRAIPIIAMT 956
Cdd:PRK13856     3 HVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGL---EIVRSLATKSDVPIIIIS 79
                           90       100
                   ....*....|....*....|....
gi 2256105915  957 ADVMER-DRERAYQSGMNDIIAKP 979
Cdd:PRK13856    80 GDRLEEaDKVVALELGATDFIAKP 103
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
728-825 3.96e-04

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: 40.95  E-value: 3.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAQSDSafDVVITDWQMPGKDGVELIHAIQQSESlNPKIL 807
Cdd:cd19928      1 ILVADDDRAIRTVLTQALGRAGYEVRTTG---NAATLWRWVEEGEG--DLVITDVVMPDENGLDLIPRIKKARP-DLPII 74
                           90
                   ....*....|....*...
gi 2256105915  808 MLTAYDRQLLADSVQERG 825
Cdd:cd19928     75 VMSAQNTLMTAVKAAERG 92
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
548-710 4.16e-04

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 44.51  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  548 DIEHVDFR--LENVLDNISNLvglkaseqglelliHTSKDVPTALYGDPLRLGQ--------ILTNLANNAVK--FTEQG 615
Cdd:COG3920    355 DWEGVDLRdyLRELLEPLRDS--------------YGGRGIRIELDGPDVELPAdaavplglILNELVTNALKhaFLSGE 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  616 EVKITITadnLENDDVTLRFAVSDTGIGMTPEQTQKlfnkftqadssttrkyGGTGLGLAISKELCLLMGGDIEVRSqfG 695
Cdd:COG3920    421 GGRIRVS---WRREDGRLRLTVSDNGVGLPEDVDPP----------------ARKGLGLRLIRALVRQLGGTLELDR--P 479
                          170
                   ....*....|....*
gi 2256105915  696 EGSTFEFTINMKRSQ 710
Cdd:COG3920    480 EGTRVRITFPLAELA 494
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
585-699 5.43e-04

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 41.94  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  585 DVPTALYGDPLRLGQILTNLANNAVKFT-EQGE--------VKITItadNLENDDVTLRFavSDTGIGMTPEQTQKLFN- 654
Cdd:cd16929     32 DPSIRFPYVPSHLYYILFELLKNAMRATvESHGddsddlppIKVTV---AKGDEDLTIKI--SDRGGGIPREDLARLFSy 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2256105915  655 KFTQADSSTTRKY------------GGTGLGLAISKELCLLMGGDIEVRSQFGEGST 699
Cdd:cd16929    107 MYSTAPQPSLDDFsdlisgtqpsplAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTD 163
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
878-981 6.34e-04

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: 40.47  E-value: 6.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMTA 957
Cdd:cd17616      1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                           90       100
                   ....*....|....*....|....
gi 2256105915  958 DVmeRDRERAYQSGMNDIIAKPID 981
Cdd:cd17616     81 DI--EDKVKGLGFGADDYMTKPFH 102
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
774-845 7.56e-04

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: 40.33  E-value: 7.56e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2256105915  774 AFDVVITDWQMPGKDGVELIHAIQQsESLNPKILMLT-----AYDRQLLADSVqeRGLIVpsildKPVTASHLFDAI 845
Cdd:cd19930     44 SPDVAILDIEMPGRTGLEVAAELRE-ELPDTKVLIVTtfgrpGYFRRALAAGV--DGYVL-----KDRPIEELADAI 112
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
728-811 7.97e-04

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: 40.19  E-value: 7.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALNHAaqsdsAFDVVITDWQMPGKDGVELIHAIQQSESLN--Pk 805
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAE-----PPDLILLDVMMPGMDGFEVCRRLKADPATRhiP- 74

                   ....*.
gi 2256105915  806 ILMLTA 811
Cdd:cd19920     75 VIFLTA 80
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
607-708 8.28e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 43.47  E-value: 8.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  607 NAVKF---TEQGEVKITITADNLENDdvtLRFAVSDTGIGMTPEQTQKLFNKFtqadsstTRKYGGTGLGLAISKELCLL 683
Cdd:COG2972    347 NAIEHgiePKEGGGTIRISIRKEGDR---LVITVEDNGVGMPEEKLEKLLEEL-------SSKGEGRGIGLRNVRERLKL 416
                           90       100
                   ....*....|....*....|....*...
gi 2256105915  684 MGGD---IEVRSQFGEGSTFEFTINMKR 708
Cdd:COG2972    417 YYGEeygLEIESEPGEGTTVTIRIPLEE 444
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
728-789 8.70e-04

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 40.32  E-value: 8.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNF-NVRSAngvDSAIDALNHAAQSDsaFDVVITDWQM-PGKDG 789
Cdd:cd17589      1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTA---SSGEEALRMCENKT--YDIVLCDYNLgKGKNG 59
PRK10610 PRK10610
chemotaxis protein CheY;
878-979 1.12e-03

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 40.34  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQ-VTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDRAIPIIAMT 956
Cdd:PRK10610     8 FLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVT 87
                           90       100
                   ....*....|....*....|...
gi 2256105915  957 ADVMERDRERAYQSGMNDIIAKP 979
Cdd:PRK10610    88 AEAKKENIIAAAQAGASGYVVKP 110
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
878-985 1.23e-03

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 39.72  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDN-EINQELAVELLESqNIQVTVAQN---GQVAIDLykqMTFDGILMDCQMPvlDGYSATEIIRNTLNDRAIPII 953
Cdd:cd17573      1 ILLIEDDsTLGKEISKGLNEK-GYQADVAESlkdGEYYIDI---RNYDLVLVSDKLP--DGNGLSIVSRIKEKHPSIVVI 74
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2256105915  954 AMTADVMERDRERAYQSGMNDIIAKPIDVGIM 985
Cdd:cd17573     75 VLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
877-982 1.51e-03

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: 41.06  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  877 HLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCqmpVLDGYSATEIIRnTLNDR--AIPIIA 954
Cdd:COG4567      6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDL---RLGDGSGLDLIE-ALRERdpDARIVV 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  955 MT-----ADVMErdrerAYQSGMNDIIAKPIDV 982
Cdd:COG4567     82 LTgyasiATAVE-----AIKLGADDYLAKPADA 109
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
728-816 1.71e-03

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 41.33  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANGVDSAIDALnhaaqsDSAFDVVITDWQMPGKDGVELIHAIQQSESLnpKIL 807
Cdd:PRK10955     4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL------DDSIDLLLLDVMMPKKNGIDTLKELRQTHQT--PVI 75

                   ....*....
gi 2256105915  808 MLTAYDRQL 816
Cdd:PRK10955    76 MLTARGSEL 84
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
728-859 1.82e-03

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: 39.66  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSlNFNVRSANGVDSAIDALNhaaqsDSAFDVVITDWQMPGKDGVELIHAIQQSESlNPKIL 807
Cdd:cd17596      3 ILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILE-----EEWVQVILCDQRMPGTTGVEFLKEVRERWP-EVVRI 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2256105915  808 MLTAY-DRQLLADSVQERGliVPSILDKPVTASHLFDAI---VGLYDI--ENHRSSRD 859
Cdd:cd17596     76 IISGYtDSEDIIAGINEAG--IYQYLTKPWHPDQLLLTVrnaARLFELqrENERLSLE 131
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
728-812 2.03e-03

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 42.14  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSANgvdSAIDALNHAAqsDSAFDVVITDWQMPGKDGVELIHAIQQSESLNPKIL 807
Cdd:PRK11361     7 ILIVDDEDNVRRMLSTAFALQGFETHCAN---NGRTALHLFA--DIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVIL 81

                   ....*
gi 2256105915  808 MlTAY 812
Cdd:PRK11361    82 M-TAY 85
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
878-982 2.66e-03

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: 39.02  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNE-INQELAvELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNTLNDraIPIIAM- 955
Cdd:cd17550      1 ILIVDDEEdIRESLS-GILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPD--LPVIMIs 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2256105915  956 ------TAdvMERDRERAYqsgmnDIIAKPIDV 982
Cdd:cd17550     78 ghgtieTA--VKATKLGAY-----DFIEKPLSL 103
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
728-815 3.42e-03

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: 38.46  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSA-NGVDsaidALNHAAQSDSAfdVVITDWQMPGKDGVELIHAIQQSESLN--P 804
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQGYKVQVArNGRE----ALAMLAEHRPT--LVISDIVMPEMDGYELCRKIKSDPDLKdiP 74
                           90
                   ....*....|.
gi 2256105915  805 KILMLTAYDRQ 815
Cdd:cd17598     75 VILLTTLSDPR 85
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
878-942 3.51e-03

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: 38.41  E-value: 3.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQ--NGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIR 942
Cdd:cd19930      1 VLIAEDQEMVRGALAALLELEDDLEVVAQasNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELR 67
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
728-836 3.52e-03

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: 38.58  E-value: 3.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVrsANGVDSAIDAlnhAAQSDSAFDVVITDWQMPGKDGVELIHAIQQSESLnpKIL 807
Cdd:cd17594      2 VLVVDDDAAMRHLLILYLRERGFDV--TAAADGAEEA---RLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDV--PII 74
                           90       100
                   ....*....|....*....|....*....
gi 2256105915  808 MLTAyDRQLLADSVQERGLIVPSILDKPV 836
Cdd:cd17594     75 IISG-DRRDEIDRVVGLELGADDYLAKPF 102
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
876-999 4.60e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 40.17  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  876 AHLLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGysaTEIIRNTLNDRAIPIIAM 955
Cdd:PRK10529     2 TNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDG---IEFIRDLRQWSAIPVIVL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2256105915  956 TADVMERDRERAYQSGMNDIIAKPIDVGIMFS----TLARWITSPQRE 999
Cdd:PRK10529    79 SARSEESDKIAALDAGADDYLSKPFGIGELQArlrvALRRHSATPAPD 126
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
878-957 5.21e-03

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 38.30  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  878 LLLVEDNEINQELAVELLESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGysaTEIIRNTLN-DRAIPIIAMT 956
Cdd:cd17553      3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDG---IEILKRMKViDENIRVIIMT 79

                   .
gi 2256105915  957 A 957
Cdd:cd17553     80 A 80
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
895-994 7.10e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 40.24  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  895 LESQNIQVTVAQNGQVAIDLYKQMTFDGILMDCQMPVLDGYSATEIIRNtlNDRAIPIIAMTADVMERDRERAYQSGMND 974
Cdd:PRK10923    23 LAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIMTAHSDLDAAVSAYQQGAFD 100
                           90       100
                   ....*....|....*....|
gi 2256105915  975 IIAKPIDVGIMFSTLARWIT 994
Cdd:PRK10923   101 YLPKPFDIDEAVALVERAIS 120
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
726-812 7.17e-03

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: 37.59  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  726 LNILIVDDNASARLIVEDILQSL-NFNV--RSANGVDsaidALNHAAQSDSafDVVITDWQMPGKDGVELIHAIQQSESL 802
Cdd:cd17561      2 IKVLIADDNREFVQLLEEYLNSQpDMEVvgVAHNGQE----ALELIEEKEP--DVLLLDIIMPHLDGIGVLEKLRRMRLE 75
                           90
                   ....*....|.
gi 2256105915  803 N-PKILMLTAY 812
Cdd:cd17561     76 KrPKIIMLTAF 86
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
618-736 7.73e-03

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 38.08  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  618 KITITADNleNDDVTLRFAVSDTGIGMTPEqtqKLFNKFTQADSSTTRKYG-------GTGLGLAIskelcLLMGGDIEV 690
Cdd:pfam13589   19 NIKIEVNK--NRGGGTEIVIEDDGHGMSPE---ELINALRLATSAKEAKRGstdlgryGIGLKLAS-----LSLGAKLTV 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2256105915  691 RSqFGEGSTFEFTINMKRSQVLETKPIVVPTSLNHLNILIVDDNAS 736
Cdd:pfam13589   89 TS-KKEGKSSTLTLDRDKISNENDWLLPLLTPAPIENFDELDKDAH 133
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
728-814 9.00e-03

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: 36.76  E-value: 9.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  728 ILIVDDNASARLIVEDILQSLNFNVRSAngvDSAIDALNHAAQSDsaFDVVITDWQMPGKDGVELIHAIQqsESLNPKIL 807
Cdd:cd17620      1 ILVIEDEPQIRRFLRTALEAHGYRVFEA---ETGQEGLLEAATRK--PDLIILDLGLPDMDGLEVIRRLR--EWSAVPVI 73

                   ....*..
gi 2256105915  808 MLTAYDR 814
Cdd:cd17620     74 VLSARDE 80
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
555-704 9.33e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 39.22  E-value: 9.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  555 RLENVLDNISNLVGLKASEQGLELLIHTSKDVPTALYgdplrlgQILTNLANNAVKFTEQGEVKITITADNlenDDVTLR 634
Cdd:COG4585    128 ALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALY-------RIVQEALTNALKHAGATRVTVTLEVDD---GELTLT 197
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256105915  635 faVSDTGIGMTPEQTqklfnkftqadssttrkyGGTGLGLAISKELCLLMGGDIEVRSQFGEGSTFEFTI 704
Cdd:COG4585    198 --VRDDGVGFDPEAA------------------PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247
 
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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