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Conserved domains on  [gi|636783241|ref|WP_024319460|]
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response regulator [Rhizobium ruizarguesonis]

Protein Classification

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
577-1106 5.16e-112

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: 370.72  E-value: 5.16e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  577 RAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKLRKA 656
Cdd:PRK11107  285 RAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENI 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  657 AFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVFVDVGFETAAGGEIM 736
Cdd:PRK11107  365 PFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQ 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  737 ASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPfavaaar 816
Cdd:PRK11107  445 LEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLP------- 517
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  817 LEPKPLPIN-------VQGARILVVDDNEVNRRILTEQLSLWGFDgVaaegggTGLAILEAAADLgvTVDAVVLDYHMPD 889
Cdd:PRK11107  518 LDLNPNPIIdglptdcLAGKRLLYVEPNSAAAQATLDILSETPLE-V------TYSPTLSQLPEA--HYDILLLGLPVTF 588
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  890 MNG-ADVARRLRADPRFVELPIIFLTSMDISGTEKeFAALNGHAHLMKParanvlrntvvevVRASRVKQASEAEiarlQ 968
Cdd:PRK11107  589 REPlTMLHERLAKAKSMTDFLILALPCHEQVLAEQ-LKQDGADACLSKP-------------LSHTRLLPALLEP----C 650
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  969 TEAAVPAPALVPQKRAAefVDVLVAEDNEVNqivftQILQGTGLSFLV-----VDNGEEAVAAWERYTPRIIMMDVSMPV 1043
Cdd:PRK11107  651 HHKQPPLLPPTDESRLP--LTVMAVDDNPAN-----LKLIGALLEEQVehvvlCDSGHQAVEQAKQRPFDLILMDIQMPG 723
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636783241 1044 MNGHQATQTIRereKGQGHR-VPIIGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQW 1106
Cdd:PRK11107  724 MDGIRACELIR---QLPHNQnTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
KinE super family cl47428
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
312-809 7.56e-65

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


The actual alignment was detected with superfamily member COG5809:

Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 227.94  E-value: 7.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  312 ELLHRDIENILRSL----PVGVLILDNDHRILYVNDEFYGIWELPLDDpFDGRPFIDVIRRNYElgrydgtqtpEEIYDF 387
Cdd:COG5809     7 ELQLRKSEQRFRSLfenaPDAILILDLEGKILKVNPAAERIFGYTEDE-LLGTNILDFLHPDDE----------KELREI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  388 RKHLFETEEPEPIELGWA--GGKSVIFDSRRI----SNDRILLTYA---DITAVREREKEIHETRaalERLgemmRDATH 458
Cdd:COG5809    76 LKLLKEGESRDELEFELRhkNGKRLEFSSKLSpifdQNGDIEGMLAisrDITERKRMEEALRESE---EKF----RLIFN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  459 AMPQGLAIV-QDGIIRMSNEALSDILQIPATylergegwigmfEYCAARGD--FHDAAAETLQGWRDNIAARLPISTA-F 534
Cdd:COG5809   149 HSPDGIIVTdLDGRIIYANPAACKLLGISIE------------ELIGKSILelIHSDDQENVAAFISQLLKDGGIAQGeV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  535 HV----GGERWVNMDAT---VSRGQHW-VALFTDVTELKSREEELRqllsRAEAADRAkSEFLANMSHEIRTPMNGVLGM 606
Cdd:COG5809   217 RFwtkdGRWRLLEASGApikKNGEVDGiVIIFRDITERKKLEELLR----KSEKLSVV-GELAAGIAHEIRNPLTSLKGF 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  607 AELLAKTNlDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKLrkaaFDITEAVEDVATLLSSHAAEKNIELLVRA 686
Cdd:COG5809   292 IQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYEP----KDLNTLIEEVIPLLQPQALLKNVQIELEL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  687 APDLPAaVIGDAGRFRQIVTNLVGNAVKFTER-GHVFVDVGFEtaAGGEIMasIRIEDTGIGIPPEKLESVFDKFSqvda 765
Cdd:COG5809   367 EDDIPD-ILGDENQLKQVFINLLKNAIEAMPEgGNITIETKAE--DDDKVV--ISVTDEGCGIPEERLKKLGEPFY---- 437
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 636783241  766 ssTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:COG5809   438 --TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLP 479
PAS COG2202
PAS domain [Signal transduction mechanisms];
182-439 6.91e-24

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 102.41  E-value: 6.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  182 ELDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALEGGTSKEIESLL 261
Cdd:COG2202     9 SERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  262 PSKDGHIYSVLSRVNRVVTADGRP-YVVGSFSDISPLKEREKALIEAQKHkellhrdIENILRSLPVGVLILDNDHRILY 340
Cdd:COG2202    89 RRKDGSLFWVELSISPVRDEDGEItGFVGIARDITERKRAEEALRESEER-------LRLLVENAPDGIFVLDLDGRILY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  341 VNDEFYGIWELPLDDpFDGRPFIDVIrrnYELGRYDGTQTPEEIYDFRKHLFETEEPEPIELGWAGG--KSVIFDSRRIS 418
Cdd:COG2202   162 VNPAAEELLGYSPEE-LLGKSLLDLL---HPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWveASAVPLRDGGE 237
                         250       260
                  ....*....|....*....|.
gi 636783241  419 NDRILLTYADITAVREREKEI 439
Cdd:COG2202   238 VIGVLGIVRDITERKRAEEAL 258
PAS super family cl43642
PAS domain [Signal transduction mechanisms];
6-304 1.61e-08

PAS domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2202:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.96  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241    6 ELLELACRRIADLDTPAYVKNSELRYIAVNEAYARFLGREISDFIGRRSRELLDRPEEEDREDKERRAL----VFGTEEN 81
Cdd:COG2202     8 ESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALagggVWRGELR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   82 AICFDaaglSHERIQIESFSPSADRA----YVLGIFE-VREppRRavddsdvaadfaRVREALEQhdhpigifagdgrpl 156
Cdd:COG2202    88 NRRKD----GSLFWVELSISPVRDEDgeitGFVGIARdITE--RK------------RAEEALRE--------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  157 vvnaayrngakpaaiSEtawhesvnelDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPD 236
Cdd:COG2202   135 ---------------SE----------ERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPE 189
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636783241  237 GGEAIYQENLLALEGGTSK-EIESLLPSKDGHIYSVLSRVNRVVTADGRPYVVGSFSDISPLKEREKAL 304
Cdd:COG2202   190 DRERLLELLRRLLEGGRESyELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
577-1106 5.16e-112

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 370.72  E-value: 5.16e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  577 RAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKLRKA 656
Cdd:PRK11107  285 RAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENI 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  657 AFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVFVDVGFETAAGGEIM 736
Cdd:PRK11107  365 PFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQ 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  737 ASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPfavaaar 816
Cdd:PRK11107  445 LEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLP------- 517
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  817 LEPKPLPIN-------VQGARILVVDDNEVNRRILTEQLSLWGFDgVaaegggTGLAILEAAADLgvTVDAVVLDYHMPD 889
Cdd:PRK11107  518 LDLNPNPIIdglptdcLAGKRLLYVEPNSAAAQATLDILSETPLE-V------TYSPTLSQLPEA--HYDILLLGLPVTF 588
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  890 MNG-ADVARRLRADPRFVELPIIFLTSMDISGTEKeFAALNGHAHLMKParanvlrntvvevVRASRVKQASEAEiarlQ 968
Cdd:PRK11107  589 REPlTMLHERLAKAKSMTDFLILALPCHEQVLAEQ-LKQDGADACLSKP-------------LSHTRLLPALLEP----C 650
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  969 TEAAVPAPALVPQKRAAefVDVLVAEDNEVNqivftQILQGTGLSFLV-----VDNGEEAVAAWERYTPRIIMMDVSMPV 1043
Cdd:PRK11107  651 HHKQPPLLPPTDESRLP--LTVMAVDDNPAN-----LKLIGALLEEQVehvvlCDSGHQAVEQAKQRPFDLILMDIQMPG 723
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636783241 1044 MNGHQATQTIRereKGQGHR-VPIIGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQW 1106
Cdd:PRK11107  724 MDGIRACELIR---QLPHNQnTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
562-901 3.28e-88

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: 306.32  E-value: 3.28e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   562 TELKSREEELRQLLSRAEA--ADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIIND 639
Cdd:TIGR02956  439 TNERLNAEVKNHAKARAEAeeANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILND 518
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   640 ILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERG 719
Cdd:TIGR02956  519 ILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRG 598
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   720 HVFVDVGFEtaagGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDasSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWG 799
Cdd:TIGR02956  599 SVVLRVSLN----DDSSLLFEVEDTGCGIAEEEQATLFDAFTQAD--GRRRSGGTGLGLAISQRLVEAMDGELGVESELG 672
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   800 KGSVFTVNLPFAVAAARLEPKPL-PINVQGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtV 878
Cdd:TIGR02956  673 VGSCFWFTLPLTRGKPAEDSATLtVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHA-----F 747
                          330       340
                   ....*....|....*....|...
gi 636783241   879 DAVVLDYHMPDMNGADVARRLRA 901
Cdd:TIGR02956  748 DLALLDINLPDGDGVTLLQQLRA 770
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
478-811 4.26e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 257.14  E-value: 4.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  478 ALSDILQIPATYLERGEGWIGMFEYCAARGDFHDAAAETLQGWRDNIAARLPISTAFHVGGERWVNMDATVSRGQHWVAL 557
Cdd:COG0642     3 LLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  558 FTDVTELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTnLDTRQKTFVDIIVKSGNALLTII 637
Cdd:COG0642    83 LLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  638 NDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPaAVIGDAGRFRQIVTNLVGNAVKFTE 717
Cdd:COG0642   162 NDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  718 RGHVfVDVGFETAAGgeiMASIRIEDTGIGIPPEKLESVFDKFSQVDASstRRHEGTGLGLAITAGLVDLFGGYLNVDSE 797
Cdd:COG0642   241 EGGT-VTVSVRREGD---RVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESE 314
                         330
                  ....*....|....
gi 636783241  798 WGKGSVFTVNLPFA 811
Cdd:COG0642   315 PGKGTTFTVTLPLA 328
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
312-809 7.56e-65

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: 227.94  E-value: 7.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  312 ELLHRDIENILRSL----PVGVLILDNDHRILYVNDEFYGIWELPLDDpFDGRPFIDVIRRNYElgrydgtqtpEEIYDF 387
Cdd:COG5809     7 ELQLRKSEQRFRSLfenaPDAILILDLEGKILKVNPAAERIFGYTEDE-LLGTNILDFLHPDDE----------KELREI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  388 RKHLFETEEPEPIELGWA--GGKSVIFDSRRI----SNDRILLTYA---DITAVREREKEIHETRaalERLgemmRDATH 458
Cdd:COG5809    76 LKLLKEGESRDELEFELRhkNGKRLEFSSKLSpifdQNGDIEGMLAisrDITERKRMEEALRESE---EKF----RLIFN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  459 AMPQGLAIV-QDGIIRMSNEALSDILQIPATylergegwigmfEYCAARGD--FHDAAAETLQGWRDNIAARLPISTA-F 534
Cdd:COG5809   149 HSPDGIIVTdLDGRIIYANPAACKLLGISIE------------ELIGKSILelIHSDDQENVAAFISQLLKDGGIAQGeV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  535 HV----GGERWVNMDAT---VSRGQHW-VALFTDVTELKSREEELRqllsRAEAADRAkSEFLANMSHEIRTPMNGVLGM 606
Cdd:COG5809   217 RFwtkdGRWRLLEASGApikKNGEVDGiVIIFRDITERKKLEELLR----KSEKLSVV-GELAAGIAHEIRNPLTSLKGF 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  607 AELLAKTNlDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKLrkaaFDITEAVEDVATLLSSHAAEKNIELLVRA 686
Cdd:COG5809   292 IQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYEP----KDLNTLIEEVIPLLQPQALLKNVQIELEL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  687 APDLPAaVIGDAGRFRQIVTNLVGNAVKFTER-GHVFVDVGFEtaAGGEIMasIRIEDTGIGIPPEKLESVFDKFSqvda 765
Cdd:COG5809   367 EDDIPD-ILGDENQLKQVFINLLKNAIEAMPEgGNITIETKAE--DDDKVV--ISVTDEGCGIPEERLKKLGEPFY---- 437
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 636783241  766 ssTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:COG5809   438 --TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLP 479
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
701-810 3.01e-48

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: 166.90  E-value: 3.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  701 FRQIVTNLVGNAVKFTERGHVFVDVGFETAAGGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAI 780
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 636783241  781 TAGLVDLFGGYLNVDSEWGKGSVFTVNLPF 810
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
696-811 6.04e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.45  E-value: 6.04e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241    696 GDAGRFRQIVTNLVGNAVKFT-ERGHVFVDVGFEtaaggEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASStRRHEGT 774
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERD-----GDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRS-RKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 636783241    775 GLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFA 811
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
569-823 7.39e-31

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 128.22  E-value: 7.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  569 EELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELL--AKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKI 646
Cdd:NF040691  255 DSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRF 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  647 DAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRaAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVFVdvg 726
Cdd:NF040691  335 DAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVD-APGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVV--- 410
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  727 feTAAGGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTV 806
Cdd:NF040691  411 --TVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRL 488
                         250
                  ....*....|....*..
gi 636783241  807 NLPfAVAAARLEPKPLP 823
Cdd:NF040691  489 TLP-RVAGDRLTTSPLP 504
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
696-811 1.18e-27

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: 108.22  E-value: 1.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   696 GDAGRFRQIVTNLVGNAVKFT-ERGHVFVDVgfetAAGGEImaSIRIEDTGIGIPPEKLESVFDKFSQVDassTRRHEGT 774
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTL----SEGGEL--TLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 636783241   775 GLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFA 811
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
526-809 3.30e-25

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 110.30  E-value: 3.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  526 ARLPISTAFHVGGERWVNMDATVSRG--QHWVALfTDVTELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMnGV 603
Cdd:NF012163  180 AAFLLARGLLAPVKRLVEATHRLAAGdyTTRVTP-TSNDELGKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPL-AV 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  604 LgMAELLAKTNlDTRQKT--FVDIIVKSGNALLTIINDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIE 681
Cdd:NF012163  258 L-RAELEAIQD-GIRKFTpeSLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  682 LLVraapDLPAA--VIGDAGRFRQIVTNLVGNAVKFTERG---HVfvdvgfeTAAGGEIMASIRIEDTGIGIPPEKLESV 756
Cdd:NF012163  336 LEV----SLPDSslVFGDRDRLMQLFNNLLENSLRYTDSGgslHI-------SASQRPKEVTLTVADSAPGVSDEQLARL 404
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 636783241  757 FDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:NF012163  405 FERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
PAS COG2202
PAS domain [Signal transduction mechanisms];
182-439 6.91e-24

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 102.41  E-value: 6.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  182 ELDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALEGGTSKEIESLL 261
Cdd:COG2202     9 SERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  262 PSKDGHIYSVLSRVNRVVTADGRP-YVVGSFSDISPLKEREKALIEAQKHkellhrdIENILRSLPVGVLILDNDHRILY 340
Cdd:COG2202    89 RRKDGSLFWVELSISPVRDEDGEItGFVGIARDITERKRAEEALRESEER-------LRLLVENAPDGIFVLDLDGRILY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  341 VNDEFYGIWELPLDDpFDGRPFIDVIrrnYELGRYDGTQTPEEIYDFRKHLFETEEPEPIELGWAGG--KSVIFDSRRIS 418
Cdd:COG2202   162 VNPAAEELLGYSPEE-LLGKSLLDLL---HPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWveASAVPLRDGGE 237
                         250       260
                  ....*....|....*....|.
gi 636783241  419 NDRILLTYADITAVREREKEI 439
Cdd:COG2202   238 VIGVLGIVRDITERKRAEEAL 258
PRK13560 PRK13560
hypothetical protein; Provisional
182-342 9.82e-12

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 69.32  E-value: 9.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  182 ELDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEmFGPDGGEAIYQE-NLLALEGGTSKEIESL 260
Cdd:PRK13560  202 ALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHD-FAPAQPADDYQEaDAAKFDADGSQIIEAE 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  261 LPSKDGHIYSVLSRVNRvVTADGRPY----VVGSFSDISPLKEREKALIEaqkhKELLHRdieNILRSLPVGVLILDNDH 336
Cdd:PRK13560  281 FQNKDGRTRPVDVIFNH-AEFDDKENhcagLVGAITDISGRRAAERELLE----KEDMLR---AIIEAAPIAAIGLDADG 352

                  ....*.
gi 636783241  337 RILYVN 342
Cdd:PRK13560  353 NICFVN 358
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
182-304 1.67e-11

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 62.69  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   182 ELDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAI--YQENLLALEGGTsKEIES 259
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVreRIERRLEGEPEP-VSEER 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 636783241   260 LLPSKDGHIYSVLSRVNRVVTADGRPYVVGSFSDISPLKEREKAL 304
Cdd:TIGR00229   80 RVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
185-294 4.61e-09

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 55.12  E-value: 4.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   185 LLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLG-MTEHEMFGPDGGE--AIYQENLLALEGGTSKEIesLL 261
Cdd:pfam00989    2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGkSLLDLIPEEDDAEvaELLRQALLQGEESRGFEV--SF 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 636783241   262 PSKDGHIYSVLSRVNRVVTADGRP-YVVGSFSDI 294
Cdd:pfam00989   80 RVPDGRPRHVEVRASPVRDAGGEIlGFLGVLRDI 113
PAS COG2202
PAS domain [Signal transduction mechanisms];
6-304 1.61e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.96  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241    6 ELLELACRRIADLDTPAYVKNSELRYIAVNEAYARFLGREISDFIGRRSRELLDRPEEEDREDKERRAL----VFGTEEN 81
Cdd:COG2202     8 ESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALagggVWRGELR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   82 AICFDaaglSHERIQIESFSPSADRA----YVLGIFE-VREppRRavddsdvaadfaRVREALEQhdhpigifagdgrpl 156
Cdd:COG2202    88 NRRKD----GSLFWVELSISPVRDEDgeitGFVGIARdITE--RK------------RAEEALRE--------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  157 vvnaayrngakpaaiSEtawhesvnelDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPD 236
Cdd:COG2202   135 ---------------SE----------ERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPE 189
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636783241  237 GGEAIYQENLLALEGGTSK-EIESLLPSKDGHIYSVLSRVNRVVTADGRPYVVGSFSDISPLKEREKAL 304
Cdd:COG2202   190 DRERLLELLRRLLEGGRESyELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
resp_reg_YycF NF040534
response regulator YycF;
1007-1120 1.39e-07

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 53.57  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1007 LQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqgHRVPIIGVTAHALESDRELCLDAGM 1086
Cdd:NF040534   20 LKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKK-----YDMPIIMLTAKDSEIDKVLGLELGA 94
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241 1087 DDYMSKPISPELLEEKIRQWLGTSEQQPERTTAP 1120
Cdd:NF040534   95 DDYVTKPFSTRELIARVKANLRRHQQQNTEEEEE 128
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
193-294 2.98e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 44.16  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  193 LPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALEGGTSKEIESLLPSKDGHIYSVL 272
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                          90       100
                  ....*....|....*....|...
gi 636783241  273 SRVNRVVTADGRP-YVVGSFSDI 294
Cdd:cd00130    81 VSLTPIRDEGGEViGLLGVVRDI 103
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
316-371 7.26e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.00  E-value: 7.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241    316 RDIENILRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDpFDGRPFIDVIRRNYE 371
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEE-LIGKSLLELIHPEDR 55
PAS_7 pfam12860
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
322-436 3.79e-04

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 432837 [Multi-domain]  Cd Length: 115  Bit Score: 41.37  E-value: 3.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   322 LRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDPFDGRPFIDVIRRNYELGRYdGTQTPEEIYDFRKHLFETEEPEPIE 401
Cdd:pfam12860    1 LENMSQGLSVFDADLRLVAWNRRYRELLDLPEDLVQVGVPFEEIIRYNAERGEY-GPGDVEAHVRRRLAAARAGSPHYFE 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 636783241   402 LGWAGGKSVIFDSRRISNDRILLTYADITAVRERE 436
Cdd:pfam12860   80 RERPDGRVIEIRGNPLPDGGFVTTFTDITERRRAE 114
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
184-250 1.36e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 38.15  E-value: 1.36e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636783241    184 DLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALE 250
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
577-1106 5.16e-112

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 370.72  E-value: 5.16e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  577 RAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKLRKA 656
Cdd:PRK11107  285 RAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENI 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  657 AFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVFVDVGFETAAGGEIM 736
Cdd:PRK11107  365 PFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQ 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  737 ASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPfavaaar 816
Cdd:PRK11107  445 LEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLP------- 517
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  817 LEPKPLPIN-------VQGARILVVDDNEVNRRILTEQLSLWGFDgVaaegggTGLAILEAAADLgvTVDAVVLDYHMPD 889
Cdd:PRK11107  518 LDLNPNPIIdglptdcLAGKRLLYVEPNSAAAQATLDILSETPLE-V------TYSPTLSQLPEA--HYDILLLGLPVTF 588
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  890 MNG-ADVARRLRADPRFVELPIIFLTSMDISGTEKeFAALNGHAHLMKParanvlrntvvevVRASRVKQASEAEiarlQ 968
Cdd:PRK11107  589 REPlTMLHERLAKAKSMTDFLILALPCHEQVLAEQ-LKQDGADACLSKP-------------LSHTRLLPALLEP----C 650
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  969 TEAAVPAPALVPQKRAAefVDVLVAEDNEVNqivftQILQGTGLSFLV-----VDNGEEAVAAWERYTPRIIMMDVSMPV 1043
Cdd:PRK11107  651 HHKQPPLLPPTDESRLP--LTVMAVDDNPAN-----LKLIGALLEEQVehvvlCDSGHQAVEQAKQRPFDLILMDIQMPG 723
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636783241 1044 MNGHQATQTIRereKGQGHR-VPIIGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQW 1106
Cdd:PRK11107  724 MDGIRACELIR---QLPHNQnTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
562-901 3.28e-88

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: 306.32  E-value: 3.28e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   562 TELKSREEELRQLLSRAEA--ADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIIND 639
Cdd:TIGR02956  439 TNERLNAEVKNHAKARAEAeeANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILND 518
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   640 ILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERG 719
Cdd:TIGR02956  519 ILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRG 598
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   720 HVFVDVGFEtaagGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDasSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWG 799
Cdd:TIGR02956  599 SVVLRVSLN----DDSSLLFEVEDTGCGIAEEEQATLFDAFTQAD--GRRRSGGTGLGLAISQRLVEAMDGELGVESELG 672
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   800 KGSVFTVNLPFAVAAARLEPKPL-PINVQGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtV 878
Cdd:TIGR02956  673 VGSCFWFTLPLTRGKPAEDSATLtVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHA-----F 747
                          330       340
                   ....*....|....*....|...
gi 636783241   879 DAVVLDYHMPDMNGADVARRLRA 901
Cdd:TIGR02956  748 DLALLDINLPDGDGVTLLQQLRA 770
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
478-811 4.26e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 257.14  E-value: 4.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  478 ALSDILQIPATYLERGEGWIGMFEYCAARGDFHDAAAETLQGWRDNIAARLPISTAFHVGGERWVNMDATVSRGQHWVAL 557
Cdd:COG0642     3 LLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  558 FTDVTELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTnLDTRQKTFVDIIVKSGNALLTII 637
Cdd:COG0642    83 LLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  638 NDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPaAVIGDAGRFRQIVTNLVGNAVKFTE 717
Cdd:COG0642   162 NDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  718 RGHVfVDVGFETAAGgeiMASIRIEDTGIGIPPEKLESVFDKFSQVDASstRRHEGTGLGLAITAGLVDLFGGYLNVDSE 797
Cdd:COG0642   241 EGGT-VTVSVRREGD---RVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESE 314
                         330
                  ....*....|....
gi 636783241  798 WGKGSVFTVNLPFA 811
Cdd:COG0642   315 PGKGTTFTVTLPLA 328
PRK15347 PRK15347
two component system sensor kinase;
567-1103 1.53e-70

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 254.57  E-value: 1.53e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  567 REEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKI 646
Cdd:PRK15347  380 RTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRI 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  647 DAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVFVDVG 726
Cdd:PRK15347  460 ESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVK 539
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  727 FEtaaggEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASStrrhEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTV 806
Cdd:PRK15347  540 RH-----EQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSL 610
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  807 NLPFAVAAArlepkPLPINVQGARILVvddnevnrriLTEQLSLWGFdgvaaegggTGLAILEaaadlgvtvdavvldyh 886
Cdd:PRK15347  611 VLPLNEYAP-----PEPLKGELSAPLA----------LHRQLSAWGI---------TCQPGHQ----------------- 649
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  887 mpdmngadvarrlraDPRFVELPIIFLtsmdisgtekefaalnghahlmkPARanvLRNtvvevvrasRVKQaseaEIAR 966
Cdd:PRK15347  650 ---------------NPALLDPELAYL-----------------------PGR---LYD---------LLQQ----IIQG 675
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  967 LQTEAAVPAPaLVPQKraaefVDVLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNG 1046
Cdd:PRK15347  676 APNEPVINLP-LQPWQ-----LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDG 749
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 636783241 1047 HQATQTIREREKGQGHRVPIIGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKI 1103
Cdd:PRK15347  750 LETTQLWRDDPNNLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL 806
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
570-809 9.88e-70

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 233.26  E-value: 9.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  570 ELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAK--TNLDTRQKTFVDIIVKSGNALLTIINDILDFSKID 647
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  648 AGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPaAVIGDAGRFRQIVTNLVGNAVKFT-ERGHVFVDVg 726
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSpPGGTITISA- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  727 feTAAGGEImaSIRIEDTGIGIPPEKLESVFDKFSQVDasSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTV 806
Cdd:COG2205   159 --RREGDGV--RISVSDNGPGIPEEELERIFERFYRGD--NSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTV 232

                  ...
gi 636783241  807 NLP 809
Cdd:COG2205   233 TLP 235
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
409-809 9.91e-69

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 235.99  E-value: 9.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  409 SVIFDSRRISNDRILLTYADITAVREREKEIHETRAALERLGEMMRDATHAMPQGLAIVQDGIIRMSNEALSDILQIPAT 488
Cdd:COG5002     3 LLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  489 YLERGEGWIGMFEYCAARGDFHDAAAETLQGWRDNIAARLPISTAFHVGGERWVNMDATVSRGQHWVALFTDVTELksre 568
Cdd:COG5002    83 LLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITEL---- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  569 eelrqllsraEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDT--RQKTFVDIIVKSGNALLTIINDILDFSKI 646
Cdd:COG5002   159 ----------ERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDpeERREYLEIILEEAERLSRLVNDLLDLSRL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  647 DAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDlPAAVIGDAGRFRQIVTNLVGNAVKFT-ERGHVFVDV 725
Cdd:COG5002   229 ESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTpEGGTITVSL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  726 gfeTAAGGEIMasIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFT 805
Cdd:COG5002   308 ---REEDDQVR--ISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFT 382

                  ....
gi 636783241  806 VNLP 809
Cdd:COG5002   383 ITLP 386
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
568-1100 2.78e-68

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 247.96  E-value: 2.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  568 EEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKID 647
Cdd:PRK10841  430 EESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIE 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  648 AGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERG----HVFV 723
Cdd:PRK10841  510 SEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGcivlHVRV 589
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  724 DVGFetaaggeimASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSV 803
Cdd:PRK10841  590 DGDY---------LSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQ 660
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  804 FTVNLPfaVAAARLEPKPLPINVQGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGgtglailEAAADlgvtvDAVVL 883
Cdd:PRK10841  661 FTIRIP--LYGAQYPQKKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQRYEGQ-------EPTPE-----DVLIT 726
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  884 DYhmPDmngaDVARRLRADPRFVELPIifltsmdisGTEKEFAALNGHAHLMKPARANVLRNtvvevvRASRVKQASEae 963
Cdd:PRK10841  727 DD--PV----QKKWQGRAVITFCRRHI---------GIPLEIAPGEWVHSTATPHELPALLA------RIYRIELESD-- 783
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  964 iarlqtEAAVPAPALVPQKRAAEFVDVLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPV 1043
Cdd:PRK10841  784 ------DSANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPN 857
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 636783241 1044 MNGHQATQTIRErekgQGHRVPIIGVTAHALESDRELCLDAGMDDYMSKPISPELLE 1100
Cdd:PRK10841  858 MDGYRLTQRLRQ----LGLTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLK 910
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
312-809 7.56e-65

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: 227.94  E-value: 7.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  312 ELLHRDIENILRSL----PVGVLILDNDHRILYVNDEFYGIWELPLDDpFDGRPFIDVIRRNYElgrydgtqtpEEIYDF 387
Cdd:COG5809     7 ELQLRKSEQRFRSLfenaPDAILILDLEGKILKVNPAAERIFGYTEDE-LLGTNILDFLHPDDE----------KELREI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  388 RKHLFETEEPEPIELGWA--GGKSVIFDSRRI----SNDRILLTYA---DITAVREREKEIHETRaalERLgemmRDATH 458
Cdd:COG5809    76 LKLLKEGESRDELEFELRhkNGKRLEFSSKLSpifdQNGDIEGMLAisrDITERKRMEEALRESE---EKF----RLIFN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  459 AMPQGLAIV-QDGIIRMSNEALSDILQIPATylergegwigmfEYCAARGD--FHDAAAETLQGWRDNIAARLPISTA-F 534
Cdd:COG5809   149 HSPDGIIVTdLDGRIIYANPAACKLLGISIE------------ELIGKSILelIHSDDQENVAAFISQLLKDGGIAQGeV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  535 HV----GGERWVNMDAT---VSRGQHW-VALFTDVTELKSREEELRqllsRAEAADRAkSEFLANMSHEIRTPMNGVLGM 606
Cdd:COG5809   217 RFwtkdGRWRLLEASGApikKNGEVDGiVIIFRDITERKKLEELLR----KSEKLSVV-GELAAGIAHEIRNPLTSLKGF 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  607 AELLAKTNlDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKLrkaaFDITEAVEDVATLLSSHAAEKNIELLVRA 686
Cdd:COG5809   292 IQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYEP----KDLNTLIEEVIPLLQPQALLKNVQIELEL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  687 APDLPAaVIGDAGRFRQIVTNLVGNAVKFTER-GHVFVDVGFEtaAGGEIMasIRIEDTGIGIPPEKLESVFDKFSqvda 765
Cdd:COG5809   367 EDDIPD-ILGDENQLKQVFINLLKNAIEAMPEgGNITIETKAE--DDDKVV--ISVTDEGCGIPEERLKKLGEPFY---- 437
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 636783241  766 ssTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:COG5809   438 --TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLP 479
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
560-914 6.73e-64

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 232.52  E-value: 6.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  560 DVTELKSREEELrqllsraEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIIND 639
Cdd:PRK11091  265 DITERKRYQDAL-------EKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFND 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  640 ILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERG 719
Cdd:PRK11091  338 IIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQG 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  720 HVFVDVGFETAAggeiMASIRIEDTGIGIPPEKLESVFDKFSQV-DASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEW 798
Cdd:PRK11091  418 GVTVRVRYEEGD----MLTFEVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  799 GKGSVFTVNLPFAVAAARLEPKPLPINVQGA--RILVVDDNEVN---RRILTEQLslwGFDGVAAEGGGTGLAILEAAAd 873
Cdd:PRK11091  494 GKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPalNILLVEDIELNvivARSVLEKL---GNSVDVAMTGKEALEMFDPDE- 569
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 636783241  874 lgvtVDAVVLDYHMPDMNGADVARRLRADPRFVEL-PIIFLT 914
Cdd:PRK11091  570 ----YDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALT 607
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
563-899 2.32e-63

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 233.26  E-value: 2.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  563 ELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILD 642
Cdd:PRK11466  422 ELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILD 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  643 FSKIDAG--QMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGH 720
Cdd:PRK11466  502 YSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGS 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  721 VFVDVGFEtaaggEIMASIRIEDTGIGIPPEKLESVFDKFSQVDAsstrRHEGTGLGLAITAGLVDLFGGYLNVDSEWGK 800
Cdd:PRK11466  582 IVLRSRTD-----GEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTISSRLAQAMGGELSATSTPEV 652
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  801 GSVFTVNLPFAVAAARLEPKPL-PINVQGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAaadlGVTVD 879
Cdd:PRK11466  653 GSCFCLRLPLRVATAPVPKTVNqAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQN----SEPFA 728
                         330       340
                  ....*....|....*....|
gi 636783241  880 AVVLDYHMPDMNGADVARRL 899
Cdd:PRK11466  729 AALVDFDLPDYDGITLARQL 748
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
445-815 2.44e-52

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 188.13  E-value: 2.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  445 ALERLGEMMRDATHAMPQGLAIV-QDGIIRMSNEALSDILQIPATYLergegwIGM--FEYCAARGDFHDAAAETLQGWR 521
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVLdADGRITYVNPAAERLLGLSAEEL------LGRplAELFPEDSPLRELLERALAEGQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  522 DNIAARLPISTAFhvGGERWVNMDAT----VSRGQHWVALFTDVTELKSREEELRQLlSRAEAAdrakSEFLANMSHEIR 597
Cdd:COG3852    75 PVTEREVTLRRKD--GEERPVDVSVSplrdAEGEGGVLLVLRDITERKRLERELRRA-EKLAAV----GELAAGLAHEIR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  598 TPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKidagQMKLRKAAFDITEAVEDVATLLSShAAE 677
Cdd:COG3852   148 NPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSR----PRPPEREPVNLHEVLERVLELLRA-EAP 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  678 KNIELLVRAAPDLPAaVIGDAGRFRQIVTNLVGNAVKFTERGHV------FVDVGFETAAGGEIMASIRIEDTGIGIPPE 751
Cdd:COG3852   223 KNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEAMPEGGTitirtrVERQVTLGGLRPRLYVRIEVIDNGPGIPEE 301
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636783241  752 KLESVFDKFsqVdassTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFAVAAA 815
Cdd:COG3852   302 ILDRIFEPF--F----TTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEE 359
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
437-815 1.87e-48

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: 178.62  E-value: 1.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  437 KEIHETRAALERLGEMMRDATHAMPQGLAIV-QDGIIRMSNEALSDILQIPAtylergEGWIGM-FEYCAARGDFHDAAA 514
Cdd:COG5000    76 DQLKEQREELEERRRYLETILENLPAGVIVLdADGRITLANPAAERLLGIPL------EELIGKpLEELLPELDLAELLR 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  515 ETLQ-GWRDNIAarlpistaFHVGGERWVNMDATVSRGQHWVALFTDVTELKSREEElrqllsraeaadRAKSEFLANMS 593
Cdd:COG5000   150 EALErGWQEEIE--------LTRDGRRTLLVRASPLRDDGYVIVFDDITELLRAERL------------AAWGELARRIA 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  594 HEIRTPMNGVLGMAELLAK------TNLDTRQKTFVDIIVKSGNALLTIINDILDFSKIDagqmKLRKAAFDITEAVEDV 667
Cdd:COG5000   210 HEIKNPLTPIQLSAERLRRkladklEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLREV 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  668 ATLLSSHAAEKNIELLVRAAPDLPAaVIGDAGRFRQIVTNLVGNAVKFTE-RGHVFVDVGFETAaggeiMASIRIEDTGI 746
Cdd:COG5000   286 LALYEPALKEKDIRLELDLDPDLPE-VLADRDQLEQVLINLLKNAIEAIEeGGEIEVSTRREDG-----RVRIEVSDNGP 359
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636783241  747 GIPPEKLESVFDKFSqvdasSTRRHeGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFAVAAA 815
Cdd:COG5000   360 GIPEEVLERIFEPFF-----TTKPK-GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEAE 422
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
701-810 3.01e-48

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: 166.90  E-value: 3.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  701 FRQIVTNLVGNAVKFTERGHVFVDVGFETAAGGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAI 780
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 636783241  781 TAGLVDLFGGYLNVDSEWGKGSVFTVNLPF 810
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
303-809 5.49e-47

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 176.51  E-value: 5.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  303 ALIEAQKHKELLHRDIENILRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDPFDGRPFIDVIRRNYELGRYDGTQTPE 382
Cdd:COG4251     1 LLLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  383 EIYDFRKHLFETEEPEPIELGWAGGKSVIFDSRRISNDRILLTYADITAVREREKEIHETRAALERLGEMMRDATHAMPQ 462
Cdd:COG4251    81 LLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  463 GLAIVQDGIIRMSNEALSDILQIPATYLERGEGWIGMFEYCAARGDFHDAAAETLQGWRDNIAARLpISTAFHVGGERWV 542
Cdd:COG4251   161 LLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLG-LLLLLLLLLVLLL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  543 NMDATVSRGQHWVALFTDVTELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELL---AKTNLDTRQ 619
Cdd:COG4251   240 LLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLeedYGDKLDEEG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  620 KTFVDIIVKSGNALLTIINDILDFSKIdaGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVraaPDLPAaVIGDAG 699
Cdd:COG4251   320 REYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEV---GPLPT-VRGDPT 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  700 RFRQIVTNLVGNAVKFTERGHV-FVDVGFETAAGgeiMASIRIEDTGIGIPPEKLESVFDKFSQVDasSTRRHEGTGLGL 778
Cdd:COG4251   394 LLRQVFQNLISNAIKYSRPGEPpRIEIGAEREGG---EWVFSVRDNGIGIDPEYAEKIFEIFQRLH--SRDEYEGTGIGL 468
                         490       500       510
                  ....*....|....*....|....*....|.
gi 636783241  779 AITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:COG4251   469 AIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
554-972 2.98e-45

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 178.39  E-value: 2.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  554 WVALFTDVTELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKT-FVDIIVKSGNA 632
Cdd:PRK09959  681 YICGWQDITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVeAISLAYATGQS 760
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  633 LLTIINDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAA-PDLPAAVIgDAGRFRQIVTNLVGN 711
Cdd:PRK09959  761 LLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPDHYLVKI-DPQAFKQVLSNLLSN 839
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  712 AVKFTERGHVFVDVGFETAAGGEIMASIRIEDTGIGIPPEKLESVFDKFSQvdASSTRRHEGTGLGLAITAGLVDLFGGY 791
Cdd:PRK09959  840 ALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGD 917
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  792 LNVDSEWGKGSVFTVNLPF-------AVAAARLEPKPLPinvQGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTG 864
Cdd:PRK09959  918 LSLESHPGIGTTFTITIPVeisqqvaTVEAKAEQPITLP---EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQA 994
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  865 LAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPRfvELPIIFLTSmDISGTEKEfAALNGHAH--LMKPARANV 942
Cdd:PRK09959  995 LHKVSMQH-----YDLLITDVNMPNMDGFELTRKLREQNS--SLPIWGLTA-NAQANERE-KGLSCGMNlcLFKPLTLDV 1065
                         410       420       430
                  ....*....|....*....|....*....|.
gi 636783241  943 LRNTVVEVVRASR-VKQASEAEIARLQTEAA 972
Cdd:PRK09959 1066 LKTHLSQLHQVAHiAPQYRHLDIEALKNNTA 1096
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
447-811 4.37e-45

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 166.90  E-value: 4.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  447 ERLGEMMRDATHAMPQGLAIVQDGIIRMSNEALSDILQIPATYLERGEGWIGMFEYCAARGDFHDAAAETLQGWRDNIAA 526
Cdd:COG4191     1 ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  527 RLPISTAFHVGGERWVNMDATVSRGQHWV-ALFTDVTELKSREEELRQLLSRAEAADRAKS--EFLANMSHEIRTPMNGV 603
Cdd:COG4191    81 LLGLLLLLLLEALLLLLLAALDAEENAELeELERDITELERAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  604 LGMAELL----AKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKidagQMKLRKAAFDITEAVEDVATLLSSHAAEKN 679
Cdd:COG4191   161 LGNAELLrrrlEDEPDPEELREALERILEGAERAAEIVRSLRAFSR----RDEEEREPVDLNELIDEALELLRPRLKARG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  680 IELLVRAAPDLPAaVIGDAGRFRQIVTNLVGN---AVKFTERGHVFVdvgfETAAGGEiMASIRIEDTGIGIPPEKLESV 756
Cdd:COG4191   237 IEVELDLPPDLPP-VLGDPGQLEQVLLNLLINaidAMEEGEGGRITI----STRREGD-YVVISVRDNGPGIPPEVLERI 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241  757 FDKFSqvdasSTRR-HEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFA 811
Cdd:COG4191   311 FEPFF-----TTKPvGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
990-1103 4.10e-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: 155.32  E-value: 4.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGqGHRVPIIGV 1069
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGG-GRRTPIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKI 1103
Cdd:cd17546    80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
990-1112 3.04e-39

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: 141.91  E-value: 3.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREkgQGHRVPIIGV 1069
Cdd:COG0784     8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALP--RLPDIPIIAL 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTSEQ 1112
Cdd:COG0784    86 TAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
555-806 5.30e-39

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


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 148.51  E-value: 5.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   555 VALFTDVTELksreeelRQLlsraeaaDRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNL--DTRQKTFVDIIVKSGNA 632
Cdd:TIGR02966   98 LLVARDVTRL-------RRL-------EQMRRDFVANVSHELRTPLTVLRGYLETLADGPDedPEEWNRALEIMLEQSQR 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   633 LLTIINDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPaaVIGDAGRFRQIVTNLVGNA 712
Cdd:TIGR02966  164 MQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNA 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   713 VKFTERGHVfVDVGFETAAGGeimASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYL 792
Cdd:TIGR02966  242 IKYTPEGGT-ITVRWRRDGGG---AEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARL 317
                          250
                   ....*....|....
gi 636783241   793 NVDSEWGKGSVFTV 806
Cdd:TIGR02966  318 EIESELGKGSTFSF 331
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
282-809 1.31e-33

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: 136.40  E-value: 1.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  282 DGRPYVVGSFSDISPLKEREKALIEAQKHKELLHRDIENilrsLPVGVLILDNDHRILYVNDEFYGIWELPLDDpFDGRP 361
Cdd:COG5805     4 KLYDFIHEVKKDGTPIWINNEVLRMAIEITEELETILEN----LPDAIIAVNREGKVIYINPAMEKLLGYTSEE-IIGKT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  362 FIDVIRRNYELGRYDGTQTPEEIYDFRkhLFETEEPEPIELGWAggKSVIFDSRRISNDRILLTYADITAVREREKEIHE 441
Cdd:COG5805    79 IFDFLEKEYHYRVKTRIERLQKGYDVV--MIEQIYCKDGELIYV--EVKLFPIYNQNGQAAILALRDITKKKKIEEILQE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  442 TRAALERLgemmrdaTHAMPQGLAIV-QDGIIRMSNEALSDILQIPAtYLERGEGWIGMFEYCAARgDFHDAAAETLQGW 520
Cdd:COG5805   155 QEERLQTL-------IENSPDLICVIdTDGRILFINESIERLFGAPR-EELIGKNLLELLHPCDKE-EFKERIESITEVW 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  521 RDNIAARLPI-----STAFHVGGERWVNMDATVSRGQhWVALftDVTELKSREEELRQL--LSRAeaadrakSEFLANMS 593
Cdd:COG5805   226 QEFIIEREIItkdgrIRYFEAVIVPLIDTDGSVKGIL-VILR--DITEKKEAEELMARSekLSIA-------GQLAAGIA 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  594 HEIRTPMNGVLGMAELLaKTNLDTrQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKlrkaAFDITEAVEDVATLLSS 673
Cdd:COG5805   296 HEIRNPLTSIKGFLQLL-QPGIED-KEEYFDIMLSELDRIESIISEFLALAKPQAVNKE----KENINELIQDVVTLLET 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  674 HAAEKNIELLVRAAPDLPAaVIGDAGRFRQIVTNLVGNAVKFTERGHVfVDVGFEtAAGGEIMasIRIEDTGIGIPPEKL 753
Cdd:COG5805   370 EAILHNIQIRLELLDEDPF-IYCDENQIKQVFINLIKNAIEAMPNGGT-ITIHTE-EEDNSVI--IRVIDEGIGIPEERL 444
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241  754 ESVFDKFSqvdassTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:COG5805   445 KKLGEPFF------TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
562-809 4.24e-32

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 131.36  E-value: 4.24e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   562 TELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAE-LLAKtnlDTRQKTFVDIIVKSG---NALLTII 637
Cdd:TIGR01386  218 AELRELAQSFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQvALSQ---PRTGEEYREVLESNLeelERLSRMV 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   638 NDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAApdlpAAVIGDAGRFRQIVTNLVGNAVKFTE 717
Cdd:TIGR01386  295 SDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGE----GLVRGDPQMFRRAISNLLSNALRHTP 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   718 RGHVfVDVGFETAAGgeiMASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSE 797
Cdd:TIGR01386  371 DGGT-ITVRIERRSD---EVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESP 446
                          250
                   ....*....|..
gi 636783241   798 WGKgSVFTVNLP 809
Cdd:TIGR01386  447 DGK-TRFILRFP 457
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
696-811 6.04e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.45  E-value: 6.04e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241    696 GDAGRFRQIVTNLVGNAVKFT-ERGHVFVDVGFEtaaggEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASStRRHEGT 774
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERD-----GDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRS-RKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 636783241    775 GLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFA 811
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
990-1103 1.14e-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: 122.32  E-value: 1.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQghRVPIIGV 1069
Cdd:COG3706     4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTA--DIPIIFL 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKI 1103
Cdd:COG3706    82 TALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
558-915 6.61e-31

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 131.34  E-value: 6.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  558 FTDVTELKSREEELRQLLSRAEAADR--AKSEFLANMSHEIRTPMNGVLGMAEL-LAKTNLDTRQKTFVDIIVKSGNALL 634
Cdd:PRK13837  421 LAHAIERRRLETERDALERRLEHARRleAVGTLASGIAHNFNNILGAILGYAEMaLNKLARHSRAARYIDEIISAGARAR 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  635 TIINDILDFSKIDAGQMKlrkaAFDITEAVEDVATLLSShAAEKNIELLVRAAPDlPAAVIGDAGRFRQIVTNLVGNAVK 714
Cdd:PRK13837  501 LIIDQILAFGRKGERNTK----PFDLSELVTEIAPLLRV-SLPPGVELDFDQDQE-PAVVEGNPAELQQVLMNLCSNAAQ 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  715 -FTERGHV--FVDVGFETAAG----GEIMAS----IRIEDTGIGIPPEKLESVFDKFSqvdassTRRHEGTGLGLAITAG 783
Cdd:PRK13837  575 aMDGAGRVdiSLSRAKLRAPKvlshGVLPPGryvlLRVSDTGAGIDEAVLPHIFEPFF------TTRAGGTGLGLATVHG 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  784 LVDLFGGYLNVDSEWGKGSVFTVNLPF-----AVAAARLEPKPLPINvQGARILVVDDNEVNRRILTEQLSLWGFDGVaa 858
Cdd:PRK13837  649 IVSAHAGYIDVQSTVGRGTRFDVYLPPsskvpVAPQAFFGPGPLPRG-RGETVLLVEPDDATLERYEEKLAALGYEPV-- 725
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 636783241  859 egGGTGLA-ILEAAADLGVTVDAVVLDYHMPDMNGADVARRLRADPrfveLPIIFLTS 915
Cdd:PRK13837  726 --GFSTLAaAIAWISKGPERFDLVLVDDRLLDEEQAAAALHAAAPT----LPIILGGN 777
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
569-823 7.39e-31

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 128.22  E-value: 7.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  569 EELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELL--AKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKI 646
Cdd:NF040691  255 DSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRF 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  647 DAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRaAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVFVdvg 726
Cdd:NF040691  335 DAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVD-APGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVV--- 410
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  727 feTAAGGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTV 806
Cdd:NF040691  411 --TVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRL 488
                         250
                  ....*....|....*..
gi 636783241  807 NLPfAVAAARLEPKPLP 823
Cdd:NF040691  489 TLP-RVAGDRLTTSPLP 504
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
827-955 2.17e-30

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: 116.49  E-value: 2.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  827 QGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRFV 906
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG-----PPDLILLDINMPGMDGLELLRRIRALPRLP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 636783241  907 ELPIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVRASR 955
Cdd:COG0784    79 DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
555-809 2.04e-29

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 125.08  E-value: 2.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  555 VALFTDVTELKSREEELRQllsraeaADR--AKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNA 632
Cdd:PRK11360  365 LVIFSDLTERKRLQRRVAR-------QERlaALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDR 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  633 LLTIINDILDFSKidAGQMKLRKaaFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAAVIgDAGRFRQIVTNLVGNA 712
Cdd:PRK11360  438 LNKVIDQLLEFSR--PRESQWQP--VSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWA-DPELLKQVLLNILINA 512
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  713 VK-FTERGHVFVDVGFETAagGEIMasIRIEDTGIGIPPEKLESVFDKFSqvdassTRRHEGTGLGLAITAGLVDLFGGY 791
Cdd:PRK11360  513 VQaISARGKIRIRTWQYSD--GQVA--VSIEDNGCGIDPELLKKIFDPFF------TTKAKGTGLGLALSQRIINAHGGD 582
                         250
                  ....*....|....*...
gi 636783241  792 LNVDSEWGKGSVFTVNLP 809
Cdd:PRK11360  583 IEVESEPGVGTTFTLYLP 600
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
696-811 1.18e-27

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: 108.22  E-value: 1.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   696 GDAGRFRQIVTNLVGNAVKFT-ERGHVFVDVgfetAAGGEImaSIRIEDTGIGIPPEKLESVFDKFSQVDassTRRHEGT 774
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTL----SEGGEL--TLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 636783241   775 GLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFA 811
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
990-1105 3.58e-27

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: 106.86  E-value: 3.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqGHRVPIIGV 1069
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPA--TRDIPVIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQ 1105
Cdd:cd17548    80 TAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
990-1104 9.18e-27

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: 105.70  E-value: 9.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPIIGV 1069
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRR----DPTTPVIIL 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 636783241  1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:pfam00072   77 TAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
829-952 1.50e-26

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 107.30  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPRFVEL 908
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR-----PDLILLDLEMPDMDGLELCRRLRADPRTADI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 636783241  909 PIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVR 952
Cdd:COG3706    77 PIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVAR 120
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
990-1115 3.20e-26

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: 107.94  E-value: 3.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQghRVPIIGV 1069
Cdd:COG3437     9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTR--DIPVIFL 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTSEQQPE 1115
Cdd:COG3437    87 TALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRE 132
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
990-1104 6.89e-26

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 106.58  E-value: 6.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPIIGV 1069
Cdd:COG0745     4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR----PSDIPIIML 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:COG0745    80 TARDDEEDRVRGLEAGADDYLTKPFDPEELLARIR 114
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
543-820 2.85e-25

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 110.65  E-value: 2.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  543 NMDATVSRGQHWVALFTDVTEL-----------KSREEELRQLLSRAEAADR---AKSEFLANMSHEIRTPMNGVLGMAE 608
Cdd:PRK10364  181 NLVSAQAREQRNTLIILFALATvllasllaffwYRRYLRSRQLLQDEMKRKEklvALGHLAAGVAHEIRNPLSSIKGLAK 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  609 LLA-KTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKidagQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAA 687
Cdd:PRK10364  261 YFAeRAPAGGEAHQLAQVMAKEADRLNRVVSELLELVK----PTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTAN 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  688 PDLPAAVIgDAGRFRQIVTNLVGNAVKFTERGHVFVDVGFETAAGGEIMasirIEDTGIGIPPEKLESVFDKFSqvdass 767
Cdd:PRK10364  337 DTLPEIQA-DPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKIS----VTDSGKGIAADQLEAIFTPYF------ 405
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 636783241  768 TRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPfaVAAARLEPK 820
Cdd:PRK10364  406 TTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLP--VNITRRDPQ 456
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
526-809 3.30e-25

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 110.30  E-value: 3.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  526 ARLPISTAFHVGGERWVNMDATVSRG--QHWVALfTDVTELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMnGV 603
Cdd:NF012163  180 AAFLLARGLLAPVKRLVEATHRLAAGdyTTRVTP-TSNDELGKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPL-AV 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  604 LgMAELLAKTNlDTRQKT--FVDIIVKSGNALLTIINDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIE 681
Cdd:NF012163  258 L-RAELEAIQD-GIRKFTpeSLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  682 LLVraapDLPAA--VIGDAGRFRQIVTNLVGNAVKFTERG---HVfvdvgfeTAAGGEIMASIRIEDTGIGIPPEKLESV 756
Cdd:NF012163  336 LEV----SLPDSslVFGDRDRLMQLFNNLLENSLRYTDSGgslHI-------SASQRPKEVTLTVADSAPGVSDEQLARL 404
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 636783241  757 FDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:NF012163  405 FERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
827-971 5.22e-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: 5.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  827 QGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRFV 906
Cdd:COG3437     5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEA-----PPDLILLDVRMPGMDGFELLRLLRADPSTR 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636783241  907 ELPIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVRASRVKQASEAEIARLQTEA 971
Cdd:COG3437    80 DIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAA 144
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
422-809 2.32e-24

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 106.86  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  422 ILLTYADITAVREREKEIHETRAALERLGEMMrdatHAMPQG-LAIVQDGIIRMSNEALSDILQIPATYLERGEgwigmf 500
Cdd:COG3290    59 ILLLLLLLLLAALLLKLLEEIARLVEEREAVL----ESIREGvIAVDRDGRITLINDAARRLLGLDAIGRPIDE------ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  501 eYCAARGDFHDAAAETLQGWRDNIAARLPISTAFHVGGerwvnmdatvsrgqhWVALFTDVTELKSREEELRQLLSRAEA 580
Cdd:COG3290   129 -VLAEVLETGERDEEILLNGRVLVVNRVPIRDDGRVVG---------------AVATFRDRTELERLEEELEGVKELAEA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  581 AdRAkseflanMSHEIRTPMNGVLGMAEL--------LAKTNLDTRQKTFVDIIVKSGNallTIINDILdfskidagqmk 652
Cdd:COG3290   193 L-RA-------QRHDFRNHLHTISGLLQLgeydealeYIDEISEELQELIDSLLSRIGN---PVLAALL----------- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  653 LRKAafditeavedvatllsSHAAEKNIELLVRAAPDLPAAVIGDAGrFRQIVTNLVGNA---VKFTERGHVFVDVGFeT 729
Cdd:COG3290   251 LGKA----------------ARARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAieaVEKLPEEERRVELSI-R 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  730 AAGGEIMasIRIEDTGIGIPPEKLESVFDK-FSqvdassTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNL 808
Cdd:COG3290   313 DDGDELV--IEVEDSGPGIPEELLEKIFERgFS------TKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384

                  .
gi 636783241  809 P 809
Cdd:COG3290   385 P 385
PAS COG2202
PAS domain [Signal transduction mechanisms];
182-439 6.91e-24

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 102.41  E-value: 6.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  182 ELDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALEGGTSKEIESLL 261
Cdd:COG2202     9 SERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  262 PSKDGHIYSVLSRVNRVVTADGRP-YVVGSFSDISPLKEREKALIEAQKHkellhrdIENILRSLPVGVLILDNDHRILY 340
Cdd:COG2202    89 RRKDGSLFWVELSISPVRDEDGEItGFVGIARDITERKRAEEALRESEER-------LRLLVENAPDGIFVLDLDGRILY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  341 VNDEFYGIWELPLDDpFDGRPFIDVIrrnYELGRYDGTQTPEEIYDFRKHLFETEEPEPIELGWAGG--KSVIFDSRRIS 418
Cdd:COG2202   162 VNPAAEELLGYSPEE-LLGKSLLDLL---HPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWveASAVPLRDGGE 237
                         250       260
                  ....*....|....*....|.
gi 636783241  419 NDRILLTYADITAVREREKEI 439
Cdd:COG2202   238 VIGVLGIVRDITERKRAEEAL 258
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
549-809 6.00e-23

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 103.17  E-value: 6.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  549 SRGQhWVALFTDVTELksreeelRQLlsraEAADRaksEFLANMSHEIRTPMNGVLGMAELLAKTNLD--TRQKTfVDII 626
Cdd:PRK11006  183 TEGQ-LLMVARDVTQM-------HQL----EGARR---NFFANVSHELRTPLTVLQGYLEMMQDQPLEgaLREKA-LHTM 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  627 VKSGNALLTIINDILDFSKIDAGQMKLRKAAFDIT---EAVEDVATLLSshaaEKNIELLVRAAPDLpaAVIGDAGRFRQ 703
Cdd:PRK11006  247 REQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPmmlRVLEREAQTLS----QGKHTITFEVDNSL--KVFGNEDQLRS 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  704 IVTNLVGNAVKFTERG-HVFVDvGFETAAGgeimASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITA 782
Cdd:PRK11006  321 AISNLVYNAVNHTPEGtHITVR-WQRVPQG----AEFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVK 395
                         250       260
                  ....*....|....*....|....*..
gi 636783241  783 GLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:PRK11006  396 HALSHHDSRLEIESEVGKGTRFSFVLP 422
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
570-809 1.17e-22

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 102.93  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  570 ELRQL-------LSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAEL-LAKTNldtRQKTFVDIIVKS---GNALLTIIN 638
Cdd:PRK09835  240 ELEQLvlsfnhmIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIaLSQSR---SQKELEDVLYSNleeLTRMAKMVS 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  639 DILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPdlpAAVIGDAGRFRQIVTNLVGNAVKFTER 718
Cdd:PRK09835  317 DMLFLAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELRFVGDP---CQVAGDPLMLRRAISNLLSNALRYTPA 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  719 GHVFVDVGFETAAGGEIMasirIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEw 798
Cdd:PRK09835  394 GEAITVRCQEVDHQVQLV----VENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSD- 468
                         250
                  ....*....|.
gi 636783241  799 GKGSVFTVNLP 809
Cdd:PRK09835  469 ARGTRFVISLP 479
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
697-809 1.48e-21

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: 90.63  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  697 DAGRFRQIVTNLVGNAVKFTERGHVfVDVGFETAAGGEIMasIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGL 776
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGR-IRCILEKFRLNRFL--LTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 636783241  777 GLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16925    78 GLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
584-649 1.79e-21

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 88.81  E-value: 1.79e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241   584 AKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAG 649
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
990-1103 2.45e-21

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: 90.21  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREkgQGHRVPIIGV 1069
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELP--WLANTPAIAL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKI 1103
Cdd:cd17580    79 TGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
584-649 5.43e-21

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 87.62  E-value: 5.43e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241    584 AKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAG 649
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
829-955 5.70e-21

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: 92.33  E-value: 5.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRfvEL 908
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEE-----RPDLILLDLMLPGMDGLEVCRRLRARPS--DI 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 636783241  909 PIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVRASR 955
Cdd:COG0745    75 PIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRA 121
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
990-1094 7.88e-21

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: 88.32  E-value: 7.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQghRVPIIGV 1069
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETR--HIPVIMI 79
                          90       100
                  ....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPI 1094
Cdd:cd17538    80 TALDDREDRIRGLEAGADDFLSKPI 104
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
991-1093 1.06e-20

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: 88.05  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  991 LVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGqghrVPIIGVT 1070
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD----IPVIVLT 76
                          90       100
                  ....*....|....*....|...
gi 636783241 1071 AHALESDRELCLDAGMDDYMSKP 1093
Cdd:cd00156    77 AKADEEDAVRALELGADDYLVKP 99
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
830-917 4.11e-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: 86.40  E-value: 4.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRFVELP 909
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEE-----LPDLILLDVMMPGMDGFEVCRRLKEDPETRHIP 75

                  ....*...
gi 636783241  910 IIFLTSMD 917
Cdd:cd17538    76 VIMITALD 83
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
544-809 2.06e-19

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 92.77  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  544 MDATVSR---GQHWVAL--FTDVTELKSREE------ELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAK 612
Cdd:PRK10549  188 LLAPVKRlveGTHKLAAgdFTTRVTPTSRDElgrlaqDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRGELEAIQD 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  613 tnlDTRQKTFVDII-VKSGNALLT-IINDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVraapDL 690
Cdd:PRK10549  268 ---GVRKFTPESVAsLQAEVGTLTkLVDDLHQLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQL----SL 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  691 P--AAVIGDAGRFRQIVTNLVGNAVKFTerghvfvdvgfetAAGGEIMAS---------IRIEDTGIGIPPEKLESVFDK 759
Cdd:PRK10549  341 PdsATVFGDPDRLMQLFNNLLENSLRYT-------------DSGGSLHISaeqrdktlrLTFADSAPGVSDEQLQKLFER 407
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636783241  760 FSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVD-SEWGkGSVFTVNLP 809
Cdd:PRK10549  408 FYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAhSPFG-GVSITVELP 457
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
831-917 3.96e-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: 83.71  E-value: 3.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRFVELPI 910
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAE-----PPDLILLDVMMPGMDGFEVCRRLKADPATRHIPV 75

                  ....*..
gi 636783241  911 IFLTSMD 917
Cdd:cd19920    76 IFLTALT 82
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
991-1093 8.84e-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: 82.46  E-value: 8.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  991 LVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErekgQGHRVPIIGVT 1070
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLRE----KGSDIPIIMLT 76
                          90       100
                  ....*....|....*....|...
gi 636783241 1071 AHALESDRELCLDAGMDDYMSKP 1093
Cdd:cd17574    77 AKDEEEDKVLGLELGADDYITKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
827-963 1.19e-18

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: 90.02  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  827 QGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPRfv 906
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP-----PDLVLLDLRMPGMDGLELLRELRALDP-- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 636783241  907 ELPIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVRASRVKQASEAE 963
Cdd:COG2204    74 DLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAED 130
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
832-937 1.77e-18

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: 81.50  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  832 LVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEaaadlGVTVDAVVLDYHMPDMNGADVARRLRADPRfvELPII 911
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLR-----EERPDLVLLDLMMPGMDGLELLRKLRELPP--DIPVI 73
                          90       100
                  ....*....|....*....|....*.
gi 636783241  912 FLTSMDISGTEKEFAALNGHAHLMKP 937
Cdd:cd00156    74 VLTAKADEEDAVRALELGADDYLVKP 99
PRK10490 PRK10490
sensor protein KdpD; Provisional
572-821 2.39e-18

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 90.87  E-value: 2.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  572 RQLLSRAEAADRAKSE-------FLANMSHEIRTPMNGVLGMAELL-----------AKTNLDTRQKTfvdiivksgnaL 633
Cdd:PRK10490  644 RLTLTASEEQARLASEreqlrnaLLAALSHDLRTPLTVLFGQAEILtldlasegsphARQASEIRQQV-----------L 712
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  634 LTI--INDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELlvraapDLPAAVI---GDAGRFRQIVTNL 708
Cdd:PRK10490  713 NTTrlVNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINL------SLPEPLTlihVDGPLFERVLINL 786
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  709 VGNAVKFTERGhvfVDVGFETAAGGEIMaSIRIEDTGIGIPPEKLESVFDKFSQVDASSTRrhEGTGLGLAITAGLVDLF 788
Cdd:PRK10490  787 LENAVKYAGAQ---AEIGIDAHVEGERL-QLDVWDNGPGIPPGQEQLIFDKFARGNKESAI--PGVGLGLAICRAIVEVH 860
                         250       260       270
                  ....*....|....*....|....*....|...
gi 636783241  789 GGYLNVDSEWGKGSVFTVNLPfavaaarLEPKP 821
Cdd:PRK10490  861 GGTIWAENRPEGGACFRVTLP-------LETPP 886
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
591-811 2.63e-18

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 89.52  E-value: 2.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  591 NMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKLRKAAFDITEAVEDVATL 670
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  671 LSSHAAEKNIELLVRAAPdlpAAVIGDAGRFRQIVTNLVGNAVKFTERGHVfVDVGFETAAGGeimASIRIEDTGIGIPP 750
Cdd:PRK11100  342 REAQAAAKGITLRLRPDD---ARVLGDPFLLRQALGNLLDNAIDFSPEGGT-ITLSAEVDGEQ---VALSVEDQGPGIPD 414
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636783241  751 EKLESVFDKF-SQVDASSTRRheGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFA 811
Cdd:PRK11100  415 YALPRIFERFySLPRPANGRK--STGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRH 474
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
703-809 2.76e-18

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: 81.31  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  703 QIVTNLVGNAVK-FTERGHVFVDVGFETAAggeimASIRIEDTGIGIPPEKLESVFDKFSqvdasSTRRH-EGTGLGLAI 780
Cdd:cd16943     6 QVLLNLLVNAAQaMEGRGRITIRTWAHVDQ-----VLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVgEGTGLGLSL 75
                          90       100
                  ....*....|....*....|....*....
gi 636783241  781 TAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16943    76 SYRIIQKHGGTIRVASVPGGGTRFTIILP 104
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
990-1122 4.44e-18

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: 88.10  E-value: 4.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPIIGV 1069
Cdd:COG2204     5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRAL----DPDLPVILL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTSEQQPERTTAPRI 1122
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGL 133
PRK09303 PRK09303
histidine kinase;
571-809 5.32e-18

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 87.31  E-value: 5.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  571 LRQ----LLSRAEAADRakseFLANMSHEIRTPMNgvlgmAELLAktnLDTRQKTFVDIIVKSGNALLT----------- 635
Cdd:PRK09303  137 LRQenetLLEQLKFKDR----VLAMLAHDLRTPLT-----AASLA---LETLELGQIDEDTELKPALIEqlqdqarrqle 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  636 ----IINDILDFSKIDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVRAAPDLPAaVIGDAGRFRQIVTNLVGN 711
Cdd:PRK09303  205 eierLITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPS-VYADQERIRQVLLNLLDN 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  712 AVKFTErghvfvdvgfetaAGGEIMASI----------RIEDTGIGIPPEKLESVFDkfSQVDASSTRRHEGTGLGLAIT 781
Cdd:PRK09303  284 AIKYTP-------------EGGTITLSMlhrttqkvqvSICDTGPGIPEEEQERIFE--DRVRLPRDEGTEGYGIGLSVC 348
                         250       260
                  ....*....|....*....|....*...
gi 636783241  782 AGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:PRK09303  349 RRIVRVHYGQIWVDSEPGQGSCFHFTLP 376
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
694-808 3.87e-17

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 78.22  E-value: 3.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  694 VIGDAGRFRQIVTNLVGNAVKFTERGHVfVDVGFEtaagGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASSTrrhEG 773
Cdd:cd16940     7 VQGDALLLFLLLRNLVDNAVRYSPQGSR-VEIKLS----ADDGAVIRVEDNGPGIDEEELEALFERFYRSDGQNY---GG 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241  774 TGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNL 808
Cdd:cd16940    79 SGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
582-645 4.72e-17

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: 76.48  E-value: 4.72e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636783241  582 DRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDT-RQKTFVDIIVKSGNALLTIINDILDFSK 645
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDeEQREYLERIREEAERLLRLINDLLDLSR 65
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
830-963 5.49e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 78.47  E-value: 5.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLS-LWGFDGVA-AEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRfvE 907
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLErLPGFEVVGvASSGEEALALLAEH-----RPDLILLDIYLPDGDGLELLRELRARGP--D 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241  908 LPIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVRASRVKQASEAE 963
Cdd:COG4565    78 VDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEE 133
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
829-937 7.81e-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: 77.48  E-value: 7.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSlwGFDGVAAEGGGTGLAILEAAADlgVTVDAVVLDYHMPDMNGADVARRLRADPRFVEL 908
Cdd:cd17551     1 MRILIVDDNPTNLLLLEALLR--SAGYLEVVSFTDPREALAWCRE--NPPDLILLDYMMPGMDGLEFIRRLRALPGLEDV 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 636783241  909 PIIFLTSMdisgTEKEF--AALNGHAH--LMKP 937
Cdd:cd17551    77 PIVMITAD----TDREVrlRALEAGATdfLTKP 105
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
702-809 1.09e-16

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: 76.60  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  702 RQIVTNLVGNAVKFT-ERGHVFVDVGFETAAGGEimaSIRIEDTGIGIPPEKLESVFDKFSQVDasSTRRHEGTGLGLAI 780
Cdd:cd16921     2 GQVLTNLLGNAIKFRrPRRPPRIEVGAEDVGEEW---TFYVRDNGIGIDPEYAEKVFGIFQRLH--SREEYEGTGVGLAI 76
                          90       100
                  ....*....|....*....|....*....
gi 636783241  781 TAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16921    77 VRKIIERHGGRIWLESEPGEGTTFYFTLP 105
PRK13557 PRK13557
histidine kinase; Provisional
631-939 1.43e-16

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 84.34  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  631 NALLTIINDILDF-----SKIDAGQMKLRKAAFDITEAVEDVATL-----------------------------LSSHAA 676
Cdd:PRK13557  175 NNLLQVMSGYLDViqaalSHPDADRGRMARSVENIRAAAERAATLtqqllafarkqrlegrvlnlnglvsgmgeLAERTL 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  677 EKNIELLVRAAPDLPAAVIgDAGRFRQIVTNLVGNAVK-FTERGHVFVD-----------VGFETAAGGEiMASIRIEDT 744
Cdd:PRK13557  255 GDAVTIETDLAPDLWNCRI-DPTQAEVALLNVLINARDaMPEGGRVTIRtrnveiededlAMYHGLPPGR-YVSIAVTDT 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  745 GIGIPPEKLESVFDKFsqvdasSTRRHE--GTGLGLAITAGLVDLFGGYLNVDSEWGKGSvfTVNLPF----AVAAARLE 818
Cdd:PRK13557  333 GSGMPPEILARVMDPF------FTTKEEgkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGT--TVRLYFpasdQAENPEQE 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  819 PKPLPINVQGA-RILVVDDN----EVNRRILTEQlslwGFDGVAAEGGGTGLAILEAaadlGVTVDAVVLDYHMP-DMNG 892
Cdd:PRK13557  405 PKARAIDRGGTeTILIVDDRpdvaELARMILEDF----GYRTLVASNGREALEILDS----HPEVDLLFTDLIMPgGMNG 476
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 636783241  893 ADVARRLRAdpRFVELPIIFLT-----SM---DISGTekEFAALNghahlmKPAR 939
Cdd:PRK13557  477 VMLAREARR--RQPKIKVLLTTgyaeaSIertDAGGS--EFDILN------KPYR 521
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
702-809 4.01e-16

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: 75.32  E-value: 4.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  702 RQIVTNLVGNAVKFT-ERGHVFVDVGFEtaaggEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAI 780
Cdd:cd16952     2 RSAFSNLVSNAVKYTpPSDTITVRWSQE-----ESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAI 76
                          90       100
                  ....*....|....*....|....*....
gi 636783241  781 TAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16952    77 VKHVMSRHDARLLIASELGKGSRFTCLFP 105
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
827-969 4.11e-16

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: 77.69  E-value: 4.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  827 QGARILVVDDNEVNRRILTEQLSLWGFDGVAAegGGTGLAILEAAADLGVtvDAVVLDYHMPDMNGADVARRLRADPRfv 906
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAE--AADGEDAVELVRELKP--DLVIVDIDMPDRDGLEAARQISEERP-- 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636783241  907 eLPIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVRASRVKQASEAEIARLQT 969
Cdd:COG3707    76 -APVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRALRRELAKLRE 137
PRK10604 PRK10604
sensor protein RstB; Provisional
591-819 7.02e-16

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 81.57  E-value: 7.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  591 NMSHEIRTPMNGV---LGMAELLAKtnlDTRQKTFVDIivksgNALLTIINDILDFSKIDAGQMKLRKAAFD----ITEA 663
Cdd:PRK10604  218 GIAHELRTPLVRLryrLEMSDNLSA---AESQALNRDI-----GQLEALIEELLTYARLDRPQNELHLSEPDlpawLSTH 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  664 VEDVATLlsshAAEKNIELlVRAAPDLPAAVigDAGRFRQIVTNLVGNAVKFTErGHVFVDVGFETAaggeiMASIRIED 743
Cdd:PRK10604  290 LADIQAV----TPEKTVRL-DTPHQGDYGAL--DMRLMERVLDNLLNNALRYAH-SRVRVSLLLDGN-----QACLIVED 356
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241  744 TGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPFAVAAARLEP 819
Cdd:PRK10604  357 DGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPVWHNLPQFTS 432
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
989-1113 9.01e-16

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 75.01  E-value: 9.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  989 DVLVAEDNEVNQIVFTQILQGTGLSFLV--VDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPI 1066
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERLPGFEVVgvASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRAR----GPDVDV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 636783241 1067 IGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTSEQQ 1113
Cdd:COG4565    81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLL 127
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
990-1105 1.80e-15

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: 73.70  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQgTGLSFLVV---DNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREkgqgHRVPI 1066
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLE-SEPDIEVVgeaADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRY----PDLKV 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 636783241 1067 IGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQ 1105
Cdd:cd17535    76 IVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRA 114
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
830-937 2.66e-15

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: 72.96  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRFVELP 909
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKE-----KPDLILMDIQLPGMDGLEATRLLKEDPATRDIP 75
                          90       100
                  ....*....|....*....|....*...
gi 636783241  910 IIFLTSMDISGTEKEFAALNGHAHLMKP 937
Cdd:cd17548    76 VIALTAYAMKGDREKILEAGCDGYISKP 103
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
825-970 3.03e-15

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: 74.95  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  825 NVQGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRAdpR 904
Cdd:COG4567     1 SAEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAP-----PDYAVLDLRLGDGSGLDLIEALRE--R 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241  905 FVELPIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVRASRVKQASEAEIARLQTE 970
Cdd:COG4567    74 DPDARIVVLTGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENPMSLDRLEWE 139
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
829-947 3.48e-15

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: 72.64  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRAdpRFVEL 908
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESED-----PDLVILDIKMPGMDGLETLRKIRE--KKPDL 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 636783241  909 PIIFLTSmdISGTEKEFAALNGHAHLMKPARANVLRNTV 947
Cdd:cd17554    74 PVIICTA--YSEYKSDFSSWAADAYVVKSSDLTELKETI 110
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
832-917 3.73e-15

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 72.06  E-value: 3.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  832 LVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAaadlgVTVDAVVLDYHMPDMNGADVARRLRADPRfvELPII 911
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELARE-----EQPDLIILDVMLPGMDGFEVCRRLREKGS--DIPII 73

                  ....*.
gi 636783241  912 FLTSMD 917
Cdd:cd17574    74 MLTAKD 79
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
697-809 4.68e-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 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: 72.11  E-value: 4.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  697 DAGRFRQIVTNLVGNAVKFTERGHVFVDVGFETAAGGEIMasirIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGL 776
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQEVRLD----VEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241  777 GLAITAGLVDLFGGYLNVD-SEWGkGSVFTVNLP 809
Cdd:cd16946    77 GLAICHNIALAHGGTISAEhSPLG-GLRLVLTLP 109
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
990-1093 5.74e-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: 71.73  E-value: 5.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGlSFLVVD---NGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPI 1066
Cdd:COG4753     2 VLIVDDEPLIREGLKRILEWEA-GFEVVGeaeNGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL----DPDTKI 76
                          90       100
                  ....*....|....*....|....*..
gi 636783241 1067 IGVTAHALESDRELCLDAGMDDYMSKP 1093
Cdd:COG4753    77 IILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
831-947 7.85e-15

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: 71.72  E-value: 7.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPRFVELPI 910
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFR-----PDVILSDIGMPGMDGYELARRLRELPWLANTPA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 636783241  911 IFLTSmdiSGTE--KEFAALNG-HAHLMKPARANVLRNTV 947
Cdd:cd17580    76 IALTG---YGQPedRERALEAGfDAHLVKPVDPDELIELI 112
pleD PRK09581
response regulator PleD; Reviewed
829-1099 9.40e-15

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 78.02  E-value: 9.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPRFVEL 908
Cdd:PRK09581    3 ARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQ-----PDIILLDVMMPGMDGFEVCRRLKSDPATTHI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  909 PIIFLTSMDisGTEKEFAALNGHAH--LMKPARANVLrntVVEVVRASRVKQASEAEIARLQT--EAAVPAPALVPQKRA 984
Cdd:PRK09581   78 PVVMVTALD--DPEDRVRGLEAGADdfLTKPINDVAL---FARVKSLTRLKMVIDELRLRASTnaEIGVTALMIMAYANK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  985 AEFVDVLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWErYTPRIIMMDVSMPVMNGHQATQTIREREKGQGhrV 1064
Cdd:PRK09581  153 DEDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAE-TNYDLVIVSANFENYDPLRLCSQLRSKERTRY--V 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 636783241 1065 PIIGVTAhalESDRELC---LDAGMDDYMSKPISP-ELL 1099
Cdd:PRK09581  230 PILLLVD---EDDDPRLvkaLELGVNDYLMRPIDKnELL 265
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
989-1105 1.31e-14

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: 71.68  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  989 DVLVAEDNEVNQIVFTQILQGTGLS--FLVVDNGEEAVA-------AWERYTPRIIMMDVSMPVMNGHQATQTIREREKG 1059
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPneLHVVRDGEEALDflrgegeYADAPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 636783241 1060 QghRVPIIGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQ 1105
Cdd:cd17557    81 R--RIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
831-947 1.31e-14

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: 71.03  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPrfVELPI 910
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-----RPDLILLDINMPGMDGLELLKRIRRRD--PTTPV 73
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 636783241   911 IFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTV 947
Cdd:pfam00072   74 IILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
988-1103 1.34e-14

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: 71.28  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  988 VDVLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTP--RIIMMDVSMPVMNGHQATQTIREReKGQGHRVP 1065
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHsfQLVLLDLCMPEMDGFEVALRIRKL-FGRRERPL 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241 1066 IIGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKI 1103
Cdd:cd19933    80 IVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
990-1094 1.38e-14

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: 70.62  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQGhrVPIIGV 1069
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRH--IPVIFL 78
                          90       100
                  ....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPI 1094
Cdd:cd19920    79 TALTDTEDKVKGFELGAVDYITKPF 103
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
703-809 1.67e-14

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: 70.68  E-value: 1.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  703 QIVTNLVGNAVKFT--ERGHVFVdvgfeTAAGGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAI 780
Cdd:cd16953     3 QVLRNLIGNAISFSppDTGRITV-----SAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSI 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 636783241  781 TAGLVDLFGGYLNV----DSEWGKGSVFTVNLP 809
Cdd:cd16953    78 SRQIIEAHGGISVAenhnQPGQVIGARFTVQLP 110
glnL PRK11073
nitrogen regulation protein NR(II);
580-809 2.52e-14

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 75.89  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  580 AADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILdfskidAGQMKLRKAAFD 659
Cdd:PRK11073  125 AQQVAARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLL------GPQRPGTHVTES 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  660 ITEAVEDVATLLSSHAAEkNIELLVRAAPDLPAAVIgDAGRFRQIVTNLVGNAVKFTERGHVFVDV----GFETAAGGE- 734
Cdd:PRK11073  199 IHKVAERVVQLVSLELPD-NVRLIRDYDPSLPELAH-DPDQIEQVLLNIVRNALQALGPEGGTITLrtrtAFQLTLHGEr 276
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636783241  735 --IMASIRIEDTGIGIPPEKLESVFdkFSQVDAsstrRHEGTGLGLAITAGLVDLFGGYLNVDSeWGKGSVFTVNLP 809
Cdd:PRK11073  277 yrLAARIDIEDNGPGIPPHLQDTLF--YPMVSG----REGGTGLGLSIARNLIDQHSGKIEFTS-WPGHTEFSVYLP 346
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
991-1104 5.64e-14

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: 69.26  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  991 LVAEDNEVNQIVfTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqgHRVPIIGVT 1070
Cdd:cd17623     3 LIDDDRELTELL-TEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT-----SQVPVLMLT 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241 1071 AHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17623    77 ARGDDIDRILGLELGADDYLPKPFNPRELVARIR 110
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
589-782 5.66e-14

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 75.74  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  589 LANMSHEIRTPMNGvLGMAELLAK---------TNLDTR-QKtfvdiivksgnaLLTIINDILDFSKIdagQMK--LRKA 656
Cdd:PRK09470  247 LSDISHELRTPLTR-LQLATALLRrrqgeskelERIETEaQR------------LDSMINDLLVLSRN---QQKnhLERE 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  657 AFDITEAVEDVATLLSSHAAEKNIELLVRAAPDlPAAVIGDAGRFRQIVTNLVGNAVKFterGHVFVDVGFeTAAGGEIM 736
Cdd:PRK09470  311 TFKANSLWSEVLEDAKFEAEQMGKSLTVSAPPG-PWPINGNPNALASALENIVRNALRY---SHTKIEVAF-SVDKDGLT 385
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 636783241  737 asIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITA 782
Cdd:PRK09470  386 --ITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVE 429
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
830-937 8.33e-14

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: 68.26  E-value: 8.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQL-SLWGFDGVA-AEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRAdpRFVE 907
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILeWEAGFEVVGeAENGEEALELLEEH-----KPDLVITDINMPGMDGLELLEAIRE--LDPD 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 636783241  908 LPIIFLTSMDISGTEKEFAALNGHAHLMKP 937
Cdd:COG4753    74 TKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
830-937 8.85e-14

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 68.73  E-value: 8.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILteQLSL---WGFDGVAAEGGGTGLAIleAAADlgvTVDAVVLDYHMPDMNGADVARRLRADPRFV 906
Cdd:cd17552     3 RILVIDDEEDIREVV--QACLeklAGWEVLTASSGQEGLEK--AATE---QPDAILLDVMMPDMDGLATLKKLQANPETQ 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 636783241  907 ELPIIFLTSMDISGTEKEFAALNGHAHLMKP 937
Cdd:cd17552    76 SIPVILLTAKAQPSDRQRFASLGVAGVIAKP 106
orf27 CHL00148
Ycf27; Reviewed
991-1120 1.88e-13

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 71.29  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  991 LVAEDNEVNQIVFTQiLQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGVT 1070
Cdd:CHL00148   11 VVDDEAYIRKILETR-LSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESD-----VPIIMLT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 636783241 1071 AHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTSEQQPERTTAP 1120
Cdd:CHL00148   85 ALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNKKSFSSKIP 134
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
688-808 2.16e-13

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


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 67.92  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  688 PDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVfvdVGFeTAAGGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASS 767
Cdd:cd16947     8 PDRPIYANANTEALQRILKNLISNAIKYGSDGKF---LGM-TLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 636783241  768 TRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNL 808
Cdd:cd16947    84 NSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
831-917 2.23e-13

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: 67.40  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADLGV----TVDAVVLDYHMPDMNGADVARRLRADPRFV 906
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGNdlskELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90
                  ....*....|.
gi 636783241  907 ELPIIFLTSMD 917
Cdd:cd19924    81 NIPVILNSSLS 91
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
991-1099 2.97e-13

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: 67.30  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  991 LVAEDNE--VNQIVFTqiLQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQGhrVPIIG 1068
Cdd:cd19937     1 LVVDDEEdiVELLKYN--LEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSS--IPIIM 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 636783241 1069 VTAHALESDRELCLDAGMDDYMSKPISP-ELL 1099
Cdd:cd19937    77 LTAKGEEFDKVLGLELGADDYITKPFSPrELL 108
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
990-1107 3.36e-13

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: 67.01  E-value: 3.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVfTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGV 1069
Cdd:cd19939     3 LIVEDELELARLT-RDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSH-----VPILML 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWL 1107
Cdd:cd19939    77 TARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
990-1099 3.64e-13

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: 67.08  E-value: 3.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVV-DNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQGhrVPIIG 1068
Cdd:cd17551     3 ILIVDDNPTNLLLLEALLRSAGYLEVVSfTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLED--VPIVM 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 636783241 1069 VTAHALESDRELCLDAGMDDYMSKPISP-ELL 1099
Cdd:cd17551    81 ITADTDREVRLRALEAGATDFLTKPFDPvELL 112
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
830-916 4.32e-13

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: 66.98  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVA-AEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPRFVEL 908
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKAGG-----FDFVITDWNMPNMDGLELLKTIRADGALSHL 76

                  ....*...
gi 636783241  909 PIIFLTSM 916
Cdd:cd19923    77 PVLMVTAE 84
envZ PRK09467
osmolarity sensor protein; Provisional
582-790 4.47e-13

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 72.64  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  582 DRAKseFLANMSHEIRTPMNGVLGMAELLAKTnlDTRQKtfvDIIVKSGNALLTIINDILDFSKIDAgQMKLRKAafDIT 661
Cdd:PRK09467  228 DRTL--LMAGVSHDLRTPLTRIRLATEMMSEE--DGYLA---ESINKDIEECNAIIEQFIDYLRTGQ-EMPMEMA--DLN 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  662 EAVEDVAtlLSSHAAEKNIELlvrAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTeRGHVFVDVGFETAAggeimASIRI 741
Cdd:PRK09467  298 ALLGEVI--AAESGYEREIET---ALQPGPIEVPMNPIAIKRALANLVVNAARYG-NGWIKVSSGTEGKR-----AWFQV 366
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 636783241  742 EDTGIGIPPEKLESVFDKFSQVDasSTRRHEGTGLGLAITAGLVDLFGG 790
Cdd:PRK09467  367 EDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNG 413
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
181-311 4.98e-13

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 71.80  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  181 NELDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLAlEGGTSKEIESL 260
Cdd:COG3852     4 ESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALA-EGQPVTEREVT 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636783241  261 LPSKDGHIYSVLSRVNRVVTADGRPYVVGSFSDISPLKEREKALIEAQKHK 311
Cdd:COG3852    83 LRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLA 133
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
990-1107 5.27e-13

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: 66.64  E-value: 5.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRerekGQGHRVPIIGV 1069
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLR----AAGNDLPILVL 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWL 1107
Cdd:cd17627    77 TARDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
830-915 9.27e-13

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: 66.00  E-value: 9.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADLGVtvdaVVLDYHMPDMNGADVARRLRADPRFVELP 909
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKL----VITDYNMPEMDGFELVREIRKKYSRDQLA 77

                  ....*.
gi 636783241  910 IIFLTS 915
Cdd:cd17544    78 IIGISA 83
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
991-1099 9.89e-13

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 65.71  E-value: 9.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  991 LVAEDN-EVNQIVfTQILQGTGLSFLVVDNGEEAV--AAWERYTprIIMMDVSMPVMNGHQATQTIRErekgQGHRVPII 1067
Cdd:cd17625     1 LVVEDEkDLSEAI-TKHLKKEGYTVDVCFDGEEGLeyALSGIYD--LIILDIMLPGMDGLEVLKSLRE----EGIETPVL 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 636783241 1068 GVTAHALESDRELCLDAGMDDYMSKPIS-PELL 1099
Cdd:cd17625    74 LLTALDAVEDRVKGLDLGADDYLPKPFSlAELL 106
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
990-1104 1.11e-12

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: 65.73  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQghRVPIIGV 1069
Cdd:cd17618     3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTR--DIPIIML 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17618    81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
707-809 1.45e-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: 65.04  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  707 NLVGNAVKFTeRGHVFVDVGFEtaaGGEImaSIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVD 786
Cdd:cd16949     7 NVLRNALRYS-PSKILLDISQD---GDQW--TITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIE 80
                          90       100
                  ....*....|....*....|...
gi 636783241  787 LFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16949    81 QHGGKIKASNRKPGGLRVRIWLP 103
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
584-852 1.46e-12

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 72.27  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  584 AKSEFLANMSHEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIINDILDFSKIDAGQMKLRKAAFDITEA 663
Cdd:PRK10618  449 ARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDL 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  664 VEDVATLLSSHAAEKNIELLVRAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVFVDVGFETAAGGEImaSIRIED 743
Cdd:PRK10618  529 IDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDESSPDRL--TIRILD 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  744 TGIGIPPEKLESVFDKFSQvDASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLPfavaaarLEPKPLP 823
Cdd:PRK10618  607 TGAGVSIKELDNLHFPFLN-QTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLK-------MLAADPE 678
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 636783241  824 INVQGARILvvDD---------NEVnRRILTEQLSLWG 852
Cdd:PRK10618  679 VEEEEEKLL--DGvtvllditsEEV-RKIVTRQLENWG 713
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
703-809 1.47e-12

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 65.11  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  703 QIVTNLVGNAVKFTERGH------VFVDVGFETAAGGEIMA-SIRIEDTGIGIPPEKLESVFDKFSqvdassTRRHEGTG 775
Cdd:cd16918     3 QVFLNLVRNAAQALAGSGgeiilrTRTQRQVTLGHPRHRLAlRVSVIDNGPGIPPDLQDTIFYPMV------SGRENGTG 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241  776 LGLAITAGLVDLFGGYLNVDSEWGKgSVFTVNLP 809
Cdd:cd16918    77 LGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
703-809 1.64e-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: 64.73  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  703 QIVTNLVGNAVKFTERGHVFVD---VGFETAAGGEImaSIRIEDTGIGIPPEKLESVFDKFSqvdassTRRHEGTGLGLA 779
Cdd:cd16920     3 QVLINLVRNGIEAMSEGGCERReltIRTSPADDRAV--TISVKDTGPGIAEEVAGQLFDPFY------TTKSEGLGMGLS 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 636783241  780 ITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16920    75 ICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
990-1104 1.83e-12

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 64.99  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGlsFLVVD---NGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGqghrVPI 1066
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAG--YEVVGeaaNGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPN----AKV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 636783241 1067 IGVTA---HALESDrelCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17542    77 IMCSAmgqEEMVKE---AIKAGAKDFIVKPFQPERVLEAVE 114
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
702-809 2.07e-12

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 64.39  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  702 RQIVTNLVGNAVKFterGHVFVDVGFETAAGGeimASIRIEDTGIGIPPEKLESVFDKFSQVDASstRRHEGTGLGLAIT 781
Cdd:cd16950     2 KRVLSNLVDNALRY---GGGWVEVSSDGEGNR---TRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIV 73
                          90       100
                  ....*....|....*....|....*...
gi 636783241  782 AGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16950    74 QRISDAHGGSLTLANRAGGGLCARIELP 101
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
990-1104 3.24e-12

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: 64.41  E-value: 3.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErEKGqghrVPIIGV 1069
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-ESG----VPIVML 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17626    78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
990-1104 3.61e-12

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 64.34  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGlSFLVVD---NGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqgHRVPI 1066
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDP-DIEVVGtarDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE-----RPTPV 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636783241 1067 IGVTAHAlESDREL---CLDAGMDDYMSKP----------ISPELLeEKIR 1104
Cdd:cd17541    77 VMVSSLT-EEGAEItleALELGAVDFIAKPsggisldleeIAEELI-EKIK 125
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
990-1123 4.17e-12

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 67.14  E-value: 4.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVfTQILQGTGLSFLVVDNGEEAVAAWERyTPRIIMMDVSMPVMNGHQATQTIRerekgQGHRVPIIGV 1069
Cdd:PRK10955    5 LLVDDDRELTSLL-KELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELR-----QTHQTPVIML 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTS----EQQPERTTAPRIF 1123
Cdd:PRK10955   78 TARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRShwseQQQNNDNGSPTLE 135
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
990-1107 6.60e-12

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: 63.55  E-value: 6.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGqghrvPIIGV 1069
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG-----PILLL 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWL 1107
Cdd:cd17622    78 TALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
830-917 8.35e-12

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: 63.14  E-value: 8.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAaadlgVTVDAVVLDYHMPDMNGADVARRLRADPrfVELP 909
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAARE-----FRPDAVVLDIMLPDMDGLEVLRRLRADG--PDVP 73

                  ....*...
gi 636783241  910 IIFLTSMD 917
Cdd:cd17615    74 VLFLTAKD 81
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
990-1107 9.29e-12

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 63.11  E-value: 9.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQGhrVPIIGV 1069
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKD--IPVILL 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWL 1107
Cdd:cd17598    79 TTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
PRK13560 PRK13560
hypothetical protein; Provisional
182-342 9.82e-12

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 69.32  E-value: 9.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  182 ELDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEmFGPDGGEAIYQE-NLLALEGGTSKEIESL 260
Cdd:PRK13560  202 ALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHD-FAPAQPADDYQEaDAAKFDADGSQIIEAE 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  261 LPSKDGHIYSVLSRVNRvVTADGRPY----VVGSFSDISPLKEREKALIEaqkhKELLHRdieNILRSLPVGVLILDNDH 336
Cdd:PRK13560  281 FQNKDGRTRPVDVIFNH-AEFDDKENhcagLVGAITDISGRRAAERELLE----KEDMLR---AIIEAAPIAAIGLDADG 352

                  ....*.
gi 636783241  337 RILYVN 342
Cdd:PRK13560  353 NICFVN 358
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
701-809 1.09e-11

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: 62.69  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  701 FRQIVTNlvgnAVKFT-ERGHVFVDVgfETAAGGEIMasiRIEDTGIGIPPEKLESVFDKFSqvdASSTRRH--EGTGLG 777
Cdd:cd16948    10 IGQIVSN----ALKYSkQGGKIEIYS--ETNEQGVVL---SIKDFGIGIPEEDLPRVFDKGF---TGENGRNfqESTGMG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 636783241  778 LAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16948    78 LYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
555-792 1.15e-11

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 67.69  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  555 VALFTDVTELKSREEELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAELLAKTnldtrQKTFVDIIVKSGNALL 634
Cdd:PRK10755  107 IAIHSSTLEIEAVTSALNQLVSRLTSTLDQERLFTADVAHELRTPLAGIRLHLELLEKQ-----HHIDVAPLIARLDQMM 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  635 TIINDILDFSKidAGQmKLRKAAFDITEAVEDVAT----LLSSHAAEKNIELLVRAAPDlPAAVIGDAGRFRQIVTNLVG 710
Cdd:PRK10755  182 HTVEQLLQLAR--AGQ-SFSSGHYQTVKLLEDVILpsqdELSEMLEQRQQTLLLPESAA-DITVQGDATLLRLLLRNLVE 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  711 NAVKFTERGHVfVDVGFETAAGGEIMAsirIEDTGIGIPPEKLESVFDKFSQVDasstRRHEGTGLGLAITAGLVDLFGG 790
Cdd:PRK10755  258 NAHRYSPEGST-ITIKLSQEDGGAVLA---VEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHG 329

                  ..
gi 636783241  791 YL 792
Cdd:PRK10755  330 QF 331
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
990-1115 1.16e-11

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


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 65.81  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQghRVPIIGV 1069
Cdd:TIGR02154    5 ILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETR--AIPIIML 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 636783241  1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR-QWLGTSEQQPE 1115
Cdd:TIGR02154   83 TARGEEEDRVRGLETGADDYITKPFSPRELLARIKaVLRRIRPQLSD 129
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
705-809 1.21e-11

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 62.45  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  705 VTNLVGNAVKFTERGhvfVDVGFeTAAGGEimASIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGL 784
Cdd:cd16939     5 LDNLLRNALRYAHRT---VRIAL-LVSGGR--LTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRV 78
                          90       100
                  ....*....|....*....|....*.
gi 636783241  785 VDLFGGYLNV-DSEWGkGSVFTVNLP 809
Cdd:cd16939    79 ALWHGGHVECdDSELG-GACFRLTWP 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
182-304 1.67e-11

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 62.69  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   182 ELDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAI--YQENLLALEGGTsKEIES 259
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVreRIERRLEGEPEP-VSEER 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 636783241   260 LLPSKDGHIYSVLSRVNRVVTADGRPYVVGSFSDISPLKEREKAL 304
Cdd:TIGR00229   80 RVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
831-917 1.79e-11

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: 62.02  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILeaaadLGVTVDAVVLDYHMPDMNGADVARRLRADPRfvELPI 910
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVI-----SGNRPDAVVLDVMMPRLDGLEVCRRLRAAGN--DLPI 73

                  ....*..
gi 636783241  911 IFLTSMD 917
Cdd:cd17627    74 LVLTARD 80
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
990-1093 2.00e-11

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: 61.45  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGV 1069
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSN-----VPVIMV 75
                          90       100
                  ....*....|....*....|....
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKP 1093
Cdd:cd17621    76 TAKDSEIDKVVGLELGADDYVTKP 99
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
830-968 2.01e-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: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGgTGLAILEAAADLgvTVDAVVLDYHMPDMNGADVARRLRADPRFVelP 909
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDLEVVGEAS-NGEEALELLEEH--KPDLVFLDIQMPGLDGFELARQLRELDPPP--P 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636783241  910 IIFLTSMDisgtekEFAA----LNGHAHLMKPARANVLRNTVVEVVRASRVKQASEAEIARLQ 968
Cdd:COG3279    78 IIFTTAYD------EYALeafeVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKD 134
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
702-809 2.71e-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: 61.25  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  702 RQIVTNLVGNAVKFT-ERGHVFVDVGFEtaaggEIMASIRIEDTGIGIPPEKLESVFDKFSQVDASstRRHEGTGLGLAI 780
Cdd:cd16923     2 QRVFSNLLSNAIKYSpENTRIYITSFLT-----DDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSI 74
                          90       100
                  ....*....|....*....|....*....
gi 636783241  781 TAGLVDLFGGYLNVDSEwGKGSVFTVNLP 809
Cdd:cd16923    75 AKAIIELHGGSASAEYD-DNHDLFKVRLP 102
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
829-914 4.60e-11

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: 61.16  E-value: 4.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRFVEL 908
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSK-----KFDLIITDQNMPNMDGIELIKELRKLPAYKFT 75

                  ....*.
gi 636783241  909 PIIFLT 914
Cdd:cd17562    76 PILMLT 81
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
704-809 4.61e-11

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: 60.76  E-value: 4.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  704 IVTNLVGNAVKFTER---GHVFVDVgFETAAGGEIMasIRIEDTGIGIPPEKLESVFDKfsqvdASSTRRHEGTGLGLAI 780
Cdd:cd16915     4 IVGNLIDNALDALAAtgaPNKQVEV-FLRDEGDDLV--IEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLAL 75
                          90       100
                  ....*....|....*....|....*....
gi 636783241  781 TAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16915    76 VRQSVERLGGSITVESEPGGGTTFSIRIP 104
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
831-915 4.77e-11

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 60.78  E-value: 4.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAileAAADLgvTVDAVVLDYHMPDMNGADVARRLRADPrfvELPI 910
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLA---ALLEG--SPDLVVLDVMLPKMNGLDVLKELRKTS---QVPV 72

                  ....*
gi 636783241  911 IFLTS 915
Cdd:cd17623    73 LMLTA 77
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
990-1099 6.68e-11

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: 60.48  E-value: 6.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREkgqghRVPIIGV 1069
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS-----EVGIILV 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISP-ELL 1099
Cdd:cd17619    78 TGRDDEVDRIVGLEIGADDYVTKPFNPrELL 108
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
990-1093 7.36e-11

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: 59.87  E-value: 7.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGV 1069
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA-----VPVIVL 75
                          90       100
                  ....*....|....*....|....
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKP 1093
Cdd:cd17620    76 SARDEESDKIAALDAGADDYLTKP 99
PAS COG2202
PAS domain [Signal transduction mechanisms];
306-571 8.95e-11

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 63.89  E-value: 8.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  306 EAQKHKELLHRDIENILRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDpFDGRPFIDVIrrnyelgrydGTQTPEEIY 385
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEE-LLGKTLRDLL----------PPEDDDEFL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  386 DFRKHLFETEEPEPIELGW--AGGKSVIFDSR----RISNDRILLTYA---DITAVREREKEIHETRAALERLGEmmrda 456
Cdd:COG2202    70 ELLRAALAGGGVWRGELRNrrKDGSLFWVELSispvRDEDGEITGFVGiarDITERKRAEEALRESEERLRLLVE----- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  457 thAMPQGLAIV-QDGIIRMSNEALSDILQIPAtylergEGWIGMFEYCAARGDFHDAAAETLQGWRDNIAARLPISTAFH 535
Cdd:COG2202   145 --NAPDGIFVLdLDGRILYVNPAAEELLGYSP------EELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLK 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 636783241  536 VGGERWVNMDATVSR------GQHWVALFTDVTELKSREEEL 571
Cdd:COG2202   217 DGDGRWVWVEASAVPlrdggeVIGVLGIVRDITERKRAEEAL 258
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
990-1108 9.11e-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: 60.26  E-value: 9.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVfTQI-LQ-GTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQghRVPII 1067
Cdd:cd17552     4 ILVIDDEEDIREV-VQAcLEkLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQ--SIPVI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 636783241 1068 GVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLG 1108
Cdd:cd17552    81 LLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
990-1104 9.22e-11

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 59.99  E-value: 9.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErekgQGHRVPIIGV 1069
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRS----EGRATPVLIL 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd19934    77 TARDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
703-808 1.07e-10

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: 59.39  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  703 QIVTNLVGNAV-KFTERGHVFVDVGFETAAGgeiMASIRIEDTGIGIPPEKLESVFDKFSqvdasSTRR-HEGTGLGLAI 780
Cdd:cd16976     3 QVLMNLLQNALdAMGKVENPRIRIAARRLGG---RLVLVVRDNGPGIAEEHLSRVFDPFF-----TTKPvGKGTGLGLSI 74
                          90       100
                  ....*....|....*....|....*...
gi 636783241  781 TAGLVDLFGGYLNVDSEWGKGSVFTVNL 808
Cdd:cd16976    75 SYGIVEEHGGRLSVANEEGAGARFTFDL 102
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
990-1105 1.16e-10

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: 60.04  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVV---DNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPI 1066
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELGFEVVgeaENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL----YPDIKI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 636783241 1067 IGVTAHaleSDREL---CLDAGMDDYMSKPISPELLEEKIRQ 1105
Cdd:cd17536    77 IILSGY---DDFEYaqkAIRLGVVDYLLKPVDEEELEEALEK 115
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
829-914 1.26e-10

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 59.96  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRFVEL 908
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEP-----RPDLILLDWMLPGGSGIQFIRRLKRDEMTRDI 75

                  ....*.
gi 636783241  909 PIIFLT 914
Cdd:cd17618    76 PIIMLT 81
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
989-1093 1.35e-10

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: 59.59  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  989 DVLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghRVPIIG 1068
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHP----DLPVII 77
                          90       100
                  ....*....|....*....|....*...
gi 636783241 1069 VTAHaleSDRELCLDA---GMDDYMSKP 1093
Cdd:cd19919    78 MTAH---SDLDSAVSAyqgGAFEYLPKP 102
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
990-1099 1.60e-10

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: 59.36  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNE--VNQIVFTqiLQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqgHRVPII 1067
Cdd:cd17614     1 ILVVDDEKpiSDILKFN--LTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT-----SNVPII 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 636783241 1068 GVTAHALESDRELCLDAGMDDYMSKPISP-ELL 1099
Cdd:cd17614    74 MLTAKDSEVDKVLGLELGADDYVTKPFSNrELL 106
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
829-921 2.07e-10

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 59.14  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAaadlgVTVDAVVLDYHMPDMNGADVARRLRAdpRFVEL 908
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRS-----EQPDLVLCDLRMPEMDGLEVLKQITK--ESPDT 73
                          90
                  ....*....|...
gi 636783241  909 PIIFltsmdISGT 921
Cdd:cd17555    74 PVIV-----VSGA 81
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
831-952 3.29e-10

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: 58.68  E-value: 3.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNR----RILTEQLslwGFDGVA-AEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRAdpRF 905
Cdd:cd17535     1 VLIVDDHPLVReglrRLLESEP---DIEVVGeAADGEEALALLRELR-----PDVVLMDLSMPGMDGIEALRRLRR--RY 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636783241  906 VELPIIFLTSMDisgtEKEF--AALNGHAH--LMKPARANVLRNTVVEVVR 952
Cdd:cd17535    71 PDLKVIVLTAHD----DPEYvlRALKAGAAgyLLKDSSPEELIEAIRAVAA 117
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
990-1104 3.40e-10

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 58.52  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErekgQGHRVPIIGV 1069
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA----DGPDVPVLFL 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17615    78 TAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
832-914 3.73e-10

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: 58.44  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  832 LVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEaaadlGVTVDAVVLDYHMPDMNGADVARRLRADPRFVELPII 911
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAK-----DEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPII 75

                  ...
gi 636783241  912 FLT 914
Cdd:cd19937    76 MLT 78
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
990-1103 4.17e-10

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: 58.06  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGV 1069
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-----VPIIFI 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKI 1103
Cdd:cd18159    76 SSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKI 109
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
988-1105 4.54e-10

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: 58.12  E-value: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  988 VDVLVAEDNEVNQIVFTQILQGTGlsFLVVDNGEEAVAAWERYTP---RIIMMDVSMPVMNGHQATQTIReREKGQGHrV 1064
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELG--FNNVEEAEDGVDALEKLKAggfDFVITDWNMPNMDGLELLKTIR-ADGALSH-L 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 636783241 1065 PIIGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQ 1105
Cdd:cd19923    77 PVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEK 117
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
988-1099 4.69e-10

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: 58.30  E-value: 4.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  988 VDVLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYtP--RIIMMDVSMPVMNGHQATQTIREREKGQghRVP 1065
Cdd:cd17544     1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQH-PdiKLVITDYNMPEMDGFELVREIRKKYSRD--QLA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 636783241 1066 IIGVTAHaleSDRELC---LDAGMDDYMSKPISPELL 1099
Cdd:cd17544    78 IIGISAS---GDNALSarfIKAGANDFLTKPFLPEEF 111
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
738-809 5.26e-10

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: 58.16  E-value: 5.26e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636783241  738 SIRIEDTGIGIPPEKLESVFDKFsqvdASSTRRHEGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16919    49 CLEVSDTGSGMPAEVLRRAFEPF----FTTKEVGKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
830-947 6.33e-10

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 58.20  E-value: 6.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGF--------DGVAAegggtgLAIL--EAAADLGVTVDAVVLDYHMPDMNGADVARRL 899
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVpnelhvvrDGEEA------LDFLrgEGEYADAPRPDLILLDLNMPRMDGFEVLREI 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636783241  900 RADPRFVELPIIFLTSmdiSGTEKE-FAALNGHA--HLMKPARANVLRNTV 947
Cdd:cd17557    75 KADPDLRRIPVVVLTT---SDAEEDiERAYELGAnsYIVKPVDFEEFVEAI 122
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
990-1093 7.37e-10

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: 57.06  E-value: 7.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAV--AAWERYTprIIMMDVSMPVMNGHQATQTIRErekgQGHRVPII 1067
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLhlALTNEYD--LIILDVMLPGLDGLEVLRRLRA----AGKQTPVL 74
                          90       100
                  ....*....|....*....|....*.
gi 636783241 1068 GVTAHALESDRELCLDAGMDDYMSKP 1093
Cdd:cd19935    75 MLTARDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
990-1096 1.13e-09

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 57.00  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRerekgQGHRVPIIGV 1069
Cdd:cd19938     2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR-----RFSDVPIIMV 76
                          90       100
                  ....*....|....*....|....*..
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISP 1096
Cdd:cd19938    77 TARVEEIDRLLGLELGADDYICKPYSP 103
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
990-1104 1.25e-09

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 56.72  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRerekGQGHRVPIIGV 1069
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWR----RQGQSLPVLIL 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17624    77 TARDGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1019-1096 1.33e-09

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 59.70  E-value: 1.33e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636783241 1019 NGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRerekgQGHRVPIIGVTAHALESDRELCLDAGMDDYMSKPISP 1096
Cdd:PRK10710   42 HGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR-----RFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSP 114
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
831-969 1.42e-09

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 58.96  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDgvaAEGGGTGLAILEAAADLGVTVdaVVLDYHMPDMNGADVARRLRAdpRFVELPI 910
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLR---VETFASAEAFLAALDPDRPGC--LLLDVRMPGMSGLELQEELAA--RGSPLPV 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636783241  911 IFLTsmdisgtekefaalnGHAH---------------LMKPARANVLRNTVVEVVRASRVKQASEAEIARLQT 969
Cdd:COG4566    75 IFLT---------------GHGDvpmavramkagavdfLEKPFDDQALLDAVRRALARDRARRAERARRAELRA 133
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
990-1093 1.98e-09

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: 55.85  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQghRVPIIGV 1069
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFD--TIPVIFL 78
                          90       100
                  ....*....|....*....|....
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKP 1093
Cdd:cd19927    79 TAKGMTSDRIKGYNAGCDGYLSKP 102
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
829-947 3.57e-09

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


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 55.49  E-value: 3.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFD--GVAAegggTGLAILEAAADLgvTVDAVVLDYHMP-DMNGADVARRLRadpRF 905
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLGYEvvGIAD----SGEEAIELAEEN--KPDLILMDINLKgDMDGIEAAREIR---EK 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 636783241  906 VELPIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTV 947
Cdd:cd17534    72 FDIPVIFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
990-1099 3.75e-09

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: 57.66  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLS-FLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqgHRVPIIG 1068
Cdd:COG3707     6 VLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEE-----RPAPVIL 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 636783241 1069 VTAHALESDRELCLDAGMDDYMSKPISPELL 1099
Cdd:COG3707    81 LTAYSDPELIERALEAGVSAYLVKPLDPEDL 111
PRK15479 PRK15479
transcriptional regulator TctD;
990-1115 4.20e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 58.19  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLsflVVDNGEEAVAA-----WERYTprIIMMDVSMPVMNGHQATQTIRERekgqGHRV 1064
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNGF---AVDCVFDGLAAdhllqSEMYA--LAVLDINMPGMDGLEVLQRLRKR----GQTL 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636783241 1065 PIIGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTSEQQPE 1115
Cdd:PRK15479   74 PVLLLTARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSAGQVQ 124
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
185-294 4.61e-09

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 55.12  E-value: 4.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   185 LLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLG-MTEHEMFGPDGGE--AIYQENLLALEGGTSKEIesLL 261
Cdd:pfam00989    2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGkSLLDLIPEEDDAEvaELLRQALLQGEESRGFEV--SF 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 636783241   262 PSKDGHIYSVLSRVNRVVTADGRP-YVVGSFSDI 294
Cdd:pfam00989   80 RVPDGRPRHVEVRASPVRDAGGEIlGFLGVLRDI 113
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
697-809 5.36e-09

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 54.85  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  697 DAGRFRQIVTNLVGNAVKFTE-----RGHVFVDVgfETAAGGEImaSIRIEDTGIGIPPEKLESVFDKFSqvdassTRRH 771
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRV--EADQDGRI--VLIVCDNGKGFPREMRHRATEPYV------TTRP 70
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241  772 EGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16944    71 KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
990-1104 6.29e-09

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: 54.90  E-value: 6.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPIIGV 1069
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQER----SLPTSVIVI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 636783241 1070 TAH-----ALESDRElcldaGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17572    77 TAHgsvdiAVEAMRL-----GAYDFLEKPFDADRLRVTVR 111
PRK10610 PRK10610
chemotaxis protein CheY;
830-943 7.21e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 55.37  E-value: 7.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVA-AEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPRFVEL 908
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFNNVEeAEDGVDALNKLQAGG-----FGFVISDWNMPNMDGLELLKTIRADGAMSAL 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 636783241  909 PIIFLTSMdiSGTEKEFAALNGHA--HLMKPARANVL 943
Cdd:PRK10610   82 PVLMVTAE--AKKENIIAAAQAGAsgYVVKPFTAATL 116
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
831-945 8.30e-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: 54.56  E-value: 8.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADlgvTVDAVVLDYHMPDMNGADVARRLRADPrfvELPI 910
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKD---EFDLVITDVHMPDMDGFEFLELIRLEM---DLPV 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241  911 IFLTSMDISGTEKEFAALNGHAHLMKPARANVLRN 945
Cdd:cd17584    75 IMMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKN 109
ompR PRK09468
osmolarity response regulator; Provisional
1007-1120 1.06e-08

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 57.29  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1007 LQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGhqatQTIREREKGQGHRVPIIGVTAHALESDRELCLDAGM 1086
Cdd:PRK09468   25 LTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDG----LSICRRLRSQNNPTPIIMLTAKGEEVDRIVGLEIGA 100
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241 1087 DDYMSKPISPELLEEKIRQWLgtSEQQPERTTAP 1120
Cdd:PRK09468  101 DDYLPKPFNPRELLARIRAVL--RRQAPELPGAP 132
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
990-1042 1.16e-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: 52.19  E-value: 1.16e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 636783241    990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMP 1042
Cdd:smart00448    3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
831-937 1.26e-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: 53.50  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADlgvtVDAVVLDYHMPD-MNGADVARRLRadPRFVELP 909
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPD----IDLLVTDVIMPGgMNGSQLAEEAR--RRRPDLK 74
                          90       100
                  ....*....|....*....|....*...
gi 636783241  910 IIFLTSMDISGTEKEFAAlNGHAHLMKP 937
Cdd:cd18161    75 VLLTSGYAENAIEGGDLA-PGVDVLSKP 101
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
555-810 1.29e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 58.77  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  555 VALFTDVTELKSREEELRQLLSRAEAAdRAKSeflanmsHEIRTPMNGVLGMAELLAKTNLDtrqktfvDIIVKSGNALL 634
Cdd:PRK11086  317 IATFRDKTEVRQLAQRLDGMVNYADAL-RAQS-------HEFMNKLHVILGLLHLKSYDQLE-------DYILKTANNYQ 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  635 TIINDILDFSK--IDAGqmklrkaaFditeavedvatLLS--SHAAEKNIELLVRAAPDLPAAviGDAGRFRQIVT---N 707
Cdd:PRK11086  382 EEIGSLLGKIKspVIAG--------F-----------LLGkiSRARELGITLIISEDSQLPDS--GDEDQVHELITilgN 440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  708 LVGN---AVKFTERGHVFVDVGFetaagGEIMASIRIEDTGIGIPPEKLESVFDK-FSQvdasstrRHEGTGLGLAITAG 783
Cdd:PRK11086  441 LIENaleAVGGEEGGEISVSLHY-----RNGWLHCEVSDDGPGIAPDEIDAIFDKgYST-------KGSNRGVGLYLVKQ 508
                         250       260
                  ....*....|....*....|....*..
gi 636783241  784 LVDLFGGYLNVDSEWGKGSVFTVNLPF 810
Cdd:PRK11086  509 SVENLGGSIAVESEPGVGTQFFVQIPW 535
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
990-1107 1.37e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 58.71  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghRVPIIGV 1069
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHET----RTPVILM 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWL 1107
Cdd:PRK11361   83 TAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
172-304 1.52e-08

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: 58.45  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  172 SETAWHESVNELdllRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALEG 251
Cdd:COG5809   132 MEEALRESEEKF---RLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKD 208
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 636783241  252 GTSKEIESLLPSKDGHIYSVLSRVNRVVTADGRPYVVGSFSDISPLKEREKAL 304
Cdd:COG5809   209 GGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELL 261
PAS COG2202
PAS domain [Signal transduction mechanisms];
6-304 1.61e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.96  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241    6 ELLELACRRIADLDTPAYVKNSELRYIAVNEAYARFLGREISDFIGRRSRELLDRPEEEDREDKERRAL----VFGTEEN 81
Cdd:COG2202     8 ESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALagggVWRGELR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   82 AICFDaaglSHERIQIESFSPSADRA----YVLGIFE-VREppRRavddsdvaadfaRVREALEQhdhpigifagdgrpl 156
Cdd:COG2202    88 NRRKD----GSLFWVELSISPVRDEDgeitGFVGIARdITE--RK------------RAEEALRE--------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  157 vvnaayrngakpaaiSEtawhesvnelDLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPD 236
Cdd:COG2202   135 ---------------SE----------ERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPE 189
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636783241  237 GGEAIYQENLLALEGGTSK-EIESLLPSKDGHIYSVLSRVNRVVTADGRPYVVGSFSDISPLKEREKAL 304
Cdd:COG2202   190 DRERLLELLRRLLEGGRESyELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
564-809 1.64e-08

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: 58.99  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   564 LKSREE--ELRQLLSRAEAADRAKSEFLANMS----HEIRTPMNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTII 637
Cdd:TIGR03785  458 SRSRDEigDLSRSFAQMVARLRQYTHYLENMSsrlsHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMIL 537
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   638 NDILDFSKIDAGQMKLRKAAFD----ITEAVEDVATLLSSHAAEKNIE---LLVRAAPDLPAavigdagrfrQIVTNLVG 710
Cdd:TIGR03785  538 NNMSEATRLEQAIQSAEVEDFDlsevLSGCMQGYQMTYPPQRFELNIPetpLVMRGSPELIA----------QMLDKLVD 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   711 NAVKFTERGHVfVDVGFEtAAGGEIMasIRIEDTGIGIPPEKLESVFDKFSQVDASSTRRHEGTGLGLAITAGLVDLFGG 790
Cdd:TIGR03785  608 NAREFSPEDGL-IEVGLS-QNKSHAL--LTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQG 683
                          250       260
                   ....*....|....*....|
gi 636783241   791 YLNVDSEW-GKGSVFTVNLP 809
Cdd:TIGR03785  684 RIQAENRQqNDGVVFRISLP 703
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
990-1123 1.64e-08

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 56.36  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGT-GLSFL-VVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREkgqgHRVPII 1067
Cdd:COG3279     4 ILIVDDEPLARERLERLLEKYpDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD----PPPPII 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636783241 1068 GVTAH---ALESdrelcLDAGMDDYMSKPISPELLE---EKIRQWLGTSEQQPERTTAPRIF 1123
Cdd:COG3279    80 FTTAYdeyALEA-----FEVNAVDYLLKPIDEERLAkalEKAKERLEAKAAAEASPEEKDRI 136
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
990-1105 2.50e-08

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 53.36  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghRVPIIGV 1069
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESP----DTPVIVV 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISP-ELLEEKIRQ 1105
Cdd:cd17555    79 SGAGVMSDAVEALRLGAWDYLTKPIEDlAVLEHAVRR 115
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
697-794 2.70e-08

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: 52.85  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  697 DAGRFRQIVTNLVGNAVKFTERGHVfvdVGFETAAGGEiMASIRIEDTGIGIPPEKLESVFDKFSqvdaSSTRRHEG--- 773
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEGGL---IALQLEADTE-GIELLVFDEGSGIPDYALNRVFERFY----SLPRPHSGqks 72
                          90       100
                  ....*....|....*....|.
gi 636783241  774 TGLGLAITAGLVDLFGGYLNV 794
Cdd:cd16945    73 TGLGLAFVQEVAQLHGGRITL 93
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
990-1104 2.79e-08

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 55.74  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNE--VNQIVFTqiLQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghRVPII 1067
Cdd:PRK11083    6 ILLVEDEQaiADTLVYA--LQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHP----ALPVI 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 636783241 1068 GVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:PRK11083   80 FLTARSDEVDRLVGLEIGADDYVAKPFSPREVAARVR 116
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
990-1104 3.37e-08

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 52.83  E-value: 3.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGV 1069
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSD-----VPIIII 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 636783241 1070 TAHAL-ESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17594    77 SGDRRdEIDRVVGLELGADDYLAKPFGLRELLARVR 112
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1017-1105 3.54e-08

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 52.74  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1017 VDNGEEAVAAWERYTPRIIMMDVSMPVMNGhqaTQTIRE-REKGQGHRVPIIGVTAHalESDRELCLDAGMDDYMSKPIS 1095
Cdd:cd19931    30 ASSGEEGIELAERLDPDLILLDLNMKGMSG---LDTLKAlREEGVSARIVILTVSDA--EDDVVTALRAGADGYLLKDME 104
                          90
                  ....*....|
gi 636783241 1096 PELLEEKIRQ 1105
Cdd:cd19931   105 PEDLLEALKQ 114
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1007-1116 3.99e-08

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 54.72  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1007 LQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPIIGVTAHAlesDRELCLDA-- 1084
Cdd:COG4566    19 LESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAAR----GSPLPVIFLTGHG---DVPMAVRAmk 91
                          90       100       110
                  ....*....|....*....|....*....|...
gi 636783241 1085 -GMDDYMSKPISPELLEEKIRQWLGTSEQQPER 1116
Cdd:COG4566    92 aGAVDFLEKPFDDQALLDAVRRALARDRARRAE 124
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
830-915 4.90e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 56.78  E-value: 4.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRA-DPRfveL 908
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADI-----HPDVVLMDIRMPEMDGIKALKEMRShETR---T 77

                  ....*..
gi 636783241  909 PIIFLTS 915
Cdd:PRK11361   78 PVILMTA 84
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
831-918 4.97e-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: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAIL------EAAADLGVTVDAVVLDYHMPDMNGADVARRLRADPR 904
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeeDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90
                  ....*....|....
gi 636783241  905 FVELPIIFLTSMDI 918
Cdd:cd17581    81 LKEIPVVIMSSENI 94
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
831-937 5.54e-08

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: 51.78  E-value: 5.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAilEAAADlgvTVDAVVLDYHMPDMNGADVARRLRadpRFVELPI 910
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLL--EAATR---KPDLIILDLGLPDMDGLEVIRRLR---EWSAVPV 72
                          90       100
                  ....*....|....*....|....*....
gi 636783241  911 IFLTSMDiSGTEKeFAALNGHA--HLMKP 937
Cdd:cd17620    73 IVLSARD-EESDK-IAALDAGAddYLTKP 99
PRK11517 PRK11517
DNA-binding response regulator HprR;
990-1107 7.01e-08

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 54.52  E-value: 7.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAV--AAWERYTprIIMMDVSMPVMNGHQATQTIRerekgQGHRVPII 1067
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLylALKDDYA--LIILDIMLPGMDGWQILQTLR-----TAKQTPVI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 636783241 1068 GVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWL 1107
Cdd:PRK11517   76 CLTARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQL 115
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
990-1071 8.41e-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: 8.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghRVPIIGV 1069
Cdd:cd17554     3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKP----DLPVIIC 78

                  ..
gi 636783241 1070 TA 1071
Cdd:cd17554    79 TA 80
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
830-928 8.72e-08

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: 52.01  E-value: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQL-SLWGFD--GVAAegggTGLAILEAAADLgvTVDAVVLDYHMPDMNGADVARRLRA-DPrf 905
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILeSDPDIEvvGTAR----DGEEALEKIKEL--KPDVITLDIEMPVMDGLEALRRIMAeRP-- 73
                          90       100
                  ....*....|....*....|...
gi 636783241  906 veLPIIFLTSMDISGTEKEFAAL 928
Cdd:cd17541    74 --TPVVMVSSLTEEGAEITLEAL 94
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
830-937 9.98e-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: 50.96  E-value: 9.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADlgvtVDAVVLDYHMPDMNGADVARRLRA-DPrfvEL 908
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKD----IDIVVTDIVMPEMDGIELAREARKiDP---DV 73
                          90       100
                  ....*....|....*....|....*....
gi 636783241  909 PIIFLTSMDISGTEKEFAALNGHAHLMKP 937
Cdd:cd18160    74 KILFISGGAAAAPELLSDAVGDNATLKKP 102
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
676-799 1.06e-07

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: 51.86  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  676 AEKNIELLVRAAPDLpaAVIGDAGRFRQIVTNLVGNAVKFterGHVFVDVgfeTAAGGEIMASIRIEDTGIGIPPEKLES 755
Cdd:cd16954    15 QRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKW---CLEFVEV---TARQTDGGLHLIVDDDGPGVPESQRSK 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 636783241  756 VFDKFSQVDasstRRHEGTGLGLAITAGLVDLFGGYLNV-DSEWG 799
Cdd:cd16954    87 IFQRGQRLD----EQRPGQGLGLAIAKEIVEQYGGELSLsDSPLG 127
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
830-914 1.15e-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: 51.29  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAaadlgVTVDAVVLDYHMPDMNGADVARRLRAdpRFVELP 909
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALARE-----EKPDYAVLDLRLGGDSGLDLIPPLRA--LQPDAR 74

                  ....*
gi 636783241  910 IIFLT 914
Cdd:cd17563    75 IVVLT 79
resp_reg_YycF NF040534
response regulator YycF;
1007-1120 1.39e-07

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 53.57  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1007 LQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqgHRVPIIGVTAHALESDRELCLDAGM 1086
Cdd:NF040534   20 LKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKK-----YDMPIIMLTAKDSEIDKVLGLELGA 94
                          90       100       110
                  ....*....|....*....|....*....|....
gi 636783241 1087 DDYMSKPISPELLEEKIRQWLGTSEQQPERTTAP 1120
Cdd:NF040534   95 DDYVTKPFSTRELIARVKANLRRHQQQNTEEEEE 128
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
988-1099 1.62e-07

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: 50.88  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  988 VDVLVAEDNEVNQIVFTQILQGTGLSFLV-VDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGqghrvPI 1066
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-----PI 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 636783241 1067 IGVTAHALESDRELCLDAGMDDYMSKPISPELL 1099
Cdd:cd19932    76 VLLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
831-914 1.68e-07

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: 51.34  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADlGVtvdaVVLDYHMPDMNGADVARRLRA-DPrfvELP 909
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFP-GV----VISDIRMPGMDGLELLAQIRElDP---DLP 72

                  ....*
gi 636783241  910 IIFLT 914
Cdd:cd17549    73 VILIT 77
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
831-920 1.69e-07

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: 50.96  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAaadlgVTVDAVVLDYHMPDMNGADVARRLRAdpRFVELPI 910
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKE-----RRPDLVLLDIWLPDMDGLELLKEIKE--KYPDLPV 73
                          90
                  ....*....|
gi 636783241  911 IfltsMdISG 920
Cdd:cd17550    74 I----M-ISG 78
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1019-1105 1.86e-07

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: 50.61  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1019 NGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErekgQGHRVPIIGVTAHALESDRELCLDAGMDDYMSKPISPEL 1098
Cdd:cd17593    33 NGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPV----EQLETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEK 108

                  ....*..
gi 636783241 1099 LEEKIRQ 1105
Cdd:cd17593   109 LAQLLEE 115
orf27 CHL00148
Ycf27; Reviewed
830-946 2.53e-07

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 53.18  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPrfvELP 909
Cdd:CHL00148    8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKE-----QPDLVILDVMMPKLDGYGVCQEIRKES---DVP 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 636783241  910 IIFLTSMD-----ISGTEkefaaLNGHAHLMKP-------ARA-NVLRNT 946
Cdd:CHL00148   80 IIMLTALGdvsdrITGLE-----LGADDYVVKPfspkeleARIrSVLRRT 124
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
994-1093 2.74e-07

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: 49.67  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  994 EDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREkgQGHRVPIIGVTAHA 1073
Cdd:cd17602     5 DDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSS--ALKDTPIIMLTGKD 82
                          90       100
                  ....*....|....*....|
gi 636783241 1074 LESDRELCLDAGMDDYMSKP 1093
Cdd:cd17602    83 GLVDRIRAKMAGASGYLTKP 102
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
831-914 3.62e-07

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: 49.30  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRFVELPI 910
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQY-----IPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPV 75

                  ....
gi 636783241  911 IFLT 914
Cdd:cd19927    76 IFLT 79
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1019-1105 3.78e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 51.95  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1019 NGEEAVAAWERYTPRIIMMDVSMPVMNGhqaTQTIRE-REKGQGHRVPIIGVTAHalESDRELCLDAGMDDYMSKPISPE 1097
Cdd:PRK10651   40 NGEQGIELAESLDPDLILLDLNMPGMNG---LETLDKlREKSLSGRIVVFSVSNH--EEDVVTALKRGADGYLLKDMEPE 114

                  ....*...
gi 636783241 1098 LLEEKIRQ 1105
Cdd:PRK10651  115 DLLKALQQ 122
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
990-1079 3.94e-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: 49.71  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFL-VVDNGEEAVAAWERYTPRIIMMDVSMP-VMNGHQATQTIRERekgqgHRVPII 1067
Cdd:cd17534     3 ILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK-----FDIPVI 77
                          90
                  ....*....|..
gi 636783241 1068 GVTAHaleSDRE 1079
Cdd:cd17534    78 FLTAY---SDEE 86
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
990-1105 4.43e-07

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: 49.58  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQI--LQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIreREKGQGHRVPIi 1067
Cdd:cd19930     1 VLIAEDQEMVRGALAALleLEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAEL--REELPDTKVLI- 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241 1068 gVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQ 1105
Cdd:cd19930    78 -VTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRT 114
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
831-952 6.12e-07

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: 49.26  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQL--SLWGFDGVA-AEGGGTGLAILEAaadlgVTVDAVVLDYHMPDMNGADVARRLRAdpRFVE 907
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGFEVVGeAENGEEALELIEE-----HKPDIVITDIRMPGMDGLELIEKIRE--LYPD 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 636783241  908 LPIIFLTSMDisgtEKEFA--ALNGHAH--LMKPARANVLRNTVVEVVR 952
Cdd:cd17536    74 IKIIILSGYD----DFEYAqkAIRLGVVdyLLKPVDEEELEEALEKAKE 118
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
831-917 6.25e-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: 49.02  E-value: 6.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRAdpRFVELPI 910
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASG-----PYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPV 73

                  ....*..
gi 636783241  911 IFLTSMD 917
Cdd:cd17624    74 LILTARD 80
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
830-888 6.57e-07

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: 47.18  E-value: 6.57e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 636783241    830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMP 888
Cdd:smart00448    2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-----KPDLILLDIMMP 55
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
990-1057 6.65e-07

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 49.51  E-value: 6.65e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGlSFLVV---DNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTI---RERE 1057
Cdd:COG2197     4 VLIVDDHPLVREGLRALLEAEP-DIEVVgeaADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLltpRERE 76
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
830-901 6.82e-07

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: 48.94  E-value: 6.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRA 901
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEP-----VDVVISDQRMPGMDGAELLKRVRE 68
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1007-1093 7.12e-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: 7.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1007 LQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGVTAHALESDRELCLDAGM 1086
Cdd:cd19936    18 LEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKST-----LPVIFLTSKDDEIDEVFGLRMGA 92

                  ....*..
gi 636783241 1087 DDYMSKP 1093
Cdd:cd19936    93 DDYITKP 99
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
827-914 7.50e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 51.50  E-value: 7.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  827 QGARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRAdpRFV 906
Cdd:PRK11083    2 QQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQP-----PDLVILDVGLPDISGFELCRQLLA--FHP 74

                  ....*...
gi 636783241  907 ELPIIFLT 914
Cdd:PRK11083   75 ALPVIFLT 82
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
990-1104 8.35e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 51.26  E-value: 8.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREreKGQGHRVPIIGV 1069
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKR--ESMTRDIPVVML 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:PRK10161   83 TARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
297-815 8.50e-07

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 52.99  E-value: 8.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  297 LKEREKALIEAQKHKELLHRDIENILRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDPFDGRPFIDVIRRNYELGRYD 376
Cdd:COG3920    14 AALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  377 GTQTPEEIYDFRKHLFETEEPEPIELGWAGGKSVIFDSRRISNDRILLTYADITAVREREKEIHETRAALERLGEMMRDA 456
Cdd:COG3920    94 AAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  457 THAMPQGLAIVQDGIIRMSNEALSDILQIPATYLERGEGWIGMFEYCAARGDFHDAAAETLQGWRDNIAARLPISTAFHV 536
Cdd:COG3920   174 AAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  537 GGERWVNMDATVSRGQHWVALFTDVTELKSREEELRQLLSRAEAAdraksefLANMSHEIRTPMNGVLGMAELLAKTNLD 616
Cdd:COG3920   254 LLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELL-------LRELHHRVKNNLQVVSSLLRLQARRADD 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  617 TRQKTFVDII---VKSgnalLTIINDIL----DFSKIDAGQMklrkaafditeaVEDVATLLSSHAAEKNIELLVRAAP- 688
Cdd:COG3920   327 PEAREALEESqnrIQA----LALVHELLyqseDWEGVDLRDY------------LRELLEPLRDSYGGRGIRIELDGPDv 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  689 --DLPAAV-IGdagrfrQIVTNLVGNAVK--FTERGHVFVDVGFETAAGGeimASIRIEDTGIGIPPEklesvfdkfsqV 763
Cdd:COG3920   391 elPADAAVpLG------LILNELVTNALKhaFLSGEGGRIRVSWRREDGR---LRLTVSDNGVGLPED-----------V 450
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 636783241  764 DASSTRrhegtGLGLAITAGLVDLFGGYLNVDSEwgKGSVFTVNLPFAVAAA 815
Cdd:COG3920   451 DPPARK-----GLGLRLIRALVRQLGGTLELDRP--EGTRVRITFPLAELAA 495
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
990-1105 1.18e-06

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: 48.64  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGqghrVPIIGV 1069
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPD----LPVILI 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 636783241 1070 TAHAlesDRELCLDA---GMDDYMSKPISPELLEEKIRQ 1105
Cdd:cd17549    77 TGHG---DVPMAVEAmraGAYDFLEKPFDPERLLDVVRR 112
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
190-299 1.22e-06

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 48.18  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   190 LEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALEGGTS-KEIESLLPSKDGHI 268
Cdd:pfam08448    1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPiDFLEELLLNGEERH 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 636783241   269 YSVlsRVNRVVTADGRP-YVVGSFSDISPLKE 299
Cdd:pfam08448   81 YEL--RLTPLRDPDGEViGVLVISRDITERRR 110
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
831-917 1.34e-06

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: 47.82  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRAdpRFVELPI 910
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNE-----YDLIILDVMLPGLDGLEVLRRLRA--AGKQTPV 73

                  ....*..
gi 636783241  911 IFLTSMD 917
Cdd:cd19935    74 LMLTARD 80
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
831-916 1.42e-06

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: 48.09  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADlgvtvDAVVLDYHMPDMNGADVARRLRADPRFVELPI 910
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRP-----TLVISDIVMPEMDGYELCRKIKSDPDLKDIPV 75

                  ....*.
gi 636783241  911 IFLTSM 916
Cdd:cd17598    76 ILLTTL 81
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
990-1093 1.82e-06

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: 47.76  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEA---VAAWERYTPR------IIMMDVSMPVMNGHQATQTIREREKGQ 1060
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEAlnkLENLAKEGNDlskeldLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 636783241 1061 ghRVPIIGVTAHALESDRELCLDAGMDDYMSKP 1093
Cdd:cd19924    81 --NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10643 PRK10643
two-component system response regulator PmrA;
990-1104 2.00e-06

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 50.03  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErekgQGHRVPIIGV 1069
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ----KKYTLPVLIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:PRK10643   79 TARDTLEDRVAGLDVGADDYLVKPFALEELHARIR 113
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
829-915 2.46e-06

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: 47.46  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAeggGTGLAILEAAADLGVtvDAVVLDYHMPDMNGADVARRLRADPrfvEL 908
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFC---GDGTQALAAFREVRP--DLVLLDLMLPGIDGIEVCRQIRAES---GV 72

                  ....*..
gi 636783241  909 PIIFLTS 915
Cdd:cd17626    73 PIVMLTA 79
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
830-985 2.49e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 50.92  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLwgfD------GVAAegggTGLAILEAAADLgvTVDAVVLDYHMPDMNGADVARRL-RAD 902
Cdd:PRK00742    5 RVLVVDDSAFMRRLISEILNS---DpdievvGTAP----DGLEAREKIKKL--NPDVITLDVEMPVMDGLDALEKImRLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  903 PrfveLPIIFLTSMDISGTEKEFAALNGHA--HLMKPARAnvLRNTVVEVVR--ASRVKQASEAEIARLQTEAAVPAPAL 978
Cdd:PRK00742   76 P----TPVVMVSSLTERGAEITLRALELGAvdFVTKPFLG--ISLGMDEYKEelAEKVRAAARARVRALPPRAAAAARAA 149

                  ....*..
gi 636783241  979 VPQKRAA 985
Cdd:PRK00742  150 AAAPAAL 156
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
990-1101 2.98e-06

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 47.44  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTG-LSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqGHRVPII- 1067
Cdd:cd17530     3 VLVLDDDPFQCMMAATILEDLGpGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHS--NAAVILMs 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 636783241 1068 GVTAHALESDRELCLDAGMD--DYMSKPISPELLEE 1101
Cdd:cd17530    81 GLDGGILESAETLAGANGLNllGTLSKPFSPEELTE 116
PRK10766 PRK10766
two-component system response regulator TorR;
990-1099 4.12e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 49.27  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGV 1069
Cdd:PRK10766    5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRST-----VGIILV 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISP-ELL 1099
Cdd:PRK10766   80 TGRTDSIDRIVGLEMGADDYVTKPLELrELL 110
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1007-1105 4.81e-06

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 46.82  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1007 LQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPIIGVTAH-----ALEsdrelC 1081
Cdd:cd17537    20 LRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLAR----GSNIPIIFITGHgdvpmAVE-----A 90
                          90       100
                  ....*....|....*....|....
gi 636783241 1082 LDAGMDDYMSKPISPELLEEKIRQ 1105
Cdd:cd17537    91 MKAGAVDFLEKPFRDQVLLDAIEQ 114
PRK11173 PRK11173
two-component response regulator; Provisional
990-1121 5.49e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 48.86  E-value: 5.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghrVPIIGV 1069
Cdd:PRK11173    6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQAN-----VALMFL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTSEQQPERTTAPR 1121
Cdd:PRK11173   81 TGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLLSRTMNLGTVSEERR 132
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
831-914 5.79e-06

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 46.43  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTeqlSLWGFDGVAAEGGGTGLAILEAAAdlGVTVDAVVLDYHMPDMNGADVARRLRAdpRFVELPI 910
Cdd:cd17537     3 VYVVDDDEAVRDSLA---FLLRSVGLAVKTFTSASAFLAAAP--PDQPGCLVLDVRMPGMSGLELQDELLA--RGSNIPI 75

                  ....
gi 636783241  911 IFLT 914
Cdd:cd17537    76 IFIT 79
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
830-915 5.88e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 48.65  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAaadlgvTVDAVVLDYHMPDMNGADVARRLRadpRFVELP 909
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD------SIDLLLLDVMMPKKNGIDTLKELR---QTHQTP 73

                  ....*.
gi 636783241  910 IIFLTS 915
Cdd:PRK10955   74 VIMLTA 79
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
830-899 6.47e-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: 46.81  E-value: 6.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGgTGLAILEAAADLgvTVDAVVLDYHMPDMNGADVARRL 899
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEPDIEVVGEAA-DGEEALELLEEL--RPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
831-917 6.70e-06

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: 46.12  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGgtglailEAAADLGVT--VDAVVLDYHMPDMNGADVARRLRADPRfvEL 908
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDG-------EEALFQGEEepYDLVVLDLGLPGMDGLSVLRRWRSEGR--AT 71

                  ....*....
gi 636783241  909 PIIFLTSMD 917
Cdd:cd19934    72 PVLILTARD 80
PRK10693 PRK10693
two-component system response regulator RssB;
1018-1095 6.86e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 49.22  E-value: 6.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1018 DNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqGHRVPIIGVTA--HALESDRELCLdaGMDDYMSKPIS 1095
Cdd:PRK10693    4 ANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNR----GDQTPVLVISAteNMADIAKALRL--GVQDVLLKPVK 77
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1019-1104 6.90e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 49.76  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1019 NGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqgHRVPIIGVTAHALE-SDREL-CLDAGMDDYMSKP--- 1093
Cdd:PRK00742   37 DGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRL-----RPTPVVMVSSLTERgAEITLrALELGAVDFVTKPflg 111
                          90
                  ....*....|....*..
gi 636783241 1094 ISP------ELLEEKIR 1104
Cdd:PRK00742  112 ISLgmdeykEELAEKVR 128
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
990-1120 7.66e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 49.87  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghRVPIIGV 1069
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHP----MLPVIIM 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 636783241 1070 TAHaleSDRELCLDA---GMDDYMSKPISPE----LLEEKIRQWLgtSEQQPERTTAP 1120
Cdd:PRK10923   82 TAH---SDLDAAVSAyqqGAFDYLPKPFDIDeavaLVERAISHYQ--EQQQPRNIQVN 134
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
184-313 9.26e-06

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 49.38  E-value: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  184 DLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFgpdGGEAIYQenllALEggTSKEIESLLPS 263
Cdd:COG3829    11 EELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELI---PNSPLLE----VLK--TGKPVTGVIQK 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636783241  264 KDGHIYSVLSRVNRVVtADGRP-YVVGSFSDISPLKEREKALIEAQKHKEL 313
Cdd:COG3829    82 TGGKGKTVIVTAIPIF-EDGEViGAVETFRDITELKRLERKLREEELERGL 131
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
563-803 1.09e-05

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 49.68  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  563 ELKSREEELRQllsraeAADRAKS-EFLANMSHEIRTP---MNGVLGMAELLAKTNLDTRQKTFVDIIVKSGNALLTIIN 638
Cdd:COG4192   416 NLRQTQDELIQ------AAKMAVVgQTMTSLAHELNQPlnaMSMYLFSAKKALEQENYAQLPTSLDKIEGLIERMDKIIK 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  639 DILDFSKIDAGQMKlrkaAFDITEAVEDVATLLSSHAAEKNIELLVraaPDlPAAVIGDAGRFRQIVTNLVGNAVKFTEr 718
Cdd:COG4192   490 SLRQFSRKSDTPLQ----PVDLRQVIEQAWELVESRAKPQQITLHI---PD-DLMVQGDQVLLEQVLVNLLVNALDAVA- 560
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  719 GHVFVDVGFETAAGgeiMASIRIEDTGIGIPpeKLESVFDKFSqvdassTRRHEGTGLGLAITAGLVDLFGGYLNVDSEW 798
Cdd:COG4192   561 TQPQISVDLLSNAE---NLRVAISDNGNGWP--LVDKLFTPFT------TTKEVGLGLGLSICRSIMQQFGGDLYLASTL 629

                  ....*
gi 636783241  799 GKGSV 803
Cdd:COG4192   630 ERGAM 634
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
830-946 1.34e-05

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 45.31  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDN----EVNRRILtEQLSlwGFDGVA-AEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRAdpR 904
Cdd:cd19925     2 NVLIVEDDpmvaEIHRAYV-EQVP--GFTVIGtAGTGEEALKLLKERQ-----PDLILLDIYLPDGNGLDLLRELRA--A 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 636783241  905 FVELPIIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNT 946
Cdd:cd19925    72 GHDVDVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQR 113
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1018-1105 1.41e-05

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: 45.22  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1018 DNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREkgqgHRVPIIGVTAHalesdRELCLDA---GMDDYMSKPI 1094
Cdd:cd17532    31 ENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLA----KPPLIVFVTAY-----DEYAVEAfelNAVDYLLKPF 101
                          90
                  ....*....|....
gi 636783241 1095 SPELLEE---KIRQ 1105
Cdd:cd17532   102 SEERLAEalaKLRK 115
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
990-1097 1.41e-05

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: 45.31  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWeRYTP---RIIMMDVSMPVMNGHQATQTIRErEKgqghRVPI 1066
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSML-RENKdefDLVITDVHMPDMDGFEFLELIRL-EM----DLPV 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 636783241 1067 IGVTAHALESDRELCLDAGMDDYMSKPISPE 1097
Cdd:cd17584    75 IMMSADGSTSTVMKGLAHGACDYLLKPVSIE 105
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
989-1104 1.50e-05

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 47.49  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  989 DVLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRerekgQGHRVPIIG 1068
Cdd:PRK10529    3 NVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR-----QWSAIPVIV 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 636783241 1069 VTAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:PRK10529   78 LSARSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
830-900 1.54e-05

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: 45.08  E-value: 1.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlGVTVDAVVLDYHMPDMNGADVARRLR 900
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASA---EHSFQLVLLDLCMPEMDGFEVALRIR 69
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
831-918 1.55e-05

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: 44.97  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEgggTGLAILEAAADlgVTVDAVVLDYHMPDMNGADVARRLRAdprFVELPI 910
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIE---DFEDVLEEFLQ--FKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPI 72
                          90
                  ....*....|..
gi 636783241  911 IFLTS----MDI 918
Cdd:cd18159    73 IFISSrddnMDQ 84
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
990-1121 1.75e-05

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: 46.45  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREkgqgHRVPIIGV 1069
Cdd:COG4567     7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERD----PDARIVVL 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 636783241 1070 TAHA-LESDRELClDAGMDDYMSKPISPELLEEKIRQWLGTSEQQPERTTAPR 1121
Cdd:COG4567    83 TGYAsIATAVEAI-KLGADDYLAKPADADDLLAALERAEGDAPAPPENPMSLD 134
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
690-808 1.97e-05

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: 45.53  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  690 LPAAVIGDAGRFRQIVTNLVGNAVKFTERghvfvdvgfetaaGGEIMASIRIEDTGIGI---------PPEKLESVFDKF 760
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNG-------------GGNITFRVFLEGGSEDRsdrdwgpwrPSMSDESVEIRF 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241  761 --------SQVD------ASSTRRH----EGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNL 808
Cdd:cd16938    68 eveindsgSPSIesasmrNSLNRRYnlseLGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
990-1104 2.36e-05

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: 44.71  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgqghRVPIIGV 1069
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKV----KTPILIL 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17616    77 SGLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
831-914 2.45e-05

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: 44.74  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTglailEAAADLGVTVDAVVLDYHMPDMNGADVARRLRADPrfvELPI 910
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAE-----EARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS---DVPI 73

                  ....
gi 636783241  911 IFLT 914
Cdd:cd17594    74 IIIS 77
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
193-294 2.98e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 44.16  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  193 LPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALEGGTSKEIESLLPSKDGHIYSVL 272
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                          90       100
                  ....*....|....*....|...
gi 636783241  273 SRVNRVVTADGRP-YVVGSFSDI 294
Cdd:cd00130    81 VSLTPIRDEGGEViGLLGVVRDI 103
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
831-917 3.21e-05

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 43.97  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNevnRRILTE---QLSLWGFDGVAAEGGGTGL-AILEAAADLgvtvdaVVLDYHMPDMNGADVARRLRADPrfv 906
Cdd:cd19936     1 IALVDDD---RNILTSvsmALEAEGFSVETYTDGASALdGLNARPPDL------AILDIKMPRMDGMELLQRLRQKS--- 68
                          90
                  ....*....|.
gi 636783241  907 ELPIIFLTSMD 917
Cdd:cd19936    69 TLPVIFLTSKD 79
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
695-799 3.69e-05

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 47.71  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  695 IGDAGRFRQIVTNLVGNAVKFTERghvFVDVgfeTAAGGEIMASIRIEDTGIGIPPEKLESVFDKFSQVDassTRRhEGT 774
Cdd:PRK10815  373 VGEKNDFMEVMGNVLDNACKYCLE---FVEI---SARQTDEHLHIVVEDDGPGIPESKRELIFDRGQRAD---TLR-PGQ 442
                          90       100
                  ....*....|....*....|....*.
gi 636783241  775 GLGLAITAGLVDLFGGYLNV-DSEWG 799
Cdd:PRK10815  443 GLGLSVAREITEQYEGKISAgDSPLG 468
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
829-917 3.96e-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: 43.91  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPrfvEL 908
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQ-----DIDLVLLDINLPGKDGLSLTRELREQS---EV 72

                  ....*....
gi 636783241  909 PIIFLTSMD 917
Cdd:cd17619    73 GIILVTGRD 81
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
831-947 5.09e-05

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: 43.68  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLS-LWGFDGVA-AEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRadpRFVEL 908
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEeHPDIEIVGeAENGEEALEAIEELK-----PDVVFLDIQMPGLDGLELAKKLS---KLAKP 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 636783241  909 P-IIFLTSMDisgtekEFA--ALNGHA--HLMKPARANVLRNTV 947
Cdd:cd17532    73 PlIVFVTAYD------EYAveAFELNAvdYLLKPFSEERLAEAL 110
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
988-1112 5.67e-05

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 46.95  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  988 VDVLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGhqaTQTIREReKGQGHRVPII 1067
Cdd:PRK10365    6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDG---IATLKEI-KALNPAIPVL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 636783241 1068 GVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIRQWLGTSEQ 1112
Cdd:PRK10365   82 IMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHS 126
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
990-1106 5.91e-05

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 43.77  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDN----EVNQIVFTQILQGTGLSflVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErekgQGHRVP 1065
Cdd:cd19925     3 VLIVEDDpmvaEIHRAYVEQVPGFTVIG--TAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA----AGHDVD 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 636783241 1066 IIGVTAHA-LESDRELcLDAGMDDYMSKPISPELLEEKIRQW 1106
Cdd:cd19925    77 VIVVTAANdVETVREA-LRLGVVDYLIKPFTFERLRQRLERY 117
fixJ PRK09390
response regulator FixJ; Provisional
829-914 6.38e-05

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 45.38  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEgggTGLAILEAAADLGVTVdaVVLDYHMPDMNGADVARRLRAdpRFVEL 908
Cdd:PRK09390    4 GVVHVVDDDEAMRDSLAFLLDSAGFEVRLFE---SAQAFLDALPGLRFGC--VVTDVRMPGIDGIELLRRLKA--RGSPL 76

                  ....*.
gi 636783241  909 PIIFLT 914
Cdd:PRK09390   77 PVIVMT 82
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
316-371 7.26e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.00  E-value: 7.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 636783241    316 RDIENILRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDpFDGRPFIDVIRRNYE 371
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEE-LIGKSLLELIHPEDR 55
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
831-917 7.66e-05

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: 42.96  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPrfvELPI 910
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAG-----ADIVLLDLMLPGLSGTEVCRQLRARS---NVPV 72

                  ....*..
gi 636783241  911 IFLTSMD 917
Cdd:cd17621    73 IMVTAKD 79
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
708-810 7.79e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 46.55  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  708 LVGNAVKF-----TERGHVFVDVgfeTAAGGEIMasIRIEDTGIGIPPEKLESVFDKFSqvdasstRRHEGTGLGLA-IT 781
Cdd:COG2972   344 LVENAIEHgiepkEGGGTIRISI---RKEGDRLV--ITVEDNGVGMPEEKLEKLLEELS-------SKGEGRGIGLRnVR 411
                          90       100       110
                  ....*....|....*....|....*....|.
gi 636783241  782 AGLVDLFGGY--LNVDSEWGKGSVFTVNLPF 810
Cdd:COG2972   412 ERLKLYYGEEygLEIESEPGEGTTVTIRIPL 442
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
990-1104 9.05e-05

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: 43.06  E-value: 9.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNE-VNQIV-FTqiLQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKGQGhrVPII 1067
Cdd:cd17562     3 ILAVDDSAsIRQMVsFT--LRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKF--TPIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 636783241 1068 GVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:cd17562    79 MLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVK 115
PRK10610 PRK10610
chemotaxis protein CheY;
1012-1105 9.07e-05

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 43.42  E-value: 9.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1012 LSFLVVDNGEEAVAAWERYTP---RIIMMDVSMPVMNGHQATQTIREreKGQGHRVPIIGVTAHALESDRELCLDAGMDD 1088
Cdd:PRK10610   28 LGFNNVEEAEDGVDALNKLQAggfGFVISDWNMPNMDGLELLKTIRA--DGAMSALPVLMVTAEAKKENIIAAAQAGASG 105
                          90
                  ....*....|....*..
gi 636783241 1089 YMSKPISPELLEEKIRQ 1105
Cdd:PRK10610  106 YVVKPFTAATLEEKLNK 122
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
830-970 9.56e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 44.92  E-value: 9.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRADPRfvELP 909
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTG-----DYDLIILDIMLPDVNGWDIVRMLRSANK--GMP 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636783241  910 IIFLTSMDISGTEKEFAALNGHAHLMKP-ARANVLRNTVVEVVRASRVKQASEAEIARLQTE 970
Cdd:PRK09836   75 ILLLTALGTIEHRVKGLELGADDYLVKPfAFAELLARVRTLLRRGAAVIIESQFQVADLMVD 136
PRK10337 PRK10337
sensor protein QseC; Provisional
569-780 1.04e-04

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 46.18  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  569 EELRQLLSRAEAADRAKSEFLANMSHEIRTPMNGVLGMAEL--LAKTNLDTRQKTFVDIivKSGNALLT-IINDILDFSK 645
Cdd:PRK10337  221 EALNQLFARTHAMMVRERRFTSDAAHELRSPLAALKVQTEVaqLSDDDPQARKKALLQL--HAGIDRATrLVDQLLTLSR 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  646 IDAGQMKLRKAAFDITEAVEDVATLLSSHAAEKNIELLVrAAPDLPAAVIGDAGRFRQIVTNLVGNAVKFTERGHVfVDV 725
Cdd:PRK10337  299 LDSLDNLQDVAEIPLEDLLQSAVMDIYHTAQQAGIDVRL-TLNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSV-VDV 376
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 636783241  726 GFETaaggeimASIRIEDTGIGIPPEKLESVFDKF----SQvDASstrrheGTGLGLAI 780
Cdd:PRK10337  377 TLNA-------RNFTVRDNGPGVTPEALARIGERFyrppGQ-EAT------GSGLGLSI 421
ompR PRK09468
osmolarity response regulator; Provisional
827-914 1.05e-04

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 44.96  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  827 QGARILVVDDN----EVNRRILTEQlslwGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRAD 902
Cdd:PRK09468    4 ENYKILVVDDDmrlrALLERYLTEQ----GFQVRSAANAEQMDRLLTRE-----SFHLMVLDLMLPGEDGLSICRRLRSQ 74
                          90
                  ....*....|..
gi 636783241  903 PRfvELPIIFLT 914
Cdd:PRK09468   75 NN--PTPIIMLT 84
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
831-917 1.23e-04

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 42.36  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILeaaadLGVTVDAVVLDYHMPDMNGADVARRLRADPRFVELPI 910
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTL-----LNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPI 75

                  ....*..
gi 636783241  911 IFLTSMD 917
Cdd:cd17602    76 IMLTGKD 82
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
990-1104 1.24e-04

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 44.46  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQgTGLSFLVV---DNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErekgQGHRVPI 1066
Cdd:PRK10403    9 VLIVDDHPLMRRGVRQLLE-LDPGFEVVaeaGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRR----DGVTAQI 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241 1067 IGVTAHALESDRELCLDAGMDDYMSKPISPELLEEKIR 1104
Cdd:PRK10403   84 IILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIR 121
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
831-917 1.38e-04

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 42.72  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGgTGLAILEAAADLgvTVDAVVLDYHMPDMNGADVARRLRADPrfVELPI 910
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEAS-SGEEGIELAERL--DPDLILLDLNMKGMSGLDTLKALREEG--VSARI 75

                  ....*..
gi 636783241  911 IFLTSMD 917
Cdd:cd19931    76 VILTVSD 82
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
831-917 1.53e-04

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: 42.41  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAaadlgVTVDAVVLDYHMPDMNGADVARRLRADPrfvELPI 910
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEE-----EQPDLILLDLMLPEKDGLEVCREVRKTS---NVPI 72

                  ....*..
gi 636783241  911 IFLTSMD 917
Cdd:cd17614    73 IMLTAKD 79
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
830-959 2.46e-04

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: 41.88  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDgVAAEgGGTGLAILEAAADLGvtVDAVVLDYHMPDMNGADVARRLRA-DPrfvEL 908
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYE-VVGE-AANGEEAVEKYKELK--PDLVTMDITMPEMDGIEALKEIKKiDP---NA 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636783241  909 PIIFLTSMdisgtekefaalnGHAHLMKPARANVLRNTVVEVVRASRVKQA 959
Cdd:cd17542    75 KVIMCSAM-------------GQEEMVKEAIKAGAKDFIVKPFQPERVLEA 112
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1019-1105 2.63e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 44.49  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241 1019 NGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERekgqgHRVPIIGVTAhALESDRELCLDA---GMDDYMSKPI- 1094
Cdd:PRK12555   34 DGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAE-----RPCPILIVTS-LTERNASRVFEAmgaGALDAVDTPTl 107
                          90
                  ....*....|....*....
gi 636783241 1095 --------SPELLEEKIRQ 1105
Cdd:PRK12555  108 gigagleeYAAELLAKIDQ 126
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
831-947 2.91e-04

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: 41.80  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEaaadlGVTVDAVVLDYHMPDMNGADVARRLRAdpRFVELPI 910
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLS-----DQPPDVVLLDLKLPDMSGMEILKWIQE--RSLPTSV 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 636783241  911 IFLT---SMDISgtekeFAALNGHAH--LMKPARANVLRNTV 947
Cdd:cd17572    74 IVITahgSVDIA-----VEAMRLGAYdfLEKPFDADRLRVTV 110
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
831-978 3.15e-04

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 44.64  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEaaadlGVTVDAVVLDYHMPDMNGADVARRLRA-DPrfvELP 909
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVR-----EQVFDLVLCDVRMAEMDGIATLKEIKAlNP---AIP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636783241  910 IIFLTSMDISGTEKEFAALNGHAHLMKPARANVLRNTVVEVVRASRVKQASEAEIARLQTEAAVPAPAL 978
Cdd:PRK10365   80 VLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAM 148
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
832-917 3.61e-04

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: 41.44  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  832 LVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAileaAADLGVtVDAVVLDYHMPDMNGADVARRLRADPrfVELPII 911
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLE----YALSGI-YDLIILDIMLPGMDGLEVLKSLREEG--IETPVL 73

                  ....*.
gi 636783241  912 FLTSMD 917
Cdd:cd17625    74 LLTALD 79
PAS_7 pfam12860
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
322-436 3.79e-04

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 432837 [Multi-domain]  Cd Length: 115  Bit Score: 41.37  E-value: 3.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   322 LRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDPFDGRPFIDVIRRNYELGRYdGTQTPEEIYDFRKHLFETEEPEPIE 401
Cdd:pfam12860    1 LENMSQGLSVFDADLRLVAWNRRYRELLDLPEDLVQVGVPFEEIIRYNAERGEY-GPGDVEAHVRRRLAAARAGSPHYFE 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 636783241   402 LGWAGGKSVIFDSRRISNDRILLTYADITAVRERE 436
Cdd:pfam12860   80 RERPDGRVIEIRGNPLPDGGFVTTFTDITERRRAE 114
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
708-809 4.58e-04

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


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 40.87  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  708 LVGNAVK--FTER---GHVFVDVGFETAaggeiMASIRIEDTGIGIPPEKLesvfDKFSQVDASSTrrhEGTGLGLA-IT 781
Cdd:cd16957     9 LVENAIRhaFPKRkenNEVRVVVKKDQH-----KVHVSVSDNGQGIPEERL----DLLGKTTVTSE---KGTGTALEnLN 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 636783241  782 AGLVDLFG--GYLNVDSEWGKGSVFTVNLP 809
Cdd:cd16957    77 RRLIGLFGseACLHIESEVHGGTEVWFVIP 106
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
831-937 5.14e-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: 40.86  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLaileaaaDLG--VTVDAVVLDYHMPDMNGADVARRLRADPrfVEL 908
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGL-------DLGklYDYDIILLDLNLPDMSGYEVLRTLRLAK--VKT 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 636783241  909 PIIFLTSMdiSGTEKEFAALNGHA--HLMKP 937
Cdd:cd17616    72 PILILSGL--ADIEDKVKGLGFGAddYMTKP 100
PAS_7 pfam12860
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
460-569 5.63e-04

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 432837 [Multi-domain]  Cd Length: 115  Bit Score: 40.60  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   460 MPQGLAIV-QDGIIRMSNEALSDILQIPATYLErgegwIGM-----FEYCAARGDF-HDAAAETLQGWRDNIAARLPIST 532
Cdd:pfam12860    4 MSQGLSVFdADLRLVAWNRRYRELLDLPEDLVQ-----VGVpfeeiIRYNAERGEYgPGDVEAHVRRRLAAARAGSPHYF 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 636783241   533 AFHVGGERWVNMDATVSRGQHWVALFTDVTELKSREE 569
Cdd:pfam12860   79 ERERPDGRVIEIRGNPLPDGGFVTTFTDITERRRAEE 115
PRK10336 PRK10336
two-component system response regulator QseB;
830-937 6.07e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 42.57  E-value: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgvtVDAVVLDYHMPDMNGADVARRLRADPRfvELP 909
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAP-----YDAVILDLTLPGMDGRDILREWREKGQ--REP 74
                          90       100
                  ....*....|....*....|....*...
gi 636783241  910 IIFLTSMDISGTEKEFAALNGHAHLMKP 937
Cdd:PRK10336   75 VLILTARDALAERVEGLRLGADDYLCKP 102
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
830-943 1.04e-03

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 40.05  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADlgvtvDAVVLDYHMPDMNGADVARRLRadpRFVELP 909
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKP-----DAVLLDIMLPGIDGLTLCRDLR---PKYQGP 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 636783241  910 IIFLTSMDISgtEKEFAALNGHA--HLMKPARANVL 943
Cdd:cd17622    74 ILLLTALDSD--IDHILGLELGAddYVVKPVEPAVL 107
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
830-947 1.09e-03

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 39.84  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAADlgvtvDAVVLDYHMPDMNGADVARRLRA-DPrfvEL 908
Cdd:cd17553     2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERP-----DLVLLDMKIPGMDGIEILKRMKViDE---NI 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 636783241  909 PIIFLTS---MDISGTEKEFAALnghAHLMKPARANVLRNTV 947
Cdd:cd17553    74 RVIIMTAygeLDMIQESKELGAL---THFAKPFDIDEIRDAV 112
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
830-939 1.28e-03

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: 39.70  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGtglailEAAADLGVTV--DAVVLDYHMPDMNGADVARRLRaDPRFVe 907
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYEVVGEASDG------EEAVELAKKHkpDLVIMDVKMPRLDGIEAAKIIT-SENIA- 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 636783241  908 lPIIFLTSMDISGTEKEFAALNGHAHLMKPAR 939
Cdd:cd19932    74 -PIVLLTAYSQQDLVERAKEAGAMAYLVKPFS 104
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
184-250 1.36e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 38.15  E-value: 1.36e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636783241    184 DLLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQENLLALE 250
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
988-1093 1.51e-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: 39.13  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  988 VDVLVAEDNEVnqivFTQILQgtglSFL----------VVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRERE 1057
Cdd:cd17561     2 IKVLIADDNRE----FVQLLE----EYLnsqpdmevvgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMR 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 636783241 1058 KgqGHRVPIIGVTAHALESDRELCLDAGMDDYMSKP 1093
Cdd:cd17561    74 L--EKRPKIIMLTAFGQEDITQRAVELGASYYILKP 107
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
316-441 1.52e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 39.32  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   316 RDIENILRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDPFdGRPFIDVIRRNYELGRYDgtqtpeeiyDFRKHLFETE 395
Cdd:pfam00989    1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVI-GKSLLDLIPEEDDAEVAE---------LLRQALLQGE 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 636783241   396 EPEPIELgwaggksvifdSRRISNDRILLTYADITAVREREKEIHE 441
Cdd:pfam00989   71 ESRGFEV-----------SFRVPDGRPRHVEVRASPVRDAGGEILG 105
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
990-1099 1.62e-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: 39.40  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRErekgQGHRVPIIGV 1069
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE----KYPDLPVIMI 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636783241 1070 TAH-----ALESDRElcldaGMDDYMSKPISPELL 1099
Cdd:cd17550    77 SGHgtietAVKATKL-----GAYDFIEKPLSLDRL 106
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
185-302 1.66e-03

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: 42.26  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  185 LLRTILEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYQEnllALEGGTSKEIEslLPSK 264
Cdd:COG5000    91 YLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLRE---ALERGWQEEIE--LTRD 165
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 636783241  265 DGHIYSVlsrvnRVVTADGRPYVVgSFSDISPLKEREK 302
Cdd:COG5000   166 GRRTLLV-----RASPLRDDGYVI-VFDDITELLRAER 197
PAS COG2202
PAS domain [Signal transduction mechanisms];
441-626 1.70e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 41.55  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  441 ETRAALERLGEMMRDATHAMPQGLAIV-QDGIIRMSNEALSDILQIPAtylergEGWIGMFEYCAARGDFHDAAAETLqg 519
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITdLDGRILYVNPAFERLTGYSA------EELLGKTLRDLLPPEDDDEFLELL-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  520 wRDNIAARLPISTAFHV----GGERWVNMDATVSRGQ-----HWVALFTDVTELKSREEELRQLLSRAEAADRAKSEFLA 590
Cdd:COG2202    73 -RAALAGGGVWRGELRNrrkdGSLFWVELSISPVRDEdgeitGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIF 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 636783241  591 NMSHEIRTPMNgVLGMAELLAKTNLDTRQKTFVDII 626
Cdd:COG2202   152 VLDLDGRILYV-NPAAEELLGYSPEELLGKSLLDLL 186
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
830-914 1.74e-03

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 39.18  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRAdpRFVELP 909
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASS-----QPDVLISDIRMPGMDGLALLAQIKQ--RHPDLP 74

                  ....*
gi 636783241  910 IIFLT 914
Cdd:cd19919    75 VIIMT 79
PRK10816 PRK10816
two-component system response regulator PhoP;
990-1093 2.41e-03

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 40.88  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNGEEAVAAWERYTPRIIMMDVSMPVMNGhqaTQTIReREKGQGHRVPIIGV 1069
Cdd:PRK10816    3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDG---LSLIR-RWRSNDVSLPILVL 78
                          90       100
                  ....*....|....*....|....
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSKP 1093
Cdd:PRK10816   79 TARESWQDKVEVLSAGADDYVTKP 102
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
690-809 2.44e-03

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 41.74  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  690 LPAAVigDAGRFRQIVTNLVGNAVKF---TERGHVFVDVgFETAAGGEIMasIRIEDTGIGIPPEKLESVFDKFSQVDAS 766
Cdd:PRK15053  424 LPPGL--DSTEFAAIVGNLLDNAFEAslrSDEGNKIVEL-FLSDEGDDVV--IEVADQGCGVPESLRDKIFEQGVSTRAD 498
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 636783241  767 STRRHegtGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:PRK15053  499 EPGEH---GIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
990-1096 2.45e-03

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: 38.89  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  990 VLVAEDNEVNQIVFTQILQGTGLSFLVVDNG-----------EEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIRE--- 1055
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGkraleflgledEEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKEssa 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 636783241 1056 -REkgqghrVPIIGVTAHALESDRELCLDAGMDDYMSKPISP 1096
Cdd:cd17581    81 lKE------IPVVIMSSENIPTRISRCLEEGAEDFLLKPVKL 116
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
829-901 2.55e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 40.78  E-value: 2.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636783241  829 ARILVVDDNEVNRRILTEQLSLWGFDGVAAEGGGTGLAILEAAAdlgVTVDAVVLDYHMPDMNGADVARRLRA 901
Cdd:PRK10651    7 ATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAES---LDPDLILLDLNMPGMNGLETLDKLRE 76
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
830-993 2.96e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 41.02  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLS-------LWgfdgVAAEGGgtgLAILEAAADlgvTVDAVVLDYHMPDMNGADVARRL-RA 901
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALArdpdhevVW----VATDGA---QAVERCAAQ---PPDVILMDLEMPRMDGVEATRRImAE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  902 DPrfveLPIIFLTSMDISGTEKEFAALnGHAHL---MKPA--RANVLRNTVVEVVRasRVKQASEAEIARLQTEAAVPAP 976
Cdd:PRK12555   72 RP----CPILIVTSLTERNASRVFEAM-GAGALdavDTPTlgIGAGLEEYAAELLA--KIDQIGRLLGRRLAPAAAPAAA 144
                         170
                  ....*....|....*..
gi 636783241  977 ALVPQKRAaefvDVLVA 993
Cdd:PRK12555  145 SAAPFRTT----PRLVA 157
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
318-346 3.47e-03

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 37.14  E-value: 3.47e-03
                           10        20
                   ....*....|....*....|....*....
gi 636783241   318 IENILRSLPVGVLILDNDHRILYVNDEFY 346
Cdd:pfam13188    3 LRALFESSPDGILVLDEGGRIIYVNPAAL 31
PRK15369 PRK15369
two component system response regulator;
830-914 4.05e-03

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 40.06  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFDGVAAEGGgTGLAILEAAADLgvTVDAVVLDYHMPDMNGADVARRLRAdpRFVELP 909
Cdd:PRK15369    5 KILLVDDHELIINGIKNMLAPYPRYKIVGQVD-NGLEVYNACRQL--EPDIVILDLGLPGMNGLDVIPQLHQ--RWPAMN 79

                  ....*
gi 636783241  910 IIFLT 914
Cdd:PRK15369   80 ILVLT 84
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
830-970 4.08e-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: 38.50  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDN----EVNRRILTEQlslwgFDGVAAEGGGTGLAILEAAadlgvTVDAVVLDYHMPDMNGADVARRLRAdpRF 905
Cdd:cd17596     2 TILVVDDEvrslEALRRTLEED-----FDVLTAASAEEALAILEEE-----WVQVILCDQRMPGTTGVEFLKEVRE--RW 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636783241  906 VELPIIFLTSMdiSGTEKEFAALNG---HAHLMKPARANVLRNTVVEVVRASRVKQaseaEIARLQTE 970
Cdd:cd17596    70 PEVVRIIISGY--TDSEDIIAGINEagiYQYLTKPWHPDQLLLTVRNAARLFELQR----ENERLSLE 131
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
653-811 4.22e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 40.37  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  653 LRKAAFDITEAVEDVATLLSSHAAEKNIELLVRA---APDLPAAVIGDAGRfrqIVTNLVGNAVKFTERGHVFVDVGFEt 729
Cdd:COG4585   115 LRPPALDDLGLAAALEELAERLLRAAGIRVELDVdgdPDRLPPEVELALYR---IVQEALTNALKHAGATRVTVTLEVD- 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  730 aaGGEImaSIRIEDTGIGIPPEKLEsvfdkfsqvdasstrrheGTGLGLAITAGLVDLFGGYLNVDSEWGKGSVFTVNLP 809
Cdd:COG4585   191 --DGEL--TLTVRDDGVGFDPEAAP------------------GGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLP 248

                  ..
gi 636783241  810 FA 811
Cdd:COG4585   249 LA 250
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
312-443 4.51e-03

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 40.91  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  312 ELLHRDIENILRSLPVGVLILDNDHRILYVNDEFYGIWELPLDDpFDGRPFIDVIrrnyelgrydgtqtPEEIYdfrKHL 391
Cdd:COG3829     7 KELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREE-VIGKNVTELI--------------PNSPL---LEV 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 636783241  392 FETEEPEPIELGWAGG--KSVIFDSRRISND----RILLTYADITAVREREKEIHETR 443
Cdd:COG3829    69 LKTGKPVTGVIQKTGGkgKTVIVTAIPIFEDgeviGAVETFRDITELKRLERKLREEE 126
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
830-915 6.16e-03

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: 37.74  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  830 RILVVDDNEVNRRILTEQLSLWGFD-GVAAEGGGTGLAILEAAADLgvtvdaVVLDYHMPDMNGADVARRLRadpRFVEL 908
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEvSVFTDGQRAVRRIIDEQPSL------VVLDIMLPGMDGLTVCREVR---EHSHV 71

                  ....*..
gi 636783241  909 PIIFLTS 915
Cdd:cd19939    72 PILMLTA 78
PRK14867 PRK14867
DNA topoisomerase VI subunit B; Provisional
694-812 6.80e-03

DNA topoisomerase VI subunit B; Provisional


Pssm-ID: 237841 [Multi-domain]  Cd Length: 659  Bit Score: 40.57  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  694 VIGDAGRFRQ---IVTNLVGNAVKFTERGHVFVDVGFETAAGGEIMASIRIEDTGIGIPPEKLESVFDKFsqVDASSTRR 770
Cdd:PRK14867   27 MLGYSGKLRSmttIIHELVTNSLDACEEAEILPDIKVEIEKLGSDHYKVAVEDNGPGIPPEFVPKVFGKM--LAGSKMHR 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 636783241  771 HEGTGLGLAITAGLVDLF-----GGYLNVDSEWGKGSVFTVNLPFAV 812
Cdd:PRK14867  105 LIQSRGQQGIGAAGVLLFsqittGKPLKITTSTGDGKIHEMEIKMSV 151
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
190-355 7.32e-03

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 40.52  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  190 LEDLPVAAFVRDEKHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPD----GGEAIYQENllalEGGTSK----EIESLL 261
Cdd:PRK11359   18 LEQNMMGAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrpaHPEYIRHNR----EGGKARvegmSRELQL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  262 PSKDG-HIYSVLSRVNrvVTADGRPYVVGSFSDISplKErekalIEAQKHKELLHRDIENILRSlpvgVLILDNDHRILY 340
Cdd:PRK11359   94 EKKDGsKIWTRFALSK--VSAEGKVYYLALVRDAS--VE-----MAQKEQTRQLIIAVDHLDRP----VIVLDPERRIVQ 160
                         170
                  ....*....|....*
gi 636783241  341 VNDEFYGIWELPLDD 355
Cdd:PRK11359  161 CNRAFTEMFGYCISE 175
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
991-1092 7.34e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 39.11  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  991 LVAEDNEVNQIVFTQILQGTGLSFLV-VDNGEEAVAAWERYTPRIIMMDVSMPVMNGHQATQTIREREKgQGhrvPIIGV 1069
Cdd:PRK09958    4 IIIDDHPLAIAAIRNLLIKNDIEILAeLTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQY-SG---IIIIV 79
                          90       100
                  ....*....|....*....|...
gi 636783241 1070 TAHALESDRELCLDAGMDDYMSK 1092
Cdd:PRK09958   80 SAKNDHFYGKHCADAGANGFVSK 102
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
831-937 8.05e-03

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: 37.10  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241  831 ILVVDDNEVNRRILTEQLSLWGFDgVAAEGGGTGLA--ILEAAADLgvtvdaVVLDYHMPDMNGADVARRL-RADPrfvE 907
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYE-VRTTGNAATLWrwVEEGEGDL------VITDVVMPDENGLDLIPRIkKARP---D 70
                          90       100       110
                  ....*....|....*....|....*....|
gi 636783241  908 LPIIFLTSMDISGTEKEFAALNGHAHLMKP 937
Cdd:cd19928    71 LPIIVMSAQNTLMTAVKAAERGAFEYLPKP 100
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
203-295 8.64e-03

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 36.67  E-value: 8.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636783241   203 KHRLVYANQYYETFSGHNRSRVLGMTEHEMFGPDGGEAIYqENLLAlEGGTSKEIESLLPSKDGHIYSVLSRVNRVVTAD 282
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERL-REALR-EGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
                           90
                   ....*....|....
gi 636783241   283 GR-PYVVGSFSDIS 295
Cdd:pfam13426   79 GElVGIIAILRDIT 92
 
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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