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Conserved domains on  [gi|499421692|ref|WP_011109156|]
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hybrid sensor histidine kinase/response regulator transcription factor [Bacteroides thetaiotaomicron]

Protein Classification

hybrid sensor histidine kinase/response regulator transcription factor( domain architecture ID 15525797)

two-component hybrid sensor histidine kinase/response regulator transcription factor containing a ligand-binding periplasmic sensor domain, a Y_Y_Y domain, and an AraC family helix-turn-helix (HTH) DNA-binding domain; receives the signal from the sensor partner in a two-component system through its receiver (REC) domain and functions as a protein kinase that phosphorylates a target protein in response to various signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
3-1160 1.83e-73

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


:

Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 265.31  E-value: 1.83e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692    3 NALLIFAFLSFYLSSVHASVEIRSNKLTTGDGLANNSIRYMFQDSKGFMWMGTVNGLSYYDGNSFVSIYPDPNLPISLAD 82
Cdd:COG3292     1 KRLLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   83 PRIRNMEEDSNGFLWIATLSSLySCYDLKHGRFvdftgcgeykQSYSKKIIASDQSIWlwdnnngcrrVVYQDGQfssqa 162
Cdd:COG3292    81 NYIRALLEDSDGRLWIGTDGGL-SRYDPKTDKF----------TRYPLDPGLPNNSIR----------SIAEDSD----- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  163 ykkelgnlssdkvlfvyesndspGHVWIGTKQGLWKYhdgkleamdtqgeswehifsydqytciitgkkeiyrhslsnnr 242
Cdd:COG3292   135 -----------------------GNIWVGTSNGLYRY------------------------------------------- 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  243 lekiasltelgdtgvitgslrlqhqwvmftatgsyilDPVTGKLRRFSRLNIKNGNVT---RDNKGNAWVhnytgnvwyv 319
Cdd:COG3292   149 -------------------------------------DPKTGKFKRFTLDGLPSNTITslaEDADGNLWV---------- 181
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  320 ntstgdikhfqflssehlgyidverysiihDSRDIIWITTYGNGLFAYDLNTGDLQHFTFEVSHSShINSNYLQYIIEDR 399
Cdd:COG3292   182 ------------------------------DSDGNLWIGTDGNGLYRLDPNTGKFEHITHDPDPNS-LSSNSIYSLFEDR 230
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  400 SGGIWVSSEFSGLSHLEiLNKGTLRIYPNGEDASDRSNTIRMLLRGKNGNVYManrmgtlyeydadlknilrrekfthnv 479
Cdd:COG3292   231 EGNLWVGTYGGGLNYLD-PNNSKFKSYRHNDPNGLSGNSVRSIAEDSDGNLWI--------------------------- 282
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  480 ysmcednegQLWLGMRGIGLrigadqwYRYNSK-------DNNSLSNDNVYLIYRDRKGRMWIGTFGGGLNLAVKTGNgy 552
Cdd:COG3292   283 ---------RLWIGTYGGGL-------FRLDPKtgkfkryNPNGLPSNSVYSILEDSDGNLWIGTSGGGLYRYDPKTG-- 344
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  553 QFKHF-FQDSYGEKRVRVIQEDRNGMMWVGTNNGIYIFHPDSliNSPKNYvLYNHVNETFPSNEIRCLVNDHEGNMWIGT 631
Cdd:COG3292   345 KFTKFsEDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKT--GKFTNF-THDPDKNGLSSNYINSIFEDSDGRLWIGT 421
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  632 TGAGFAICYPGNDyqhlTFDCYSIKDGLPNGVIQSIVEDQDNKMWIATEYgisrftlatkqIENYYFSSHTLGNVYSENT 711
Cdd:COG3292   422 DGGGLYRYDPKTG----KFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSA-----------SNLGLLSLLGGLLGGLNLG 486
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  712 ACINADGRLLFGTNYGLVVLDANKVENMEKLASTvftglhingahmlpgmddsPLNETMSYTGQLNLKHYQNSFVIAFST 791
Cdd:COG3292   487 NAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLT-------------------LLLLALLLLLSLLLLLLLLLLLLLLLL 547
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  792 FNFLSGASKYSYRMPPYDSEWSIPSAQNLATYRNLPPGKYQLQVKACNVAGVWGEESTMEIVIAPPFWQTTWAYLIYLVF 871
Cdd:COG3292   548 LLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLL 627
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  872 IGIVCYFSF--------HIIRKFNRLRNRIAVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRPLK 943
Cdd:COG3292   628 LLLLLILLLllllllllLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLLLALKLLLL 707
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  944 TMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVT 1023
Cdd:COG3292   708 LLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLELLLELALGLILLLKLLL 787
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1024 YNLLSNAFKYTPSNGKIIFKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQVHKGN 1103
Cdd:COG3292   788 LLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLLGLLLLLLLEILLLSLVE 867
                        1130      1140      1150      1160      1170
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1104 ISYDENEGGGSVFTVLLPTNSDIYQEKDFLIPNQLLTEEEEQHSKDFLRNETSEDTF 1160
Cdd:COG3292   868 LLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIELLLEEEVLLALI 924
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1169-1282 1.97e-39

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: 145.87  E-value: 1.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPI 1245
Cdd:COG0745     1 MPRILVVEDDPDIRELLAdalEREG--YEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:COG0745    77 IMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARI 113
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1277-1422 6.94e-27

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 111.41  E-value: 6.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1277 LLLARIFKLIELRDKLRQKYSNEPGLAHSIICTNDKDQKFSVKLNEVLNEHMTDTDFSVNDFAGIMGLGRTVFYKKVRGV 1356
Cdd:COG2207   113 LLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEE 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1357 TGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKKLSEDE 1422
Cdd:COG2207   193 TGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
3-1160 1.83e-73

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 265.31  E-value: 1.83e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692    3 NALLIFAFLSFYLSSVHASVEIRSNKLTTGDGLANNSIRYMFQDSKGFMWMGTVNGLSYYDGNSFVSIYPDPNLPISLAD 82
Cdd:COG3292     1 KRLLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   83 PRIRNMEEDSNGFLWIATLSSLySCYDLKHGRFvdftgcgeykQSYSKKIIASDQSIWlwdnnngcrrVVYQDGQfssqa 162
Cdd:COG3292    81 NYIRALLEDSDGRLWIGTDGGL-SRYDPKTDKF----------TRYPLDPGLPNNSIR----------SIAEDSD----- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  163 ykkelgnlssdkvlfvyesndspGHVWIGTKQGLWKYhdgkleamdtqgeswehifsydqytciitgkkeiyrhslsnnr 242
Cdd:COG3292   135 -----------------------GNIWVGTSNGLYRY------------------------------------------- 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  243 lekiasltelgdtgvitgslrlqhqwvmftatgsyilDPVTGKLRRFSRLNIKNGNVT---RDNKGNAWVhnytgnvwyv 319
Cdd:COG3292   149 -------------------------------------DPKTGKFKRFTLDGLPSNTITslaEDADGNLWV---------- 181
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  320 ntstgdikhfqflssehlgyidverysiihDSRDIIWITTYGNGLFAYDLNTGDLQHFTFEVSHSShINSNYLQYIIEDR 399
Cdd:COG3292   182 ------------------------------DSDGNLWIGTDGNGLYRLDPNTGKFEHITHDPDPNS-LSSNSIYSLFEDR 230
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  400 SGGIWVSSEFSGLSHLEiLNKGTLRIYPNGEDASDRSNTIRMLLRGKNGNVYManrmgtlyeydadlknilrrekfthnv 479
Cdd:COG3292   231 EGNLWVGTYGGGLNYLD-PNNSKFKSYRHNDPNGLSGNSVRSIAEDSDGNLWI--------------------------- 282
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  480 ysmcednegQLWLGMRGIGLrigadqwYRYNSK-------DNNSLSNDNVYLIYRDRKGRMWIGTFGGGLNLAVKTGNgy 552
Cdd:COG3292   283 ---------RLWIGTYGGGL-------FRLDPKtgkfkryNPNGLPSNSVYSILEDSDGNLWIGTSGGGLYRYDPKTG-- 344
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  553 QFKHF-FQDSYGEKRVRVIQEDRNGMMWVGTNNGIYIFHPDSliNSPKNYvLYNHVNETFPSNEIRCLVNDHEGNMWIGT 631
Cdd:COG3292   345 KFTKFsEDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKT--GKFTNF-THDPDKNGLSSNYINSIFEDSDGRLWIGT 421
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  632 TGAGFAICYPGNDyqhlTFDCYSIKDGLPNGVIQSIVEDQDNKMWIATEYgisrftlatkqIENYYFSSHTLGNVYSENT 711
Cdd:COG3292   422 DGGGLYRYDPKTG----KFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSA-----------SNLGLLSLLGGLLGGLNLG 486
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  712 ACINADGRLLFGTNYGLVVLDANKVENMEKLASTvftglhingahmlpgmddsPLNETMSYTGQLNLKHYQNSFVIAFST 791
Cdd:COG3292   487 NAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLT-------------------LLLLALLLLLSLLLLLLLLLLLLLLLL 547
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  792 FNFLSGASKYSYRMPPYDSEWSIPSAQNLATYRNLPPGKYQLQVKACNVAGVWGEESTMEIVIAPPFWQTTWAYLIYLVF 871
Cdd:COG3292   548 LLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLL 627
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  872 IGIVCYFSF--------HIIRKFNRLRNRIAVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRPLK 943
Cdd:COG3292   628 LLLLLILLLllllllllLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLLLALKLLLL 707
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  944 TMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVT 1023
Cdd:COG3292   708 LLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLELLLELALGLILLLKLLL 787
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1024 YNLLSNAFKYTPSNGKIIFKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQVHKGN 1103
Cdd:COG3292   788 LLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLLGLLLLLLLEILLLSLVE 867
                        1130      1140      1150      1160      1170
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1104 ISYDENEGGGSVFTVLLPTNSDIYQEKDFLIPNQLLTEEEEQHSKDFLRNETSEDTF 1160
Cdd:COG3292   868 LLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIELLLEEEVLLALI 924
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1169-1282 1.97e-39

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: 145.87  E-value: 1.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPI 1245
Cdd:COG0745     1 MPRILVVEDDPDIRELLAdalEREG--YEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:COG0745    77 IMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARI 113
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
894-1285 3.94e-38

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 154.71  E-value: 3.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  894 AVEKQLTEyKLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRpLKTMDKSTQRMLRLINQLLEFRKMQKNKLALS 973
Cdd:PRK11091  275 ALEKASRD-KTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY-LKTIHVSAITLGNIFNDIIDMDKMERRKLQLD 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  974 LEETDVIAFLYEI-FLSFKDTsESKNIDFSFEPSQP-AYKMFIDKGNLDKVTYNLLSNAFKYTPsNGKIIFKIdIQEDKQ 1051
Cdd:PRK11091  353 NQPIDFTDFLADLeNLSGLQA-EQKGLRFDLEPLLPlPHKVITDGTRLRQILWNLISNAVKFTQ-QGGVTVRV-RYEEGD 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1052 QLRIQVIDNGIGIPKEKRSELFKRFMQSSFSH-----SSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNsdi 1126
Cdd:PRK11091  430 MLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHggkpaTGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAP--- 506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1127 yqekdflipnqlLTEEEEqhskdflrnetsEDTFQPPVDPLNKRKVLIIED---DTDIREFLREEIGvyFEVEVAADGTS 1203
Cdd:PRK11091  507 ------------AVAEEV------------EDAFDEDDMPLPALNILLVEDielNVIVARSVLEKLG--NSVDVAMTGKE 560
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1204 GFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHI-PIILLTAlNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK11091  561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMI 639

                  ...
gi 499421692 1283 FKL 1285
Cdd:PRK11091  640 KKF 642
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
894-1335 8.02e-33

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: 138.37  E-value: 8.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   894 AVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLINIENPPkEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALS 973
Cdd:TIGR02956  455 AEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTS-QQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSIS 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   974 LEETDVIAFLYEIFLSFKDTSESKNIDFSFE-PSQ-PAYKMfIDKGNLDKVTYNLLSNAFKYTpSNGKIIFKIDIQEDKq 1051
Cdd:TIGR02956  534 PRPFDLNALLDDVHHLMVSRAQLKGIQLRLNiPEQlPNWWQ-GDGPRIRQVLINLVGNAIKFT-DRGSVVLRVSLNDDS- 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1052 QLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHL--THELVQVHKGNISYDENEGGGSVFTVLLPtnsdiyqe 1129
Cdd:TIGR02956  611 SLLFEVEDTGCGIAEEEQATLFDAFTQADGRRRSGGTGLGLaiSQRLVEAMDGELGVESELGVGSCFWFTLP-------- 682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1130 kdflipnqllteeeeqhskdFLRNETSEDTFQPPVDPLNKRKVLIIEDD---TDIREFLREEIGVyfEVEVAADGTSGFE 1206
Cdd:TIGR02956  683 --------------------LTRGKPAEDSATLTVIDLPPQRVLLVEDNevnQMVAQGFLTRLGH--KVTLAESGQSALE 740
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1207 KASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSH-IPIILLTALNIEEKYQEGIESGADAYITKPFNVSLL---LARI 1282
Cdd:TIGR02956  741 CFHQHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNeVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLtamIAVI 820
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 499421692  1283 FKLIELRDKLRQKYSNEPGLAHSIICTNDKDQK-FSVKLNE-VLNEHMTDTDFSV 1335
Cdd:TIGR02956  821 LAGGKSNTEAPVLSASPSFDSASVIENAQADDIpESNQASEfLLDEEQLQQDIEV 875
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
905-1121 1.08e-32

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 135.65  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  905 EFFTNISHEFRTPLT--------LIQGAlnklinIENPpkEM-QRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLE 975
Cdd:NF033092  374 EFVANVSHELRTPLTtmrsyleaLADGA------WKDP--ELaPRFLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKE 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  976 ETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIIFKIDiqEDKQQLRI 1055
Cdd:NF033092  446 WVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGTITFRLL--ETHNRIII 523
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1056 QVIDNGIGIPKEKRSELFKRF----------MQSSfshssvGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:NF033092  524 SISDQGLGIPKKDLDKIFDRFyrvdkarsrkMGGT------GLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLP 593
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1173-1272 1.33e-32

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 122.13  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1173 LIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILLT 1249
Cdd:cd17574     1 LVVEDDEEIAELLSdylEKEG--YEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLRE--KGSDIPIIMLT 76
                          90       100
                  ....*....|....*....|...
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKP 1272
Cdd:cd17574    77 AKDEEEDKVLGLELGADDYITKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1172-1283 3.99e-28

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 109.93  E-value: 3.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIILLTA 1250
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 499421692  1251 LNIEEKYQEGIESGADAYITKPFNVSLLLARIF 1283
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1014-1121 4.10e-27

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 106.96  E-value: 4.10e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   1014 IDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSV---GVGL 1090
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRI--TVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIggtGLGL 78
                            90       100       110
                    ....*....|....*....|....*....|.
gi 499421692   1091 HLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:smart00387   79 SIVKKLVELHGGEISVESEPGGGTTFTITLP 109
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1277-1422 6.94e-27

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 111.41  E-value: 6.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1277 LLLARIFKLIELRDKLRQKYSNEPGLAHSIICTNDKDQKFSVKLNEVLNEHMTDTDFSVNDFAGIMGLGRTVFYKKVRGV 1356
Cdd:COG2207   113 LLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEE 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1357 TGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKKLSEDE 1422
Cdd:COG2207   193 TGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
1019-1120 2.76e-25

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 101.53  E-value: 2.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTPSNGKIIfkIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLT--HEL 1096
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPGGTIE--ISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREGGGTGLGLAivRRI 78
                          90       100
                  ....*....|....*....|....
gi 499421692 1097 VQVHKGNISYDENEGGGSVFTVLL 1120
Cdd:cd00075    79 VEAHGGRITVESEPGGGTTFTVTL 102
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
1019-1121 3.04e-25

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: 101.68  E-value: 3.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1019 LDKVTYNLLSNAFKYTPSNGKIIFKIdiqEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQS-SFSHSSVGVGLHLTHELV 1097
Cdd:pfam02518    6 LRQVLSNLLDNALKHAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAdKRGGGGTGLGLSIVRKLV 82
                           90       100
                   ....*....|....*....|....
gi 499421692  1098 QVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:pfam02518   83 ELLGGTITVESEPGGGTTVTLTLP 106
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1332-1415 2.20e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 98.01  E-value: 2.20e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   1332 DFSVNDFAGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSP 1411
Cdd:smart00342    1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                    ....
gi 499421692   1412 SAYR 1415
Cdd:smart00342   81 SEYR 84
pleD PRK09581
response regulator PleD; Reviewed
1192-1307 6.46e-24

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 106.91  E-value: 6.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1192 YFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLTAL-NIEEKYQeGIESGADAYIT 1270
Cdd:PRK09581   26 YYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALdDPEDRVR-GLEAGADDFLT 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499421692 1271 KPFNVSLLLARI-----FKLI--ELRdkLRQKYSNEPGLAHSII 1307
Cdd:PRK09581  105 KPINDVALFARVksltrLKMVidELR--LRASTNAEIGVTALMI 146
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
1170-1282 9.00e-24

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: 101.25  E-value: 9.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1170 RKVLIIEDDTDIREFLREEI-GVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILL 1248
Cdd:TIGR02154    3 RRILVVEDEPAIRELIAYNLeKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPIIML 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 499421692  1249 TALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:TIGR02154   83 TARGEEEDRVRGLETGADDYITKPFSPRELLARI 116
HTH_18 pfam12833
Helix-turn-helix domain;
1339-1417 1.49e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 87.26  E-value: 1.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1339 AGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTE-DLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKK 1417
Cdd:pfam12833    2 AAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
886-1121 1.37e-18

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 90.66  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  886 FNRLRNriAVEKQlTEYKLEFFTNISHEFRTPLTLIQGALNKL------INIENPPKeMQRPLKTMDKstqrmlrLINQL 959
Cdd:NF012163  226 FNQLAS--TLEKN-EQMRRDFMADISHELRTPLAVLRAELEAIqdgirkFTPESLDS-LQAEVGTLTK-------LVDDL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  960 LEFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFE-PSQPAykMFIDKGNLDKVTYNLLSNAFKYTPSNG 1038
Cdd:NF012163  295 HDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSlPDSSL--VFGDRDRLMQLFNNLLENSLRYTDSGG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1039 KIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSV----GVGLHLTHELVQVHKGNISYDENEGGGS 1114
Cdd:NF012163  373 SL--HISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRAsggsGLGLAISLNIVQAHGGTLHAAHSPLGGL 450

                  ....*..
gi 499421692 1115 VFTVLLP 1121
Cdd:NF012163  451 RIVVTLP 457
resp_reg_YycF NF040534
response regulator YycF;
1170-1282 2.20e-16

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 80.15  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDD---TDIREFLREEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshiPII 1246
Cdd:NF040534    1 KKILVVDDEkpiADILEFNLKKEG--YEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKYDM---PII 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:NF040534   76 MLTAKDSEIDKVLGLELGADDYVTKPFSTRELIARV 111
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1171-1223 9.28e-10

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: 55.65  E-value: 9.28e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692   1171 KVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMP 1223
Cdd:smart00448    2 RILVVDDDPLLRELLKallEKEG--YEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
1355-1420 4.39e-09

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 59.22  E-value: 4.39e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1355 GVTGYSPYEYLRVMRMKKaaeMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKKLSE 1420
Cdd:PRK10572  225 GISVLRWREDQRISRAKL---LLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEE 287
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
906-1125 2.54e-08

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 58.11  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  906 FFTNISHEFRTPLTLIQGAlNKLINIENP--PKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIAFL 983
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMA-ADVIHDSRDdfDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLV 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  984 YEIFLSFKDTSESKNIDFSFE-PSQPAyKMFIDKGNLDKVTYNLLSNAFKYtpSNGKIIfKIDIQEDKQQLRIQVIDNGI 1062
Cdd:NF040691  353 RRVVDALRQLAERAGVELRVDaPGTPV-VAEVDPRRVERVLRNLVVNAIEH--GEGKPV-VVTVAQDDTAVAVTVRDHGV 428
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1063 GIPKEKRSELFKRFMQSSFSHS----SVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNSD 1125
Cdd:NF040691  429 GLKPGEVALVFDRFWRADPARArttgGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAG 495
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
3-1160 1.83e-73

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 265.31  E-value: 1.83e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692    3 NALLIFAFLSFYLSSVHASVEIRSNKLTTGDGLANNSIRYMFQDSKGFMWMGTVNGLSYYDGNSFVSIYPDPNLPISLAD 82
Cdd:COG3292     1 KRLLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   83 PRIRNMEEDSNGFLWIATLSSLySCYDLKHGRFvdftgcgeykQSYSKKIIASDQSIWlwdnnngcrrVVYQDGQfssqa 162
Cdd:COG3292    81 NYIRALLEDSDGRLWIGTDGGL-SRYDPKTDKF----------TRYPLDPGLPNNSIR----------SIAEDSD----- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  163 ykkelgnlssdkvlfvyesndspGHVWIGTKQGLWKYhdgkleamdtqgeswehifsydqytciitgkkeiyrhslsnnr 242
Cdd:COG3292   135 -----------------------GNIWVGTSNGLYRY------------------------------------------- 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  243 lekiasltelgdtgvitgslrlqhqwvmftatgsyilDPVTGKLRRFSRLNIKNGNVT---RDNKGNAWVhnytgnvwyv 319
Cdd:COG3292   149 -------------------------------------DPKTGKFKRFTLDGLPSNTITslaEDADGNLWV---------- 181
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  320 ntstgdikhfqflssehlgyidverysiihDSRDIIWITTYGNGLFAYDLNTGDLQHFTFEVSHSShINSNYLQYIIEDR 399
Cdd:COG3292   182 ------------------------------DSDGNLWIGTDGNGLYRLDPNTGKFEHITHDPDPNS-LSSNSIYSLFEDR 230
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  400 SGGIWVSSEFSGLSHLEiLNKGTLRIYPNGEDASDRSNTIRMLLRGKNGNVYManrmgtlyeydadlknilrrekfthnv 479
Cdd:COG3292   231 EGNLWVGTYGGGLNYLD-PNNSKFKSYRHNDPNGLSGNSVRSIAEDSDGNLWI--------------------------- 282
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  480 ysmcednegQLWLGMRGIGLrigadqwYRYNSK-------DNNSLSNDNVYLIYRDRKGRMWIGTFGGGLNLAVKTGNgy 552
Cdd:COG3292   283 ---------RLWIGTYGGGL-------FRLDPKtgkfkryNPNGLPSNSVYSILEDSDGNLWIGTSGGGLYRYDPKTG-- 344
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  553 QFKHF-FQDSYGEKRVRVIQEDRNGMMWVGTNNGIYIFHPDSliNSPKNYvLYNHVNETFPSNEIRCLVNDHEGNMWIGT 631
Cdd:COG3292   345 KFTKFsEDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKT--GKFTNF-THDPDKNGLSSNYINSIFEDSDGRLWIGT 421
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  632 TGAGFAICYPGNDyqhlTFDCYSIKDGLPNGVIQSIVEDQDNKMWIATEYgisrftlatkqIENYYFSSHTLGNVYSENT 711
Cdd:COG3292   422 DGGGLYRYDPKTG----KFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSA-----------SNLGLLSLLGGLLGGLNLG 486
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  712 ACINADGRLLFGTNYGLVVLDANKVENMEKLASTvftglhingahmlpgmddsPLNETMSYTGQLNLKHYQNSFVIAFST 791
Cdd:COG3292   487 NAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLT-------------------LLLLALLLLLSLLLLLLLLLLLLLLLL 547
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  792 FNFLSGASKYSYRMPPYDSEWSIPSAQNLATYRNLPPGKYQLQVKACNVAGVWGEESTMEIVIAPPFWQTTWAYLIYLVF 871
Cdd:COG3292   548 LLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLL 627
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  872 IGIVCYFSF--------HIIRKFNRLRNRIAVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRPLK 943
Cdd:COG3292   628 LLLLLILLLllllllllLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLLLALKLLLL 707
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  944 TMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVT 1023
Cdd:COG3292   708 LLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLELLLELALGLILLLKLLL 787
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1024 YNLLSNAFKYTPSNGKIIFKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQVHKGN 1103
Cdd:COG3292   788 LLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLLGLLLLLLLEILLLSLVE 867
                        1130      1140      1150      1160      1170
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1104 ISYDENEGGGSVFTVLLPTNSDIYQEKDFLIPNQLLTEEEEQHSKDFLRNETSEDTF 1160
Cdd:COG3292   868 LLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIELLLEEEVLLALI 924
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
888-1121 1.08e-65

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 222.47  E-value: 1.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  888 RLRNRIAVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLIN-IENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQ 966
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  967 KNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDI 1046
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTI--TISA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1047 QEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSS--VGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:COG2205   159 RREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEggTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLP 235
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
858-1121 5.69e-65

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 224.02  E-value: 5.69e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  858 FWQTTWAYLIYLVFIGIVCYFSFHIIRKFNRLRNRIAVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLIniENPPKE 937
Cdd:COG0642    65 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLL--EELDEE 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  938 MQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKG 1017
Cdd:COG0642   143 QREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPD 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1018 NLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQ--SSFSHSSVGVGLHLTHE 1095
Cdd:COG0642   223 RLRQVLLNLLSNAIKYTPEGGTV--TVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRtdPSRRGGGTGLGLAIVKR 300
                         250       260
                  ....*....|....*....|....*.
gi 499421692 1096 LVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:COG0642   301 IVELHGGTIEVESEPGKGTTFTVTLP 326
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
345-1243 1.25e-63

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 235.27  E-value: 1.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  345 YSIIHDSRDIIWITTYgNGLFAYDlntG-DLQHFTFEVSHSSHINSNYLQYIIEDRSGGIWVSSEfSGLShleILNKGTL 423
Cdd:COG3292    39 NSIAQDSDGFLWIGTE-DGLNRYD---GyEFKVFRHDPGDPNSLPSNYIRALLEDSDGRLWIGTD-GGLS---RYDPKTD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  424 RIYPNGEDASDRSNTIRMLLRGKNGNVYMANRMGtLYEYDAD---LKNILRREKFTHNVYSMCE--------DNEGQLWL 492
Cdd:COG3292   111 KFTRYPLDPGLPNNSIRSIAEDSDGNIWVGTSNG-LYRYDPKtgkFKRFTLDGLPSNTITSLAEdadgnlwvDSDGNLWI 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  493 GMRGIGL---RIGADQWYRY-NSKDNNSLSNDNVYLIYRDRKGRMWIGTFGGGLNLAVKTGNGYQ-FKHFFQDSYGEKRV 567
Cdd:COG3292   190 GTDGNGLyrlDPNTGKFEHItHDPDPNSLSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKsYRHNDPNGLSGNSV 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  568 RVIQEDRNG----MMWVGT-NNGIYIFHPDSlinspKNYVLYNhvNETFPSNEIRCLVNDHEGNMWIGTTGAGFAICYPG 642
Cdd:COG3292   270 RSIAEDSDGnlwiRLWIGTyGGGLFRLDPKT-----GKFKRYN--PNGLPSNSVYSILEDSDGNLWIGTSGGGLYRYDPK 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  643 NDyqhlTFDCYSIKDGLPNGVIQSIVEDQDNKMWIATEYGISRFTLATKQIENYYFSSHTLGNVYSE-NTACINADGRLL 721
Cdd:COG3292   343 TG----KFTKFSEDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKTGKFTNFTHDPDKNGLSSNYiNSIFEDSDGRLW 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  722 FGTN-YGLVVLDA--NKVENM---EKLASTVFTGLHINGAHMLpgmddsplnetmsytgqlnlkhyqnsFVIAFSTFNFL 795
Cdd:COG3292   419 IGTDgGGLYRYDPktGKFKHFttkDGLPSNTIYSILEDDNGNL--------------------------WNFNSASNLGL 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  796 SGASKYSYRMPPYDSEWSIPSAQNLATYRNLPPGKYQlqvkacNVAGVWGEESTMEIVIAPPFWQTTWAYLIYLVFIGIV 875
Cdd:COG3292   473 LSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINL------SLVRSLISLLTLLLLALLLLLSLLLLLLLLLLLLLLL 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  876 CYFSFHIIRKFNRLRNRIAVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRPLKT------MDKST 949
Cdd:COG3292   547 LLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLllllilLLLLL 626
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  950 QRMLRLINQLLEFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSN 1029
Cdd:COG3292   627 LLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLLLALKLLL 706
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1030 AFKYTPSNGKIIFKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQVHKGNISYDEN 1109
Cdd:COG3292   707 LLLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLELLLELALGLILLLKLL 786
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1110 EGGGSVFTVLLPTNSDIYQEKDFLIPNQLLTEEEEQHSKDFLRNETSEDTFQPPVDPLNKRKVLIIEDDTDIREFLREEI 1189
Cdd:COG3292   787 LLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLLGLLLLLLLEILLLSLV 866
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499421692 1190 GVYFEVE----VAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHI 1243
Cdd:COG3292   867 ELLLELLegiiLALDLLLGSLSLVILLGLNELLLAELEEIDALLIELLLEEEVLLALI 924
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
889-1125 1.82e-59

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 210.18  E-value: 1.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  889 LRNRIAVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLI-NIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQK 967
Cdd:COG5002   151 VERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLdGAADDPEERREYLEIILEEAERLSRLVNDLLDLSRLES 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  968 NKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQ 1047
Cdd:COG5002   231 GELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTI--TVSLR 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1048 EDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSS----VGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTN 1123
Cdd:COG5002   309 EEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRetggTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLA 388

                  ..
gi 499421692 1124 SD 1125
Cdd:COG5002   389 RE 390
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1169-1282 1.97e-39

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: 145.87  E-value: 1.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPI 1245
Cdd:COG0745     1 MPRILVVEDDPDIRELLAdalEREG--YEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:COG0745    77 IMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARI 113
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
894-1285 3.94e-38

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 154.71  E-value: 3.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  894 AVEKQLTEyKLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRpLKTMDKSTQRMLRLINQLLEFRKMQKNKLALS 973
Cdd:PRK11091  275 ALEKASRD-KTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY-LKTIHVSAITLGNIFNDIIDMDKMERRKLQLD 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  974 LEETDVIAFLYEI-FLSFKDTsESKNIDFSFEPSQP-AYKMFIDKGNLDKVTYNLLSNAFKYTPsNGKIIFKIdIQEDKQ 1051
Cdd:PRK11091  353 NQPIDFTDFLADLeNLSGLQA-EQKGLRFDLEPLLPlPHKVITDGTRLRQILWNLISNAVKFTQ-QGGVTVRV-RYEEGD 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1052 QLRIQVIDNGIGIPKEKRSELFKRFMQSSFSH-----SSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNsdi 1126
Cdd:PRK11091  430 MLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHggkpaTGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAP--- 506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1127 yqekdflipnqlLTEEEEqhskdflrnetsEDTFQPPVDPLNKRKVLIIED---DTDIREFLREEIGvyFEVEVAADGTS 1203
Cdd:PRK11091  507 ------------AVAEEV------------EDAFDEDDMPLPALNILLVEDielNVIVARSVLEKLG--NSVDVAMTGKE 560
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1204 GFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHI-PIILLTAlNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK11091  561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMI 639

                  ...
gi 499421692 1283 FKL 1285
Cdd:PRK11091  640 KKF 642
PRK15347 PRK15347
two component system sensor kinase;
903-1285 7.54e-38

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 154.41  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  903 KLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRpLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIAF 982
Cdd:PRK15347  398 KSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDL-ADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPL 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  983 LYEIFLSFKDTSESKNIDFS--FEPSQPAYkMFIDKGNLDKVTYNLLSNAFKYTPSnGKIIFKIDIQEdkQQLRIQVIDN 1060
Cdd:PRK15347  477 LDQAMLTIQGPAQSKSLTLRtfVGAHVPLY-LHLDSLRLRQILVNLLGNAVKFTET-GGIRLRVKRHE--QQLCFTVEDT 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1061 GIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNsDIYQEKDF-------- 1132
Cdd:PRK15347  553 GCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLN-EYAPPEPLkgelsapl 631
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1133 -LIPnQL----LTEEEEQHSKDFLRNETS-------------------EDTFQPPVDPLnKRKVLIIeDDTDIReflREE 1188
Cdd:PRK15347  632 aLHR-QLsawgITCQPGHQNPALLDPELAylpgrlydllqqiiqgapnEPVINLPLQPW-QLQILLV-DDVETN---RDI 705
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1189 IGVYF-----EVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTT--SHIPIILLTALNIEEKYQEGI 1261
Cdd:PRK15347  706 IGMMLvelgqQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNldPDCMIVALTANAAPEEIHRCK 785
                         410       420
                  ....*....|....*....|....*
gi 499421692 1262 ESGADAYITKPfnVSL-LLARIFKL 1285
Cdd:PRK15347  786 KAGMNHYLTKP--VTLaQLARALEL 808
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1169-1282 1.59e-37

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: 139.27  E-value: 1.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPI 1245
Cdd:COG3706     1 PARILVVDDDPTNRKLLRrllEAAG--YEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPI 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:COG3706    79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1166-1291 2.19e-36

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: 134.21  E-value: 2.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1166 PLNKRKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSH 1242
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRrllERLG--YEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 499421692 1243 IPIILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLIELRDK 1291
Cdd:COG0784    80 IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1169-1294 4.21e-36

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: 136.83  E-value: 4.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLREEIG-VYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIIL 1247
Cdd:COG3437     6 APTVLIVDDDPENLELLRQLLRtLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIF 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLIELRDKLRQ 1294
Cdd:COG3437    86 LTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRE 132
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
900-1285 1.05e-34

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 145.26  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  900 TEYKLEFFTNISHEFRTPLTLIQGALnKLINIENPPKEMQRPLKTMDKST-QRMLRLINQLLEFRKMQKNKLALSLEETD 978
Cdd:PRK09959  709 TVAKSQFLATMSHEIRTPISSIMGFL-ELLSGSGLSKEQRVEAISLAYATgQSLLGLIGEILDVDKIESGNYQLQPQWVD 787
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  979 VIAFLYEIFLSFKDTSESKNIDFSFEPSQP-AYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIIFK--IDIQEDKQQLRI 1055
Cdd:PRK09959  788 IPTLVQNTCHSFGAIAASKSIALSCSSTFPdHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTslGHIDDNHAVIKM 867
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1056 QVIDNGIGIPKEKRSELFKRFMQSSF--SHSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNsdiyqekdfl 1133
Cdd:PRK09959  868 TIMDSGSGLSQEEQQQLFKRYSQTSAgrQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVE---------- 937
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1134 IPNQLLTEEEEQhskdflrnetsedtfQPPVDPLNKRKVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYD 1212
Cdd:PRK09959  938 ISQQVATVEAKA---------------EQPITLPEKLSILIADDHPTNRLLLKRQLNLLgYDVDEATDGVQALHKVSMQH 1002
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421692 1213 ADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPIILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKL 1285
Cdd:PRK09959 1003 YDLLITDVNMPNMDGFELTRKLREQ--NSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
910-1125 1.65e-33

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 135.09  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  910 ISHEFRTPLTLIQGALNKLI-----NIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLalslEETDVIAFLY 984
Cdd:COG5000   208 IAHEIKNPLTPIQLSAERLRrkladKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQL----EPVDLNELLR 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  985 EIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGI 1064
Cdd:COG5000   284 EVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEI--EVSTRREDGRVRIEVSDNGPGI 361
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421692 1065 PKEKRSELFKRFmqssFSH--SSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNSD 1125
Cdd:COG5000   362 PEEVLERIFEPF----FTTkpKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEE 420
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
864-1122 4.01e-33

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


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 134.49  E-value: 4.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  864 AYLIYLVFIGIVCYFsFHIIRKFNRLRNRIAVEKQLTE-----YKL--EFFTNISHEFRTPLTLIQGALnKLINIENPPK 936
Cdd:COG5808   196 ALAIRKLIILVLISI-IFLLLQYNLLKRKTLLERVIQEintqkLELigTFAASTAHEIRNPLTSIKGFI-QLLQEKYPEL 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  937 EMQRPLKTMDKSTQRMLRLINQLLEFRKMQknklALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDK 1016
Cdd:COG5808   274 EDQKYFDIIQEEIQRINQIVSEFLVLGKPT----AKKLELDDLNELIEEILSIIDSEANLKNIRVEKQSLDEPLHIKCDK 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1017 GNLDKVTYNLLSNAFKYTPSNGKIIFKIDIQEDKQQlrIQVIDNGIGIPKEKRSELFKRFMQSsfSHSSVGVGLHLTHEL 1096
Cdd:COG5808   350 DRIKQVLLNLIKNAIEAMKEGGKLTISIENDDEKAV--IEVIDNGEGIPEDIIDEIFEPFVTT--KEGGTGLGLSVCKRI 425
                         250       260
                  ....*....|....*....|....*.
gi 499421692 1097 VQVHKGNISYDENEGGGSVFTVLLPT 1122
Cdd:COG5808   426 VEMHGGEIDIESEEGKGTTFTIRLPL 451
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
894-1335 8.02e-33

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: 138.37  E-value: 8.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   894 AVEKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLINIENPPkEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALS 973
Cdd:TIGR02956  455 AEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTS-QQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSIS 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   974 LEETDVIAFLYEIFLSFKDTSESKNIDFSFE-PSQ-PAYKMfIDKGNLDKVTYNLLSNAFKYTpSNGKIIFKIDIQEDKq 1051
Cdd:TIGR02956  534 PRPFDLNALLDDVHHLMVSRAQLKGIQLRLNiPEQlPNWWQ-GDGPRIRQVLINLVGNAIKFT-DRGSVVLRVSLNDDS- 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1052 QLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHL--THELVQVHKGNISYDENEGGGSVFTVLLPtnsdiyqe 1129
Cdd:TIGR02956  611 SLLFEVEDTGCGIAEEEQATLFDAFTQADGRRRSGGTGLGLaiSQRLVEAMDGELGVESELGVGSCFWFTLP-------- 682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1130 kdflipnqllteeeeqhskdFLRNETSEDTFQPPVDPLNKRKVLIIEDD---TDIREFLREEIGVyfEVEVAADGTSGFE 1206
Cdd:TIGR02956  683 --------------------LTRGKPAEDSATLTVIDLPPQRVLLVEDNevnQMVAQGFLTRLGH--KVTLAESGQSALE 740
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1207 KASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSH-IPIILLTALNIEEKYQEGIESGADAYITKPFNVSLL---LARI 1282
Cdd:TIGR02956  741 CFHQHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNeVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLtamIAVI 820
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 499421692  1283 FKLIELRDKLRQKYSNEPGLAHSIICTNDKDQK-FSVKLNE-VLNEHMTDTDFSV 1335
Cdd:TIGR02956  821 LAGGKSNTEAPVLSASPSFDSASVIENAQADDIpESNQASEfLLDEEQLQQDIEV 875
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
905-1121 1.08e-32

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 135.65  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  905 EFFTNISHEFRTPLT--------LIQGAlnklinIENPpkEM-QRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLE 975
Cdd:NF033092  374 EFVANVSHELRTPLTtmrsyleaLADGA------WKDP--ELaPRFLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKE 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  976 ETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIIFKIDiqEDKQQLRI 1055
Cdd:NF033092  446 WVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGTITFRLL--ETHNRIII 523
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1056 QVIDNGIGIPKEKRSELFKRF----------MQSSfshssvGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:NF033092  524 SISDQGLGIPKKDLDKIFDRFyrvdkarsrkMGGT------GLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLP 593
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
897-1120 1.10e-32

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


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 130.41  E-value: 1.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   897 KQLTEYKLEFFTNISHEFRTPLTLIQGALNKLI-NIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLE 975
Cdd:TIGR02966  108 RRLEQMRRDFVANVSHELRTPLTVLRGYLETLAdGPDEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDE 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   976 ETDVIAFLYEIFLSFKDTSESKNIDFSFEpSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRI 1055
Cdd:TIGR02966  188 PVDMPALLDHLRDEAEALSQGKNHQITFE-IDGGVDVLGDEDELRSAFSNLVSNAIKYTPEGGTI--TVRWRRDGGGAEF 264
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1056 QVIDNGIGIPKEKRSELFKRF--MQSSFSHSSVGVGLHLT---HELVQvHKGNISYDENEGGGSVFTVLL 1120
Cdd:TIGR02966  265 SVTDTGIGIAPEHLPRLTERFyrVDKSRSRDTGGTGLGLAivkHVLSR-HHARLEIESELGKGSTFSFIF 333
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1173-1272 1.33e-32

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 122.13  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1173 LIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILLT 1249
Cdd:cd17574     1 LVVEDDEEIAELLSdylEKEG--YEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLRE--KGSDIPIIMLT 76
                          90       100
                  ....*....|....*....|...
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKP 1272
Cdd:cd17574    77 AKDEEEDKVLGLELGADDYITKP 99
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1171-1273 6.19e-31

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: 117.60  E-value: 6.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGV-YFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLT 1249
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAeGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                          90       100
                  ....*....|....*....|....
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPF 1273
Cdd:cd17538    81 ALDDREDRIRGLEAGADDFLSKPI 104
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
904-1124 7.03e-30

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 125.67  E-value: 7.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  904 LEFFTNI-SHEFRTPLTLIQGALNKLIN--IENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMqkNKLALSLEETDVI 980
Cdd:COG4251   282 LEQFAYVaSHDLREPLRKISGFSQLLEEdyGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLN 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  981 AFLYEIFLSFKDTSESKNIDFSFEPSQPAYkmfIDKGNLDKVTYNLLSNAFKYTPSN--GKIifKIDIQEDKQQLRIQVI 1058
Cdd:COG4251   360 ELLEEVLEDLEPRIEERGAEIEVGPLPTVR---GDPTLLRQVFQNLISNAIKYSRPGepPRI--EIGAEREGGEWVFSVR 434
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421692 1059 DNGIGIPKEKRSELFKRF--MQSSFSHSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNS 1124
Cdd:COG4251   435 DNGIGIDPEYAEKIFEIFqrLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAP 502
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
909-1121 1.97e-29

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 121.49  E-value: 1.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  909 NISHEFRTPLTLIQGALnKLINIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQknklALSLEETDVIAFLYEIFL 988
Cdd:COG3852   141 GLAHEIRNPLTGIRGAA-QLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPR----PPEREPVNLHEVLERVLE 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  989 SFK-DTSESKNIDFSFEPSQPAykMFIDKGNLDKVTYNLLSNAFKYTPSNGKIIFK--------IDIQEDKQQLRIQVID 1059
Cdd:COG3852   216 LLRaEAPKNIRIVRDYDPSLPE--VLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRtrverqvtLGGLRPRLYVRIEVID 293
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421692 1060 NGIGIPKEKRSELFKRFmqssFS--HSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:COG3852   294 NGPGIPEEILDRIFEPF----FTtkEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLP 353
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
910-1121 1.15e-28

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 119.52  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  910 ISHEFRTPLTLIQGALN---KLINIENPPKEMQRPLKTMDKSTQRMLRLINQLLEF-RKMQknklaLSLEETDVIAFLYE 985
Cdd:COG4191   149 IAHEINNPLAAILGNAEllrRRLEDEPDPEELREALERILEGAERAAEIVRSLRAFsRRDE-----EEREPVDLNELIDE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  986 IFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTP--SNGKIifKIDIQEDKQQLRIQVIDNGIG 1063
Cdd:COG4191   224 ALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEegEGGRI--TISTRREGDYVVISVRDNGPG 301
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421692 1064 IPKEKRSELFKRFmqssFS----HSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:COG4191   302 IPPEVLERIFEPF----FTtkpvGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1173-1282 2.14e-28

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: 110.83  E-value: 2.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1173 LIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLT 1249
Cdd:cd19937     1 LVVDDEEDIVELLKynlEKEG--YEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLT 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd19937    79 AKGEEFDKVLGLELGADDYITKPFSPRELLARV 111
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1173-1272 3.19e-28

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: 109.62  E-value: 3.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1173 LIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIILLTAL 1251
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 499421692 1252 NIEEKYQEGIESGADAYITKP 1272
Cdd:cd00156    79 ADEEDAVRALELGADDYLVKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1168-1302 3.77e-28

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: 118.91  E-value: 3.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1168 NKRKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIP 1244
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKellERAG--YEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALD--PDLP 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499421692 1245 IILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLIELRdKLRQKYSNEPGL 1302
Cdd:COG2204    77 VILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERR-RLRRENAEDSGL 133
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1172-1283 3.99e-28

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 109.93  E-value: 3.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIILLTA 1250
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 499421692  1251 LNIEEKYQEGIESGADAYITKPFNVSLLLARIF 1283
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1171-1282 1.93e-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: 108.01  E-value: 1.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLT 1249
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17548    81 AYAMKGDREKILEAGCDGYISKPIDTREFLETV 113
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1014-1121 4.10e-27

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 106.96  E-value: 4.10e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   1014 IDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSV---GVGL 1090
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRI--TVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIggtGLGL 78
                            90       100       110
                    ....*....|....*....|....*....|.
gi 499421692   1091 HLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:smart00387   79 SIVKKLVELHGGEISVESEPGGGTTFTITLP 109
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1277-1422 6.94e-27

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 111.41  E-value: 6.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1277 LLLARIFKLIELRDKLRQKYSNEPGLAHSIICTNDKDQKFSVKLNEVLNEHMTDTDFSVNDFAGIMGLGRTVFYKKVRGV 1356
Cdd:COG2207   113 LLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEE 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1357 TGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKKLSEDE 1422
Cdd:COG2207   193 TGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1167-1294 7.97e-27

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 106.98  E-value: 7.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1167 LNKRKVLIIEDDTDIREFLR---EEIGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHI 1243
Cdd:COG4565     1 MKMIRVLIVEDDPMVAELLRrylERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARG--PDV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499421692 1244 PIILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLIELRDKLRQ 1294
Cdd:COG4565    79 DVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1172-1273 2.04e-26

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: 104.52  E-value: 2.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIeDDT--DIR---EFLREEigvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPII 1246
Cdd:cd19920     1 ILIV-DDVpdNLRllsELLRAA---GYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVI 76
                          90       100
                  ....*....|....*....|....*...
gi 499421692 1247 LLTALN-IEEKyQEGIESGADAYITKPF 1273
Cdd:cd19920    77 FLTALTdTEDK-VKGFELGAVDYITKPF 103
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1172-1286 3.34e-26

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 104.39  E-value: 3.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILLTA 1250
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEgYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1251 LNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:cd17627    79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1170-1282 4.24e-26

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: 104.25  E-value: 4.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPII 1246
Cdd:cd17618     1 RTILIVEDEPAIREMIAfnlERAG--FDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPII 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17618    79 MLTARGEEEDKVRGLEAGADDYITKPFSPRELVARI 114
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1169-1285 1.46e-25

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: 103.01  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLR---EEIGVYfEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPI 1245
Cdd:cd17552     1 SKRILVIDDEEDIREVVQaclEKLAGW-EVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPV 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKL 1285
Cdd:cd17552    80 ILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKL 119
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1171-1272 1.75e-25

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: 102.16  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIIL 1247
Cdd:COG4753     1 KVLIVDDEPLIREGLKrilEWEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELD--PDTKIII 78
                          90       100
                  ....*....|....*....|....*
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKP 1272
Cdd:COG4753    79 LSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
1019-1120 2.76e-25

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 101.53  E-value: 2.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTPSNGKIIfkIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLT--HEL 1096
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPGGTIE--ISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREGGGTGLGLAivRRI 78
                          90       100
                  ....*....|....*....|....
gi 499421692 1097 VQVHKGNISYDENEGGGSVFTVLL 1120
Cdd:cd00075    79 VEAHGGRITVESEPGGGTTFTVTL 102
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
1019-1121 3.04e-25

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: 101.68  E-value: 3.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1019 LDKVTYNLLSNAFKYTPSNGKIIFKIdiqEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQS-SFSHSSVGVGLHLTHELV 1097
Cdd:pfam02518    6 LRQVLSNLLDNALKHAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAdKRGGGGTGLGLSIVRKLV 82
                           90       100
                   ....*....|....*....|....
gi 499421692  1098 QVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:pfam02518   83 ELLGGTITVESEPGGGTTVTLTLP 106
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1172-1272 1.21e-24

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 99.44  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILL 1248
Cdd:cd19935     1 ILVVEDEKKLAEYLKkglTEEG--YAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLML 76
                          90       100
                  ....*....|....*....|....*
gi 499421692 1249 TAL-NIEEKYqEGIESGADAYITKP 1272
Cdd:cd19935    77 TARdSVEDRV-KGLDLGADDYLVKP 100
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
888-1124 1.68e-24

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 110.44  E-value: 1.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  888 RLRNRIAVEKQLTEYKlEFFTNISHEFRTPLTLIQGALnKLINIENPPKEMQRPLKTMDKSTQRMLRLINQLLEF---RK 964
Cdd:PRK11360  376 RLQRRVARQERLAALG-ELVAGVAHEIRNPLTAIRGYV-QIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFsrpRE 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  965 MQKNKLALSLEETDVIAFlyeiflsFKDTSESKNIDFS--FEPSQPAykMFIDKGNLDKVTYNLLSNAFKYTPSNGKIif 1042
Cdd:PRK11360  454 SQWQPVSLNALVEEVLQL-------FQTAGVQARVDFEteLDNELPP--IWADPELLKQVLLNILINAVQAISARGKI-- 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1043 KIDI-QEDKQQLRIQVIDNGIGIPKEKRSELFKRFmqssFSHSSVGVGLHLT--HELVQVHKGNISYDENEGGGSVFTVL 1119
Cdd:PRK11360  523 RIRTwQYSDGQVAVSIEDNGCGIDPELLKKIFDPF----FTTKAKGTGLGLAlsQRIINAHGGDIEVESEPGVGTTFTLY 598

                  ....*
gi 499421692 1120 LPTNS 1124
Cdd:PRK11360  599 LPINP 603
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1332-1415 2.20e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 98.01  E-value: 2.20e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   1332 DFSVNDFAGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSP 1411
Cdd:smart00342    1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                    ....
gi 499421692   1412 SAYR 1415
Cdd:smart00342   81 SEYR 84
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
1025-1121 2.37e-24

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: 99.10  E-value: 2.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1025 NLLSNAFKYTPSnGKIIFKI---DIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQ--SSFS--HSSVGVGLHLTHELV 1097
Cdd:cd16922     7 NLLGNAIKFTEE-GEVTLRVsleEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQadSSTTrkYGGTGLGLAISKKLV 85
                          90       100
                  ....*....|....*....|....
gi 499421692 1098 QVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16922    86 ELMGGDISVESEPGQGSTFTFTLP 109
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1169-1294 3.40e-24

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 98.71  E-value: 3.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIR----EFLREEigvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshIP 1244
Cdd:COG5803     2 MKKILIVDDQAGIRmllkEVLKKE---GYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPD--IP 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 499421692 1245 IILLTALNIEEKYQEGIESGADAYITKPFNvslllarifkLIELRDKLRQ 1294
Cdd:COG5803    77 VIMMTAYGELDMVEEAKELGAKGYFTKPFD----------IDELREAVNK 116
pleD PRK09581
response regulator PleD; Reviewed
1192-1307 6.46e-24

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 106.91  E-value: 6.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1192 YFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLTAL-NIEEKYQeGIESGADAYIT 1270
Cdd:PRK09581   26 YYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALdDPEDRVR-GLEAGADDFLT 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499421692 1271 KPFNVSLLLARI-----FKLI--ELRdkLRQKYSNEPGLAHSII 1307
Cdd:PRK09581  105 KPINDVALFARVksltrLKMVidELR--LRASTNAEIGVTALMI 146
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
1170-1282 9.00e-24

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: 101.25  E-value: 9.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1170 RKVLIIEDDTDIREFLREEI-GVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILL 1248
Cdd:TIGR02154    3 RRILVVEDEPAIRELIAYNLeKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPIIML 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 499421692  1249 TALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:TIGR02154   83 TARGEEEDRVRGLETGADDYITKPFSPRELLARI 116
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
903-1272 1.34e-23

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 108.40  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  903 KLEFFTNISHEFRTPLtliqgalNKLIN-----IENPPKEMQRP-LKTMDKSTQRMLRLINQLLEFRKMQKNKLAL---- 972
Cdd:PRK11107  293 KSEFLANMSHELRTPL-------NGVIGftrqtLKTPLTPTQRDyLQTIERSANNLLAIINDILDFSKLEAGKLVLenip 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  973 -SLEET--DVIAFLyeiflsfKDTSESKNIDFSF--EPSQPAYkmFI-DKGNLDKVTYNLLSNAFKYTPSnGKIIFKI-- 1044
Cdd:PRK11107  366 fSLRETldEVVTLL-------AHSAHEKGLELTLniDPDVPDN--VIgDPLRLQQIITNLVGNAIKFTES-GNIDILVel 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1045 -DIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQ--SSFS--HSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVL 1119
Cdd:PRK11107  436 rALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQadASISrrHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFH 515
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1120 LPTNSDIYQEKDFLI-------------PN--------QLLTE------------EEEQHSKDFL--------RNETSED 1158
Cdd:PRK11107  516 LPLDLNPNPIIDGLPtdclagkrllyvePNsaaaqatlDILSEtplevtysptlsQLPEAHYDILllglpvtfREPLTML 595
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1159 T------------------FQPPVD---------------PLNKRK---VLIIEDDTDIREFLREE-------------- 1188
Cdd:PRK11107  596 HerlakaksmtdflilalpCHEQVLaeqlkqdgadaclskPLSHTRllpALLEPCHHKQPPLLPPTdesrlpltvmavdd 675
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1189 -------IGVYFE-----VEVAADGTSGFEKASTYDADLIVCDVLMPGMNGF---EVTRKLKNEFTTshiPIILLTALNI 1253
Cdd:PRK11107  676 npanlklIGALLEeqvehVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIracELIRQLPHNQNT---PIIAVTAHAM 752
                         490
                  ....*....|....*....
gi 499421692 1254 EEKYQEGIESGADAYITKP 1272
Cdd:PRK11107  753 AGERERLLSAGMDDYLAKP 771
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1173-1286 2.38e-23

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: 96.52  E-value: 2.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1173 LIIEDDTDIRE----FLREEigvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKL-KNEFTTshiPIIL 1247
Cdd:cd17625     1 LVVEDEKDLSEaitkHLKKE---GYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLrEEGIET---PVLL 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:cd17625    75 LTALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1172-1286 2.59e-23

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: 96.20  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIG-VYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshIPIILLTA 1250
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSdAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--TPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1251 LNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:cd19934    79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALI 114
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1172-1282 4.76e-23

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: 95.47  E-value: 4.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILL 1248
Cdd:cd17598     1 ILIVEDSPTQAEQLKhilEEQG--YKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17598    79 TTLSDPRDVIRGLECGADNFITKPYDEKYLLSRI 112
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1172-1282 5.64e-23

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 95.45  E-value: 5.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttSHIPIILLTA 1250
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEgFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT---SQVPVLMLTA 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499421692 1251 LNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17623    78 RGDDIDRILGLELGADDYLPKPFNPRELVARI 109
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1172-1282 1.11e-22

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: 94.46  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKL-KNEFTTSHIPIIL 1247
Cdd:cd17546     1 VLVVDDNPVNRKVLKkllEKLG--YEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIrELEGGGRRTPIIA 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17546    79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1172-1282 1.79e-22

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: 93.73  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIILL 1248
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPDIEVvgeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRY--PDLKVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17535    79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112
PRK09303 PRK09303
histidine kinase;
912-1121 2.37e-22

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 100.80  E-value: 2.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  912 HEFRTPLTL-------IQGALNKLINiENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIAFLY 984
Cdd:PRK09303  160 HDLRTPLTAaslaletLELGQIDEDT-ELKPALIEQLQDQARRQLEEIERLITDLLEVGRTRWEALRFNPQKLDLGSLCQ 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  985 EIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIIFKIdIQEDKQQLRIQVIDNGIGI 1064
Cdd:PRK09303  239 EVILELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGGTITLSM-LHRTTQKVQVSICDTGPGI 317
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499421692 1065 PKEKRSELFK-RF-MQSSFSHSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:PRK09303  318 PEEEQERIFEdRVrLPRDEGTEGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLP 376
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
889-1121 3.19e-22

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 100.69  E-value: 3.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  889 LRNRIAVEKQLTEYKL--EFFTNI---SHEFRTPLTLIQGalnkLINIENppkemqrplktmdksTQRMLRLINQLLEFR 963
Cdd:COG3290   170 FRDRTELERLEEELEGvkELAEALraqRHDFRNHLHTISG----LLQLGE---------------YDEALEYIDEISEEL 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  964 KMQKNKLALSLEETDVIAFLyeifLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAF----KYTPSNGK 1039
Cdd:COG3290   231 QELIDSLLSRIGNPVLAALL----LGKAARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIeaveKLPEEERR 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1040 IifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSvGVGLHLTHELVQVHKGNISYDENEGGGSVFTVL 1119
Cdd:COG3290   307 V--ELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLGEGR-GLGLALVKQIVEKYGGTIEVESEEGEGTVFTVR 383

                  ..
gi 499421692 1120 LP 1121
Cdd:COG3290   384 LP 385
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1171-1282 3.85e-22

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: 92.89  E-value: 3.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIIL 1247
Cdd:cd17551     2 RILIVDDNPTNLLLLEallRSAG-YLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17551    81 ITADTDREVRLRALEAGATDFLTKPFDPVELLARV 115
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1170-1286 5.28e-22

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: 92.75  E-value: 5.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPII 1246
Cdd:cd17562     1 KKILAVDDSASIRQMVSftlRGAG--YEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPIL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:cd17562    79 MLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
910-1122 5.78e-22

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: 101.20  E-value: 5.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  910 ISHEFRTPLTLIQG---ALNKLINIENppkemQRPLKTMDKSTQRMLRLINQLLEFRKMQknklALSLEETDVIAFLYEI 986
Cdd:COG5809   277 IAHEIRNPLTSLKGfiqLLKDTIDEEQ-----KTYLDIMLSELDRIESIISEFLVLAKPQ----AIKYEPKDLNTLIEEV 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  987 FLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIIFKIDIQEDkQQLRIQVIDNGIGIPK 1066
Cdd:COG5809   348 IPLLQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIETKAEDD-DKVVISVTDEGCGIPE 426
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499421692 1067 EKRSELFKRFmqssFSHSSVGVGLHLTH--ELVQVHKGNISYDENEGGGSVFTVLLPT 1122
Cdd:COG5809   427 ERLKKLGEPF----YTTKEKGTGLGLMVsyKIIEEHGGKITVESEVGKGTTFSITLPI 480
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1172-1282 6.12e-22

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: 92.49  E-value: 6.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDD---TDIREFLREEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNeftTSHIPIILL 1248
Cdd:cd17614     1 ILVVDDEkpiSDILKFNLTKEG--YEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRK---TSNVPIIML 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17614    76 TAKDSEVDKVLGLELGADDYVTKPFSNRELLARV 109
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1171-1282 2.73e-21

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: 90.52  E-value: 2.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTD----IREFLREEigvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshiPII 1246
Cdd:cd17622     2 RILLVEDDPKlarlIADFLESH---GFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG---PIL 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17622    76 LLTALDSDIDHILGLELGADDYVVKPVEPAVLLARL 111
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1172-1282 2.89e-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: 2.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILL 1248
Cdd:cd17580     1 ILVVDDNEDAAEMLAlllELEG--AEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIAL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17580    79 TGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1171-1282 3.21e-21

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 90.22  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREF----LREEigvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttSHIPII 1246
Cdd:cd17626     2 RILVVDDDAALAEMigivLRGE---GFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE---SGVPIV 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17626    76 MLTAKSDTVDVVLGLESGADDYVAKPFKPKELVARI 111
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
898-1277 5.56e-21

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 100.05  E-value: 5.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  898 QLTEYKLEFFTNISHEFRTPLTLIQGALNkLINIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLEE- 976
Cdd:PRK10841  442 QASQSKSMFLATVSHELRTPLYGIIGNLD-LLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREf 520
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  977 --TDVIAFLYEIFLSF---KDTSESKNIdfsfEPSQPAYkMFIDKGNLDKVTYNLLSNAFKYTPSnGKIIFKIDIQEDkq 1051
Cdd:PRK10841  521 spREVINHITANYLPLvvkKRLGLYCFI----EPDVPVA-LNGDPMRLQQVISNLLSNAIKFTDT-GCIVLHVRVDGD-- 592
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1052 QLRIQVIDNGIGIPKEKRSELFKRFMQSSF---SHSS-VGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP------ 1121
Cdd:PRK10841  593 YLSFRVRDTGVGIPAKEVVRLFDPFFQVGTgvqRNFQgTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPlygaqy 672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1122 ----TNSDIYQEKDFL-IPNQLLteeeEQHSKDFLRN-----------ETSED----TFQPPVDPLNKR----------- 1170
Cdd:PRK10841  673 pqkkGVEGLQGKRCWLaVRNASL----EQFLETLLQRsgiqvqryegqEPTPEdvliTDDPVQKKWQGRavitfcrrhig 748
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 ------------------------------------------------------KVLIIEDDTDIREFLREEIG-VYFEV 1195
Cdd:PRK10841  749 ipleiapgewvhstatphelpallariyrielesddsanalpstdkavsdnddmMILVVDDHPINRRLLADQLGsLGYQC 828
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1196 EVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshIPIILLTALNIEEKYQEGIESGADAYITKPfnV 1275
Cdd:PRK10841  829 KTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLT--LPVIGVTANALAEEKQRCLEAGMDSCLSKP--V 904

                  ..
gi 499421692 1276 SL 1277
Cdd:PRK10841  905 TL 906
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1171-1286 6.05e-21

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: 89.72  E-value: 6.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEI---GvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPIIL 1247
Cdd:cd17615     1 RVLVVDDEPNITELLSMALryeG--WDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLF 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1248 LTALN-IEEKYQeGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:cd17615    77 LTAKDsVEDRIA-GLTAGGDDYVTKPFSLEEVVARLRALL 115
HTH_18 pfam12833
Helix-turn-helix domain;
1339-1417 1.49e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 87.26  E-value: 1.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1339 AGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTE-DLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKK 1417
Cdd:pfam12833    2 AAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1170-1285 4.12e-20

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: 86.89  E-value: 4.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLREEI---GvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPII 1246
Cdd:cd17554     1 KKILVVDDEENIRELYKEELedeG--YEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK--KPDLPVI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1247 LLTALNieeKYQEGIES-GADAYITKPFNVSLLLARIFKL 1285
Cdd:cd17554    77 ICTAYS---EYKSDFSSwAADAYVVKSSDLTELKETIKRL 113
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
897-1121 8.42e-20

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 93.92  E-value: 8.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  897 KQLTEYKLEFFTNISHEFRTPLTLIQGALNKLIN--IENPPKEmqRPLKTMDKSTQRMLRLINQLLEFRKMQKNKlALSL 974
Cdd:PRK11006  198 HQLEGARRNFFANVSHELRTPLTVLQGYLEMMQDqpLEGALRE--KALHTMREQTQRMEGLVKQLLTLSKIEAAP-TIDL 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  975 EET-DVIAFLyEIFLSFKDTSESKNIDFSFEpSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQL 1053
Cdd:PRK11006  275 NEKvDVPMML-RVLEREAQTLSQGKHTITFE-VDNSLKVFGNEDQLRSAISNLVYNAVNHTPEGTHI--TVRWQRVPQGA 350
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421692 1054 RIQVIDNGIGIPKEKRSELFKRFMQSSFSHSS----VGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:PRK11006  351 EFSVEDNGPGIAPEHIPRLTERFYRVDKARSRqtggSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
912-1122 1.05e-19

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 94.14  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  912 HEFRTPLTLIQGALnKLINIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQkNKLALS-LEETDVIAFLYEIFLSF 990
Cdd:PRK11100  265 HELKSPLAAIRGAA-ELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLE-QRQELEvLEPVALAALLEELVEAR 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  991 KDTSESKNIDFSFEPsqPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRS 1070
Cdd:PRK11100  343 EAQAAAKGITLRLRP--DDARVLGDPFLLRQALGNLLDNAIDFSPEGGTI--TLSAEVDGEQVALSVEDQGPGIPDYALP 418
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499421692 1071 ELFKRFmqssFS-------HSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPT 1122
Cdd:PRK11100  419 RIFERF----YSlprpangRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
1015-1121 1.76e-19

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 85.24  E-value: 1.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1015 DKGNLDKVTYNLLSNAFKYTPSNGKIIFKIDIQeDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHS----SVGVGL 1090
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKF-RLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTrahgGTGLGL 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 499421692 1091 HLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16925    80 SIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
886-1130 1.80e-19

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 93.46  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  886 FNRLRNriAVEkQLTEYKLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRplktMDKSTQRMLRLINQLLEFRKM 965
Cdd:PRK09470  229 FNQMVT--ALE-RMMTSQQRLLSDISHELRTPLTRLQLATALLRRRQGESKELER----IETEAQRLDSMINDLLVLSRN 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  966 QKNkLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYtpSNGKIifKID 1045
Cdd:PRK09470  302 QQK-NHLERETFKANSLWSEVLEDAKFEAEQMGKSLTVSAPPGPWPINGNPNALASALENIVRNALRY--SHTKI--EVA 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1046 IQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFS---HS-SVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:PRK09470  377 FSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEArdrESgGTGLGLAIVENAIQQHRGWVKAEDSPLGGLRLTIWLP 456

                  ....*....
gi 499421692 1122 tnsdIYQEK 1130
Cdd:PRK09470  457 ----LYKRS 461
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1171-1286 1.82e-19

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 88.83  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLRE---EIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIIL 1247
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKgltEAG--FVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:PRK09836   78 LTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL 116
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1172-1272 2.13e-19

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: 84.74  E-value: 2.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILL 1248
Cdd:cd19927     1 ILLVDDDPGIRLAVKdylEDQG--FTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFL 78
                          90       100
                  ....*....|....*....|....
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKP 1272
Cdd:cd19927    79 TAKGMTSDRIKGYNAGCDGYLSKP 102
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1169-1294 2.47e-19

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: 87.70  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLRE---EIGvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttSHIPI 1245
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREglrEAG-YEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEE---RPAPV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLL-------LARIFKLIELRDKLRQ 1294
Cdd:COG3707    79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLlpalelaLARFRELRALRRELAK 134
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1171-1282 3.81e-19

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: 84.35  E-value: 3.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREE-IGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttsHIPIILLT 1249
Cdd:cd19939     1 RILIVEDELELARLTRDYlIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS---HVPILMLT 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd19939    78 ARTEEMDRVLGLEMGADDYLCKPFSPRELLARV 110
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1172-1287 3.88e-19

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: 84.31  E-value: 3.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR-----EEIGVYfEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPII 1246
Cdd:cd17536     1 VLIVDDEPLIREGLKklidwEELGFE-VVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELY--PDIKII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499421692 1247 LLTALNiEEKY-QEGIESGADAYITKPFNVSLLLARIFKLIE 1287
Cdd:cd17536    78 ILSGYD-DFEYaQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1171-1285 7.47e-19

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: 83.54  E-value: 7.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIIL 1247
Cdd:cd19923     2 KVLVVDDFSTMRRIIKnllKELG-FNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKL 1285
Cdd:cd19923    81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKI 118
orf27 CHL00148
Ycf27; Reviewed
1168-1334 8.87e-19

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 87.08  E-value: 8.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1168 NKRKVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttSHIPII 1246
Cdd:CHL00148    5 SKEKILVVDDEAYIRKILETRLSIIgYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE---SDVPII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLIELRDKLRQKYSN-EPGLAHSIICTNDKDQKFSVKLNEVLn 1325
Cdd:CHL00148   82 MLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNKKSFSSKIpNSSIIRIGFLKIDLNKKQVYKNNERI- 160

                  ....*....
gi 499421692 1326 eHMTDTDFS 1334
Cdd:CHL00148  161 -RLTGMEFS 168
PRK11517 PRK11517
DNA-binding response regulator HprR;
1171-1294 1.25e-18

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 86.49  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLRE---EIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKnefTTSHIPIIL 1247
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQglsEAG--YVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR---TAKQTPVIC 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARIfklielRDKLRQ 1294
Cdd:PRK11517   77 LTARDSVDDRVRGLDSGANDYLVKPFSFSELLARV------RAQLRQ 117
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
886-1121 1.37e-18

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 90.66  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  886 FNRLRNriAVEKQlTEYKLEFFTNISHEFRTPLTLIQGALNKL------INIENPPKeMQRPLKTMDKstqrmlrLINQL 959
Cdd:NF012163  226 FNQLAS--TLEKN-EQMRRDFMADISHELRTPLAVLRAELEAIqdgirkFTPESLDS-LQAEVGTLTK-------LVDDL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  960 LEFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFE-PSQPAykMFIDKGNLDKVTYNLLSNAFKYTPSNG 1038
Cdd:NF012163  295 HDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSlPDSSL--VFGDRDRLMQLFNNLLENSLRYTDSGG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1039 KIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSV----GVGLHLTHELVQVHKGNISYDENEGGGS 1114
Cdd:NF012163  373 SL--HISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRAsggsGLGLAISLNIVQAHGGTLHAAHSPLGGL 450

                  ....*..
gi 499421692 1115 VFTVLLP 1121
Cdd:NF012163  451 RIVVTLP 457
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1172-1282 1.76e-18

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: 82.33  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKnefTTSHIPIILLTA 1250
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWgYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR---QISNVPIIFISS 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499421692 1251 LNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd18159    78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKI 109
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1172-1282 2.65e-18

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: 81.76  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEI-GVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPIILLTA 1250
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLrKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQ--GQSLPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 499421692 1251 L-NIEEKYqEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17624    79 RdGVDDRV-AGLDAGADDYLVKPFALEELLARL 110
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1172-1272 2.72e-18

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: 81.44  E-value: 2.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKnefTTSHIPIILLTA 1250
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHgYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSA 77
                          90       100
                  ....*....|....*....|..
gi 499421692 1251 LNIEEKYQEGIESGADAYITKP 1272
Cdd:cd17620    78 RDEESDKIAALDAGADDYLTKP 99
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1171-1324 3.04e-18

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 85.64  E-value: 3.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIIL 1247
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDLEVvgeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRE--LDPPPPIIF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1248 LTALniEEKYQEGIESGADAYITKPFNVSLLLARIFKLIELRDKLRQKYSNEPGLAHsiICTNDKDQKFSVKLNEVL 1324
Cdd:COG3279    81 TTAY--DEYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKDR--IFVKSGGKLVKIPLDDIL 153
ompR PRK09468
osmolarity response regulator; Provisional
1171-1301 5.98e-18

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 84.64  E-value: 5.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSgFEKASTYDA-DLIVCDVLMPGMNGFEVTRKLKNEftTSHIPII 1246
Cdd:PRK09468    7 KILVVDDDMRLRALLErylTEQG--FQVRSAANAEQ-MDRLLTRESfHLMVLDLMLPGEDGLSICRRLRSQ--NNPTPII 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIfklielRDKLRQKYSNEPG 1301
Cdd:PRK09468   82 MLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARI------RAVLRRQAPELPG 130
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1172-1281 1.04e-17

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: 80.12  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREeigvYFE-----VEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttSHIPII 1246
Cdd:cd17619     3 ILIVEDEPVTRATLKS----YFEqegydVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ---SEVGII 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLAR 1281
Cdd:cd17619    76 LVTGRDDEVDRIVGLEIGADDYVTKPFNPRELLVR 110
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1170-1282 1.14e-17

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 83.61  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIRE---FLREEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPII 1246
Cdd:PRK10161    3 RRILVVEDEAPIREmvcFVLEQNG--FQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVV 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK10161   81 MLTARGEEEDRVRGLETGADDYITKPFSPKELVARI 116
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
906-1121 1.17e-17

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: 87.83  E-value: 1.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   906 FFTNISHEFRTPLT-LI---QGALNKliniENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIA 981
Cdd:TIGR01386  244 FSADLAHELRTPLTnLLgqtQVALSQ----PRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAA 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   982 FLYEIFLSFKDTSE--SKNIDFSFEPSQPAykmfiDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVID 1059
Cdd:TIGR01386  320 ELAKVAEYFEPLAEerGVRIRVEGEGLVRG-----DPQMFRRAISNLLSNALRHTPDGGTI--TVRIERRSDEVRVSVSN 392
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692  1060 NGIGIPKEKRSELFKRFMQS----SFSHSSVGVGLHLTHELVQVHKGNISYdENEGGGSVFTVLLP 1121
Cdd:TIGR01386  393 PGPGIPPEHLSRLFDRFYRVdparSNSGEGTGLGLAIVRSIMEAHGGRASA-ESPDGKTRFILRFP 457
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1170-1274 1.33e-17

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: 80.14  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLR---EEIGvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPG-MNGFEVTRKLKNEFttsHIPI 1245
Cdd:cd17534     1 KKILIVEDEAIIALDLKeilESLG-YEVVGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREKF---DIPV 76
                          90       100
                  ....*....|....*....|....*....
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFN 1274
Cdd:cd17534    77 IFLTAYSDEETLERAKETNPYGYLVKPFN 105
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
886-1129 4.16e-17

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 85.84  E-value: 4.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  886 FNRLRNriAVEKQlTEYKLEFFTNISHEFRTPLTLIQGALNKLIN-IENPPKE----MQRPLKTMDKstqrmlrLINQLL 960
Cdd:PRK10549  226 FNQLAS--TLEKN-EQMRRDFMADISHELRTPLAVLRGELEAIQDgVRKFTPEsvasLQAEVGTLTK-------LVDDLH 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  961 EFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNI--DFSFEPSQPaykMFIDKGNLDKVTYNLLSNAFKYTPSNG 1038
Cdd:PRK10549  296 QLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLtlQLSLPDSAT---VFGDPDRLMQLFNNLLENSLRYTDSGG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1039 KIIfkIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRF--MQSSFSHSSVGVGLHLT--HELVQVHKGNISYDENEGGGS 1114
Cdd:PRK10549  373 SLH--ISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFyrTEGSRNRASGGSGLGLAicLNIVEAHNGRIIAAHSPFGGV 450
                         250
                  ....*....|....*
gi 499421692 1115 VFTVLLPTNSDIYQE 1129
Cdd:PRK10549  451 SITVELPLERDLQRE 465
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1171-1274 4.43e-17

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: 79.00  E-value: 4.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDD-TDIREFLR--EEIGVYFEVEVAADG---------TSGFEKASTydADLIVCDVLMPGMNGFEVTRKLKNEF 1238
Cdd:cd17557     1 TILLVEDNpGDAELIQEafKEAGVPNELHVVRDGeealdflrgEGEYADAPR--PDLILLDLNMPRMDGFEVLREIKADP 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1239 TTSHIPIILLTALNIEEKYQEGIESGADAYITKPFN 1274
Cdd:cd17557    79 DLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVD 114
PRK10604 PRK10604
sensor protein RstB; Provisional
880-1126 4.92e-17

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 85.43  E-value: 4.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  880 FHIIRKFNRLRNRI----AVEKQLTEyklefftNISHEFRTPLTLIQGALNKLINI-ENPPKEMQRPLKTMDKstqrmlr 954
Cdd:PRK10604  192 ERLGVAFNQMADNInaliASKKQLID-------GIAHELRTPLVRLRYRLEMSDNLsAAESQALNRDIGQLEA------- 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  955 LINQLLEFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFsfEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYt 1034
Cdd:PRK10604  258 LIEELLTYARLDRPQNELHLSEPDLPAWLSTHLADIQAVTPEKTVRL--DTPHQGDYGALDMRLMERVLDNLLNNALRY- 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1035 pSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQ--SSFSHSSVGVGLHLT--HELVQVHKGNISYDENE 1110
Cdd:PRK10604  335 -AHSRV--RVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRldPSRDRATGGCGLGLAivHSIALAMGGSVNCDESE 411
                         250
                  ....*....|....*.
gi 499421692 1111 GGGSVFTVLLPTNSDI 1126
Cdd:PRK10604  412 LGGARFSFSWPVWHNL 427
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1172-1272 5.61e-17

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: 78.19  E-value: 5.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIG-VYFEVEVAADGTSGFEK---------ASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTS 1241
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKnLGFEIAEAVDGEEALNKlenlakegnDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 499421692 1242 HIPIILLTALNIEEKYQEGIESGADAYITKP 1272
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1171-1293 1.54e-16

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: 77.05  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLRE------EIGVyfeVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshiP 1244
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRilesdpDIEV---VGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPT---P 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499421692 1245 IILLTALNIE--EKYQEGIESGADAYITKPFN-VSLLLARIFKliELRDKLR 1293
Cdd:cd17541    76 VVMVSSLTEEgaEITLEALELGAVDFIAKPSGgISLDLEEIAE--ELIEKIK 125
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
1330-1417 1.81e-16

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 82.13  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1330 DTDFSVNDFAGIMGLG-RTvFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFG 1408
Cdd:COG4977   224 EEPLSVDELARRAGMSpRT-LERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFG 302

                  ....*....
gi 499421692 1409 VSPSAYRKK 1417
Cdd:COG4977   303 VSPSAYRRR 311
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
910-1121 2.13e-16

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: 84.01  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  910 ISHEFRTPLTLIQGALNKL-INIENPPKEMQRPLKTMDkstqRMLRLINQLLEFRKMQ---KNKLALSLEETDVIAFLye 985
Cdd:COG5805   294 IAHEIRNPLTSIKGFLQLLqPGIEDKEEYFDIMLSELD----RIESIISEFLALAKPQavnKEKENINELIQDVVTLL-- 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  986 iflsfkdTSES--KNIDFSFEPSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIIfkIDIQEDKQQLRIQVIDNGIG 1063
Cdd:COG5805   368 -------ETEAilHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTIT--IHTEEEDNSVIIRVIDEGIG 438
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499421692 1064 IPKEKRSELFKRFMqsSFSHSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:COG5805   439 IPEERLKKLGEPFF--TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
PRK10490 PRK10490
sensor protein KdpD; Provisional
910-1121 2.14e-16

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 85.09  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  910 ISHEFRTPLTLIQGALNKL---INIENPPKEMQrplktMDKSTQRML---RLINQLLEFRKMQK-----NKLALSLEETd 978
Cdd:PRK10490  671 LSHDLRTPLTVLFGQAEILtldLASEGSPHARQ-----ASEIRQQVLnttRLVNNLLDMARIQSggfnlRKEWLTLEEV- 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  979 VIAFLY--EIFLSfkdtseSKNIDFSFepSQPAYKMFIDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQ 1056
Cdd:PRK10490  745 VGSALQmlEPGLS------GHPINLSL--PEPLTLIHVDGPLFERVLINLLENAVKYAGAQAEI--GIDAHVEGERLQLD 814
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421692 1057 VIDNGIGIPKEKRSELFKRFMQSSfSHSS---VGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:PRK10490  815 VWDNGPGIPPGQEQLIFDKFARGN-KESAipgVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLP 881
resp_reg_YycF NF040534
response regulator YycF;
1170-1282 2.20e-16

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 80.15  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDD---TDIREFLREEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshiPII 1246
Cdd:NF040534    1 KKILVVDDEkpiADILEFNLKKEG--YEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKYDM---PII 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:NF040534   76 MLTAKDSEIDKVLGLELGADDYVTKPFSTRELIARV 111
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
1172-1272 2.94e-16

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: 75.70  E-value: 2.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDD---TDIREFLREEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKnefTTSHIPIILL 1248
Cdd:cd17621     1 VLVVEDEesfSDPLAYLLRKEG--FEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMV 75
                          90       100
                  ....*....|....*....|....
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKP 1272
Cdd:cd17621    76 TAKDSEIDKVVGLELGADDYVTKP 99
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
859-1123 4.20e-16

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 82.91  E-value: 4.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  859 WQTTWAYLIYLVFIGIVCYFSFHIIRKFNRLRNRIAVEKQLTEyKLEFFTN----ISHEFRTPLTLIQGaLNKLINIENP 934
Cdd:PRK10364  190 QRNTLIILFALATVLLASLLAFFWYRRYLRSRQLLQDEMKRKE-KLVALGHlaagVAHEIRNPLSSIKG-LAKYFAERAP 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  935 PKEMQRPL-KTMDKSTQRMLRLINQLLEFRKMQKnklaLSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAYKMF 1013
Cdd:PRK10364  268 AGGEAHQLaQVMAKEADRLNRVVSELLELVKPTH----LALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLPEIQ 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1014 IDKGNLDKVTYNLLSNAFKYTPSNGKIIFKIdiQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSfsHSSVGVGLHLT 1093
Cdd:PRK10364  344 ADPDRLTQVLLNLYLNAIQAIGQHGVISVTA--SESGAGVKISVTDSGKGIAADQLEAIFTPYFTTK--AEGTGLGLAVV 419
                         250       260       270
                  ....*....|....*....|....*....|
gi 499421692 1094 HELVQVHKGNISYDENEGGGSVFTVLLPTN 1123
Cdd:PRK10364  420 HNIVEQHGGTIQVASQEGKGATFTLWLPVN 449
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1170-1285 4.78e-16

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: 75.39  E-value: 4.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLRE--EIGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKnEFtTSHIPIIL 1247
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDilTKAGYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIK-KI-DPNAKVIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKL 1285
Cdd:cd17542    79 CSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1172-1286 9.16e-16

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: 74.75  E-value: 9.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTD----IREFLREEigvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKneftTSHI--PI 1245
Cdd:cd17616     1 VLLIEDDSAtaqsIELMLKSE---GFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLR----LAKVktPI 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:cd17616    74 LILSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1171-1299 1.88e-15

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 77.15  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTyDADLIVCDVLMPGMNGFEVTRKLKNEFTTshiPIILLT 1249
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTHQT---PVIMLT 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPFNVSLLLARIfklielRDKLRQKYSNE 1299
Cdd:PRK10955   79 ARGSELDRVLGLELGADDYLPKPFNDRELVARI------RAILRRSHWSE 122
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1171-1282 2.20e-15

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: 73.57  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEI-GVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKnefTTSHIPIILLT 1249
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLrAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR---RFSDVPIIMVT 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd19938    78 ARVEEIDRLLGLELGADDYICKPYSPREVVARV 110
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1170-1282 3.15e-15

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 73.22  E-value: 3.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDT----DIREFLREEigVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttsHI-P 1244
Cdd:cd19932     1 VRVLIAEDEAlirmDLREMLEEA--GYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE----NIaP 74
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499421692 1245 IILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd19932    75 IVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
886-1121 3.55e-15

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 80.20  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  886 FNRLRNRIavEKQLTEyKLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKM 965
Cdd:PRK09835  248 FNHMIERI--EDVFTR-QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQA 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  966 QKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSQPAykMFIDKGNLDKVTYNLLSNAFKYTPSNGKIIfkID 1045
Cdd:PRK09835  325 DNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELRFVGDPCQ--VAGDPLMLRRAISNLLSNALRYTPAGEAIT--VR 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1046 IQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHS----SVGVGLHLTHELVQVHKGNISYdENEGGGSVFTVLLP 1121
Cdd:PRK09835  401 CQEVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQrkgeGSGIGLAIVKSIVVAHKGTVAV-TSDARGTRFVISLP 479
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1171-1272 4.49e-15

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: 72.62  E-value: 4.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDtdirEFLREEIGVY-----FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPI 1245
Cdd:cd17555     2 TILVIDDD----EVVRESIAAYledsgFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPV 75
                          90       100
                  ....*....|....*....|....*..
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKP 1272
Cdd:cd17555    76 IVVSGAGVMSDAVEALRLGAWDYLTKP 102
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
1169-1287 4.87e-15

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


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 76.76  E-value: 4.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1169 KRKVLIIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLkNEFTTSHIP- 1244
Cdd:TIGR02875    2 KIRIVIADDNKEFCNLLKEYLAAQPDMEVvgvAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKL-NEIELSARPr 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 499421692  1245 IILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLIE 1287
Cdd:TIGR02875   81 VIMLSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQLAW 123
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
852-1121 7.46e-15

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 78.37  E-value: 7.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  852 IVIAPPFWQTTWAY-----LIYLVFIGIVCYFsFHIIRKFNRLRNRIA-VEKQltEYKLEFFTNISHEFRTPLTLIQGAL 925
Cdd:COG5806   147 AIIFIADISELLDFilyfiIIQLLAMLIAVYL-IENLIENILLRKELQrAEKL--EVVSELAASIAHEVRNPLTVVRGFI 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  926 nKLINIENPPKEMQRP-LKTMDKSTQRMLRLINQLLEFRKMQ---KNKLALSLEETDVIAflyeIFLSFKDTsesKNIDF 1001
Cdd:COG5806   224 -QLLQEPELSDEKRKQyIRIALEELDRAEAIITDYLTFAKPQpekLEKIDVSEELEHVID----VLSPYANM---NNVEI 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1002 SFEPSQPAYkMFIDKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEkrsELfKRFMQSSF 1081
Cdd:COG5806   296 QTELEPGLY-IEGDRQKLQQCLINIIKNGIEAMPNGGTL--TIDVSIDKNKVIISIKDTGVGMTKE---QL-ERLGEPYF 368
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 499421692 1082 SHSSVGVGLHL--THELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:COG5806   369 STKEKGTGLGTmvSYRIIEAMNGTIRVESEVGKGTTFTITLP 410
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1024-1118 7.64e-15

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 72.05  E-value: 7.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1024 YNLLSNAFKYTPSNGKIIFKIDiQEDKQQLRIQviDNGIGIPKEKRSELFKRFMQSSFSHSS-VGVGLHLTHELVQVHKG 1102
Cdd:cd16940    19 RNLVDNAVRYSPQGSRVEIKLS-ADDGAVIRVE--DNGPGIDEEELEALFERFYRSDGQNYGgSGLGLSIVKRIVELHGG 95
                          90
                  ....*....|....*.
gi 499421692 1103 NISYDENEGGGSVFTV 1118
Cdd:cd16940    96 QIFLGNAQGGGLEAWV 111
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1172-1282 1.47e-14

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 74.46  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGV-YFEVEVAadgTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNeftTSHIPIIL 1247
Cdd:PRK10529    4 VLIVEDEQAIRRFLRtalEGDGMrVFEAETL---QRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQ---WSAIPVIV 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK10529   78 LSARSEESDKIAALDAGADDYLSKPFGIGELQARL 112
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
903-966 1.85e-14

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 69.16  E-value: 1.85e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421692   903 KLEFFTNISHEFRTPLTLIQGALnKLINIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQ 966
Cdd:pfam00512    2 KSEFLANLSHELRTPLTAIRGYL-ELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIE 64
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1172-1272 3.46e-14

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: 69.78  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttSHIPIILL 1248
Cdd:cd19936     1 IALVDDDRNILTSVSmalEAEG--FSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFL 75
                          90       100
                  ....*....|....*....|....
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKP 1272
Cdd:cd19936    76 TSKDDEIDEVFGLRMGADDYITKP 99
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1015-1121 3.60e-14

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: 69.80  E-value: 3.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1015 DKGNLDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRF--MQSSFSHSS--VGVGL 1090
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKL--RIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFyrVESSRNRASggSGLGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 499421692 1091 HLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16946    79 AICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
903-964 4.54e-14

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 68.01  E-value: 4.54e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421692  903 KLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRK 964
Cdd:cd00082     4 KGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
903-966 4.72e-14

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 67.98  E-value: 4.72e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421692    903 KLEFFTNISHEFRTPLTLIQGALNKLINIENPPKEmQRPLKTMDKSTQRMLRLINQLLEFRKMQ 966
Cdd:smart00388    2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQ-REYLETILREAERLLRLINDLLDLSRIE 64
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
996-1120 5.09e-14

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: 70.35  E-value: 5.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  996 SKNIDFSFEPSqPAYKMFIDKGNLDKVTYNLLSNAFKYtpSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKR 1075
Cdd:cd16954    16 RKGVSISLDIS-PELRFPGERNDLMELLGNLLDNACKW--CLEFV--EVTARQTDGGLHLIVDDDGPGVPESQRSKIFQR 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499421692 1076 FMQSSFSHSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLL 1120
Cdd:cd16954    91 GQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
901-1238 5.51e-14

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 77.25  E-value: 5.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  901 EYKLEFFTNISHEFRTPLTLIQGALNKLIniENPPKEMQRP-LKTMDKSTQRMLRLINQLLEFRKMQKNKLALSL-EETD 978
Cdd:PRK11466  442 QAKSAFLAAMSHEIRTPLYGILGTAQLLA--DNPALNAQRDdLRAITDSGESLLTILNDILDYSAIEAGGKNVSVsDEPF 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  979 VIAFLYEIFLSFKDTSESKN---IDFSFEPSQPAYKMFiDKGNLDKVTYNLLSNAFKYTpSNGKIIFKIDIqeDKQQLRI 1055
Cdd:PRK11466  520 EPRPLLESTLQLMSGRVKGRpirLATDIADDLPTALMG-DPRRIRQVITNLLSNALRFT-DEGSIVLRSRT--DGEQWLV 595
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1056 QVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPtnsdiyqekdflip 1135
Cdd:PRK11466  596 EVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLP-------------- 661
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1136 nqllteeeeqhskdfLRNET--SEDTFQPPVDpLNKRKVLIIEDDTDIREFLREEI---GVYFE-VEVAADGTSGFEKAS 1209
Cdd:PRK11466  662 ---------------LRVATapVPKTVNQAVR-LDGLRLLLIEDNPLTQRITAEMLntsGAQVVaVGNAAQALETLQNSE 725
                         330       340
                  ....*....|....*....|....*....
gi 499421692 1210 TYDADLIvcDVLMPGMNGFEVTRKLKNEF 1238
Cdd:PRK11466  726 PFAAALV--DFDLPDYDGITLARQLAQQY 752
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1171-1288 5.86e-14

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: 69.86  E-value: 5.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEK-ASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPII-- 1246
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHnFQVLEAANGQEALEVlEQHPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIgi 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499421692 1247 ------LLTAlnieeKYqegIESGADAYITKPFNVSLLLARIFKLIEL 1288
Cdd:cd17544    82 sasgdnALSA-----RF---IKAGANDFLTKPFLPEEFYCRVTQNLET 121
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1121 7.15e-14

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 68.99  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTPSNGKIIfkIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQ 1098
Cdd:cd16943     4 LNQVLLNLLVNAAQAMEGRGRIT--IRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGEGTGLGLSLSYRIIQ 81
                          90       100
                  ....*....|....*....|...
gi 499421692 1099 VHKGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16943    82 KHGGTIRVASVPGGGTRFTIILP 104
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1167-1282 1.11e-13

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 71.92  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1167 LNKRKVLIIEDDTDIREFLreeigVY------FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftT 1240
Cdd:PRK11083    1 MQQPTILLVEDEQAIADTL-----VYalqsegFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAF--H 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499421692 1241 SHIPIILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK11083   74 PALPVIFLTARSDEVDRLVGLEIGADDYVAKPFSPREVAARV 115
envZ PRK09467
osmolarity sensor protein; Provisional
882-1122 1.82e-13

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 74.18  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  882 IIRKFNRLRNRIaveKQLTEYKLEFFTNISHEFRTPLTLIQGAlnklinienppKEMQRP----LK-TMDKSTQRMLRLI 956
Cdd:PRK09467  211 VTRAFNQMAAGI---KQLEDDRTLLMAGVSHDLRTPLTRIRLA-----------TEMMSEedgyLAeSINKDIEECNAII 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  957 NQLLEF-RKMQKnklaLSLEETDVIAFLYEIFLSfkDTSESKNIDFSFEPSQPAYKMfidkgN---LDKVTYNLLSNAFK 1032
Cdd:PRK09467  277 EQFIDYlRTGQE----MPMEMADLNALLGEVIAA--ESGYEREIETALQPGPIEVPM-----NpiaIKRALANLVVNAAR 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1033 YtpSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLT--HELVQVHKGNISYDENE 1110
Cdd:PRK09467  346 Y--GNGWI--KVSSGTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSARGSSGTGLGLAivKRIVDQHNGKVELGNSE 421
                         250
                  ....*....|..
gi 499421692 1111 GGGSVFTVLLPT 1122
Cdd:PRK09467  422 EGGLSARAWLPL 433
PRK10766 PRK10766
two-component system response regulator TorR;
1171-1295 6.25e-13

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 69.68  E-value: 6.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREeigvYFE-----VEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNeftTSHIPI 1245
Cdd:PRK10766    4 HILVVEDEPVTRARLQG----YFEqegytVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS---RSTVGI 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKL---IELRDKLRQK 1295
Cdd:PRK10766   77 ILVTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLlwrISLARQAQPH 129
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1025-1121 7.44e-13

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: 66.16  E-value: 7.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1025 NLLSNAFKY---TPSNGKIIfKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMqSSFSHSSVGVGLHLTHELVQVHK 1101
Cdd:cd16915     7 NLIDNALDAlaaTGAPNKQV-EVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGV-STKGQGERGIGLALVRQSVERLG 84
                          90       100
                  ....*....|....*....|
gi 499421692 1102 GNISYDENEGGGSVFTVLLP 1121
Cdd:cd16915    85 GSITVESEPGGGTTFSIRIP 104
PRK10610 PRK10610
chemotaxis protein CheY;
1171-1287 9.93e-13

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 66.54  E-value: 9.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIIL 1247
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRnllKELG-FNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLM 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLIE 1287
Cdd:PRK10610   86 VTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
1172-1289 1.08e-12

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: 66.36  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLRE--EIGVyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILLT 1249
Cdd:cd17549     1 VLLVDDDADVREALQQtlELAG-FRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRE--LDPDLPVILIT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499421692 1250 -----ALNIeekyqEGIESGADAYITKPFNVSLLLARIFKLIELR 1289
Cdd:cd17549    78 ghgdvPMAV-----EAMRAGAYDFLEKPFDPERLLDVVRRALEKR 117
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1025-1122 1.21e-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: 65.42  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1025 NLLSNAFKYtpSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSS----VGVGLHLTHELVQVH 1100
Cdd:cd16949     7 NVLRNALRY--SPSKI--LLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDResggTGLGLAIAERAIEQH 82
                          90       100
                  ....*....|....*....|..
gi 499421692 1101 KGNISYDENEGGGSVFTVLLPT 1122
Cdd:cd16949    83 GGKIKASNRKPGGLRVRIWLPA 104
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1172-1282 1.67e-12

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: 65.31  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIRE---FLREEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILL 1248
Cdd:cd17537     3 VYVVDDDEAVRDslaFLLRSVG--LAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLA--RGSNIPIIFI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 499421692 1249 T-------ALnieekyqEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17537    79 TghgdvpmAV-------EAMKAGAVDFLEKPFRDQVLLDAI 112
PRK15479 PRK15479
transcriptional regulator TctD;
1171-1286 1.78e-12

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 68.21  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEI-GVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshIPIILLT 1249
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALvQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQT--LPVLLLT 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:PRK15479   80 ARSAVADRVKGLNVGADDYLPKPFELEELDARLRALL 116
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1170-1282 1.99e-12

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 67.25  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTtsHIPII 1246
Cdd:COG4567     5 RSLLLVDDDEAFARVLAralERRG--FEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDP--DARIV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499421692 1247 LLTAlnieekY------QEGIESGADAYITKPFNVSLLLARI 1282
Cdd:COG4567    81 VLTG------YasiataVEAIKLGADDYLAKPADADDLLAAL 116
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1026-1121 2.03e-12

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


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 65.00  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1026 LLSNAFKYTPSNGKIIfkIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSH---SSVGVGLHLTHELVQVHKG 1102
Cdd:cd16948    13 IVSNALKYSKQGGKIE--IYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGRnfqESTGMGLYLVKKLCDKLGH 90
                          90
                  ....*....|....*....
gi 499421692 1103 NISYDENEGGGSVFTVLLP 1121
Cdd:cd16948    91 KIDVESEVGEGTTFTITFP 109
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
886-1125 2.24e-12

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 70.38  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  886 FNRLRNRIAVEKQLTeykleffTNISHEFRTPLTLIQGALN---KLINIENPPKemqrpLKTMDkstqRMLRLINQLLEF 962
Cdd:PRK10755  127 VSRLTSTLDQERLFT-------ADVAHELRTPLAGIRLHLElleKQHHIDVAPL-----IARLD----QMMHTVEQLLQL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  963 -RKMQK----NKLALSLEEtDVIAFLYEIFLSFKDTSEsKNIDFSFEPSqpaykMFIDKGN---LDKVTYNLLSNAFKYT 1034
Cdd:PRK10755  191 aRAGQSfssgHYQTVKLLE-DVILPSQDELSEMLEQRQ-QTLLLPESAA-----DITVQGDatlLRLLLRNLVENAHRYS 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1035 PSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRF--MQSSFSHSsvGVGLHLTHELVQVHKGNISY-DENEG 1111
Cdd:PRK10755  264 PEGSTI--TIKLSQEDGGAVLAVEDEGPGIDESKCGELSKAFvrMDSRYGGI--GLGLSIVSRITQLHHGQFFLqNRQER 339
                         250
                  ....*....|....
gi 499421692 1112 GGSVFTVLLPTNSD 1125
Cdd:PRK10755  340 SGTRAWVWLPKAQN 353
Y_Y_Y pfam07495
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ...
796-854 3.08e-12

Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a family of two component regulators. However they are also found tandemly repeated in Swiss:Q891H4 without other signal conduction domains being present. It's named after the conserved tyrosines found in the alignment. The exact function is not known.


Pssm-ID: 400051 [Multi-domain]  Cd Length: 65  Bit Score: 63.14  E-value: 3.08e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   796 SGASKYSYRMPPYDSEWSIPSAQNLATYRNLPPGKYQLQVKACNVAGVWG-EESTMEIVI 854
Cdd:pfam07495    5 PENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSyDDASLNFTI 64
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1171-1282 4.89e-12

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: 64.00  E-value: 4.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKnefTTSHIPIILLT 1249
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERgFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR---ARSDVPIIIIS 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499421692 1250 A-LNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17594    78 GdRRDEIDRVVGLELGADDYLAKPFGLRELLARV 111
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1172-1294 5.54e-12

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: 66.28  E-value: 5.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIRE---FLREEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIILL 1248
Cdd:COG4566     2 VYIVDDDEAVRDslaFLLESAG--LRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARG--SPLPVIFL 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499421692 1249 TAlnieekyqEG--------IESGADAYITKPFNVSLLLARIFKLIELRDKLRQ 1294
Cdd:COG4566    78 TG--------HGdvpmavraMKAGAVDFLEKPFDDQALLDAVRRALARDRARRA 123
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1169-1310 6.07e-12

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 69.88  E-value: 6.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTShiPIIL 1247
Cdd:PRK11361    4 INRILIVDDEDNVRRMLSTAFALQgFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRT--PVIL 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNV---SLLLARIFKLIELRDK---LRQKYSNEPGLAHsiICTN 1310
Cdd:PRK11361   82 MTAYAEVETAVEALRCGAFDYVIKPFDLdelNLIVQRALQLQSMKKEirhLHQALSTSWQWGH--ILTN 148
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1172-1282 7.09e-12

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 66.59  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHipIILL 1248
Cdd:PRK10651    9 ILLIDDHPMLRTGVKQLISMAPDITVvgeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGR--IVVF 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK10651   87 SVSNHEEDVVTALKRGADGYLLKDMEPEDLLKAL 120
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1171-1275 7.69e-12

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 63.45  E-value: 7.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFL-REEIGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIILLT 1249
Cdd:cd19919     2 TVWIVDDDSSIRWVLeRALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRH--PDLPVIIMT 79
                          90       100
                  ....*....|....*....|....*.
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPFNV 1275
Cdd:cd19919    80 AHSDLDSAVSAYQGGAFEYLPKPFDI 105
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
1326-1416 8.93e-12

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 68.54  E-value: 8.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1326 EHMTDTDFSVNDFAGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEmLLTEDLTIAEVAYSVGINDPFYFSKCFKN 1405
Cdd:COG2169    94 EAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQ-LLQTGLSVTDAAYAAGFGSLSRFYEAFKK 172
                          90
                  ....*....|.
gi 499421692 1406 QFGVSPSAYRK 1416
Cdd:COG2169   173 LLGMTPSAYRR 183
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1170-1295 1.92e-11

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 65.61  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKnefTTSHIPIILL 1248
Cdd:PRK13856    2 KHVLVIDDDVAMRHLIVEYLTIHaFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLA---TKSDVPIIII 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499421692 1249 TALNIEEKYQE-GIESGADAYITKPFNVSLLLARIfklielRDKLRQK 1295
Cdd:PRK13856   79 SGDRLEEADKVvALELGATDFIAKPFGTREFLARI------RVALRVR 120
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
884-1121 2.06e-11

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: 68.62  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   884 RKFNRLRNRIaveKQLTEYKLEFFTNISHEFRTPLTLIQGALNKLiNIENPPKEMQRPLKTMDKSTQRMLRLINQLLEfr 963
Cdd:TIGR03785  469 RSFAQMVARL---RQYTHYLENMSSRLSHELRTPVAVVRSSLENL-ELQALEQEKQKYLERAREGTERLSMILNNMSE-- 542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692   964 kmqKNKLALSLEETDVIAF-----LYEIFLSFKDTSESK----NIDFSFEPSQPAYKMFIDKgnLDKvtynLLSNAFKYT 1034
Cdd:TIGR03785  543 ---ATRLEQAIQSAEVEDFdlsevLSGCMQGYQMTYPPQrfelNIPETPLVMRGSPELIAQM--LDK----LVDNAREFS 613
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  1035 PSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSV----GVGLHLTHELVQVHKGNIS-YDEN 1109
Cdd:TIGR03785  614 PEDGLI--EVGLSQNKSHALLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDqphlGLGLYIVRLIADFHQGRIQaENRQ 691
                          250
                   ....*....|..
gi 499421692  1110 EGGGSVFTVLLP 1121
Cdd:TIGR03785  692 QNDGVVFRISLP 703
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
1170-1280 2.14e-11

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: 62.07  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPII 1246
Cdd:cd17563     1 KSLLLVDDDEVFAERLAralERRG--FEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQ--PDARIV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1247 LLTAlnieekYQ------EGIESGADAYITKPFNVSLLLA 1280
Cdd:cd17563    77 VLTG------YAsiatavEAIKLGADDYLAKPADADEILA 110
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
1169-1273 4.45e-11

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: 61.09  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1169 KRKVLIIEDDTDIREFLREeigvYFE-------VEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTS 1241
Cdd:cd17561     1 KIKVLIADDNREFVQLLEE----YLNsqpdmevVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEK 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499421692 1242 HIPIILLTALNIEEKYQEGIESGADAYITKPF 1273
Cdd:cd17561    77 RPKIIMLTAFGQEDITQRAVELGASYYILKPF 108
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1121 5.55e-11

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: 60.54  E-value: 5.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYtpSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLT--HEL 1096
Cdd:cd16950     1 LKRVLSNLVDNALRY--GGGWV--EVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTSGTGLGLAivQRI 76
                          90       100
                  ....*....|....*....|....*
gi 499421692 1097 VQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16950    77 SDAHGGSLTLANRAGGGLCARIELP 101
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1025-1121 7.64e-11

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: 60.42  E-value: 7.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1025 NLLSNAFKYTPSNGKIIFKIDIQEDKQQLRIQVIDNGIGIPK---EKRSELFKRFMQSSFSHSSvGVGLHLTHELVQVHK 1101
Cdd:cd16921     7 NLLGNAIKFRRPRRPPRIEVGAEDVGEEWTFYVRDNGIGIDPeyaEKVFGIFQRLHSREEYEGT-GVGLAIVRKIIERHG 85
                          90       100
                  ....*....|....*....|
gi 499421692 1102 GNISYDENEGGGSVFTVLLP 1121
Cdd:cd16921    86 GRIWLESEPGEGTTFYFTLP 105
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1121 8.44e-11

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: 60.10  E-value: 8.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSN---AFKYTPSNGKIIFKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSfsHSSVGVGLHLTHE 1095
Cdd:cd16920     1 IQQVLINLVRNgieAMSEGGCERRELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTK--SEGLGMGLSICRS 78
                          90       100
                  ....*....|....*....|....*.
gi 499421692 1096 LVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16920    79 IIEAHGGRLSVESPAGGGATFQFTLP 104
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
1172-1287 8.53e-11

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: 60.59  E-value: 8.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIRE----FLREEiGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIIL 1247
Cdd:cd17550     1 ILIVDDEEDIREslsgILEDE-G--YEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKY--PDLPVIM 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 499421692 1248 L-------TALnieekyqEGIESGADAYITKPFNVSLLLARIFKLIE 1287
Cdd:cd17550    76 IsghgtieTAV-------KATKLGAYDFIEKPLSLDRLLLTIERALE 115
PRK11173 PRK11173
two-component response regulator; Provisional
1171-1274 9.06e-11

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 63.50  E-value: 9.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttSHIPIIL 1247
Cdd:PRK11173    5 HILIVEDELVTRNTLKsifEAEG--YDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQ---ANVALMF 79
                          90       100
                  ....*....|....*....|....*..
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFN 1274
Cdd:PRK11173   80 LTGRDNEVDKILGLEIGADDYITKPFN 106
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1121 1.49e-10

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: 59.37  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTPSNgkiiFKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRF--MQSSFSHSS--VGVGLHLTH 1094
Cdd:cd16939     1 MARALDNLLRNALRYAHRT----VRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFvrLDPSRDRATggFGLGLAIVH 76
                          90       100
                  ....*....|....*....|....*..
gi 499421692 1095 ELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16939    77 RVALWHGGHVECDDSELGGACFRLTWP 103
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1171-1294 1.80e-10

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 62.73  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshiPIILLT 1249
Cdd:PRK10701    3 KIVFVEDDAEVGSLIAAYLAKHdIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG---PIVLLT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499421692 1250 ALNIEEKYQEGIESGADAYITKPFNVSLLLARifklieLRDKLRQ 1294
Cdd:PRK10701   80 SLDSDMNHILALEMGACDYILKTTPPAVLLAR------LRLHLRQ 118
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1025-1121 2.01e-10

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: 59.14  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1025 NLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSS----VGVGLHLTHELVQVH 1100
Cdd:cd16952     7 NLVSNAVKYTPPSDTI--TVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRntggTGLGLAIVKHVMSRH 84
                          90       100
                  ....*....|....*....|.
gi 499421692 1101 KGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16952    85 DARLLIASELGKGSRFTCLFP 105
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1172-1285 2.96e-10

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: 59.09  E-value: 2.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHipIILL 1248
Cdd:cd17532     1 ALIVDDEPLAREELRyllEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPL--IVFV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499421692 1249 TAlnieekYQE----GIESGADAYITKPFNVSLL---LARIFKL 1285
Cdd:cd17532    79 TA------YDEyaveAFELNAVDYLLKPFSEERLaeaLAKLRKR 116
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1171-1234 3.14e-10

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 59.52  E-value: 3.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKL 1234
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEPDIEVvgeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
1174-1272 3.27e-10

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 58.44  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1174 IIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILLTA 1250
Cdd:cd17565     3 IVDDDKNIIKILSDIIEDDDLGEVvgeADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKD--TGSNGKFIMISQ 80
                          90       100
                  ....*....|....*....|..
gi 499421692 1251 LNIEEKYQEGIESGADAYITKP 1272
Cdd:cd17565    81 VSDKEMIGKAYQAGIEFFINKP 102
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1121 3.61e-10

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: 58.17  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVG--VGLHLTHEL 1096
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPENTRI--YITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNTEGagLGLSIAKAI 78
                          90       100
                  ....*....|....*....|....*
gi 499421692 1097 VQVHKGNISYdENEGGGSVFTVLLP 1121
Cdd:cd16923    79 IELHGGSASA-EYDDNHDLFKVRLP 102
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1172-1284 4.25e-10

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: 58.51  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHipIILL 1248
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVvgeASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSAR--IVIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKPFNVSLLLARIFK 1284
Cdd:cd19931    79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQ 114
PRK10336 PRK10336
two-component system response regulator QseB;
1171-1301 5.39e-10

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 61.06  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIG-VYFEVEVAADGTSGfeKASTYDA--DLIVCDVLMPGMNGFEVTRKLKNEftTSHIPIIL 1247
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSkMGFSVDWFTQGRQG--KEALYSApyDAVILDLTLPGMDGRDILREWREK--GQREPVLI 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI-----ELRDKLRQ-KYSNEPG 1301
Cdd:PRK10336   78 LTARDALAERVEGLRLGADDYLCKPFALIEVAARLEALMrrtngQASNELRHgNVMLDPG 137
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
1172-1282 7.44e-10

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 57.83  E-value: 7.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILLTA 1250
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKgYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKE--KHPSIVVIVLSD 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499421692 1251 LNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17573    79 NPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1171-1223 9.28e-10

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: 55.65  E-value: 9.28e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692   1171 KVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMP 1223
Cdd:smart00448    2 RILVVDDDPLLRELLKallEKEG--YEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1025-1119 1.14e-09

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: 57.09  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1025 NLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHS---SVGVGLHLTHELVQVHK 1101
Cdd:cd16945    11 NLLDNAIDFSPEGGLI--ALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHSgqkSTGLGLAFVQEVAQLHG 88
                          90
                  ....*....|....*...
gi 499421692 1102 GNISYDENEGGGSVFTVL 1119
Cdd:cd16945    89 GRITLRNRPDGVLAFLTL 106
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1171-1280 1.33e-09

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 57.03  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDI-----REFLREEigvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPI 1245
Cdd:cd17569     2 TILLVDDEPNIlkalkRLLRREG----YEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERY--PDTVR 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 499421692 1246 ILLTAlnieekYQEgIESGADA--------YITKPFNVSLLLA 1280
Cdd:cd17569    76 ILLTG------YAD-LDAAIEAinegeiyrFLTKPWDDEELKE 111
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
1170-1280 1.36e-09

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: 57.45  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLREEIGVYFE--VEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIIL 1247
Cdd:cd17530     1 LRVLVLDDDPFQCMMAATILEDLGPgnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAE--SHSNAAVIL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1248 LTALniEEKYQEGIESGADAY-------ITKPFNVSLLLA 1280
Cdd:cd17530    79 MSGL--DGGILESAETLAGANglnllgtLSKPFSPEELTE 116
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
1172-1273 1.63e-09

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: 56.59  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEK-ASTYDADLIVCDVLMPG-MNGFEVTRKLKNEFttSHIPIILL 1248
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLgYTVLEAASGDEALDLlESGPDIDLLVTDVIMPGgMNGSQLAEEARRRR--PDLKVLLT 78
                          90       100
                  ....*....|....*....|....*..
gi 499421692 1249 T--ALNIEEkyQEGIESGADaYITKPF 1273
Cdd:cd18161    79 SgyAENAIE--GGDLAPGVD-VLSKPF 102
fixJ PRK09390
response regulator FixJ; Provisional
1172-1282 1.97e-09

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 58.86  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIRE---FLREEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILL 1248
Cdd:PRK09390    6 VHVVDDDEAMRDslaFLLDSAG--FEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKA--RGSPLPVIVM 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499421692 1249 T-----ALNIeekyqEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK09390   82 TghgdvPLAV-----EAMKLGAVDFIEKPFEDERLIGAI 115
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1172-1278 2.10e-09

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 56.48  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGF----EKASTYDadLIVCDVLMPGMNGFEVTRKLKNEFttsHIPII 1246
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCgYQVTTCTDAEEALsmlrENKDEFD--LVITDVHMPDMDGFEFLELIRLEM---DLPVI 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLL 1278
Cdd:cd17584    76 MMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
PRK10643 PRK10643
two-component system response regulator PmrA;
1171-1286 2.28e-09

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 59.28  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFL----REEIGVYFEVEVAADGTSGFEkASTYDadLIVCDVLMPGMNGFEVTRKLKNEFTTshIPII 1246
Cdd:PRK10643    2 KILIVEDDTLLLQGLilalQTEGYACDCASTAREAEALLE-SGHYS--LVVLDLGLPDEDGLHLLRRWRQKKYT--LPVL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:PRK10643   77 ILTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALI 116
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1118 2.29e-09

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


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 56.32  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKE---KRSELFKRFMQSSFSHSSVGVGLHLTHE 1095
Cdd:cd16975     5 LSRALINIISNACQYAPEGGTV--SISIYDEEEYLYFEIWDNGHGFSEQdlkKALELFYRDDTSRRSGGHYGMGLYIAKN 82
                          90       100
                  ....*....|....*....|...
gi 499421692 1096 LVQVHKGNISYDENEGGGSVFTV 1118
Cdd:cd16975    83 LVEKHGGSLIIENSQKGGAEVTV 105
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
1170-1298 3.57e-09

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: 56.02  E-value: 3.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIILL 1248
Cdd:cd17553     1 EKILIVDDQYGIRILLNEVFNKEgYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKV--IDENIRVIIM 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 499421692 1249 TALNIEEKYQEGIESGADAYITKPFNVSlllarifkliELRDKLRqKYSN 1298
Cdd:cd17553    79 TAYGELDMIQESKELGALTHFAKPFDID----------EIRDAVK-KYLP 117
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
1355-1420 4.39e-09

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 59.22  E-value: 4.39e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1355 GVTGYSPYEYLRVMRMKKaaeMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKKLSE 1420
Cdd:PRK10572  225 GISVLRWREDQRISRAKL---LLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEE 287
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
1172-1282 4.72e-09

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 55.73  E-value: 4.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR---EEIGVYfEVEVAADGTSGFEKASTYDADLIVCDV-LMPGMNGFEVTRKLK-NEFTTSHIPII 1246
Cdd:cd17589     1 FLIVDDQPTFRSMLKsmlRSLGVT-RIDTASSGEEALRMCENKTYDIVLCDYnLGKGKNGQQLLEELRhKKLISPSTVFI 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd17589    80 MVTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
882-1113 5.18e-09

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 60.42  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  882 IIRKFNRLRNRiavEKQ-LTEYKLEFfTNISHEFRTPLTLIQGALNKLINIENPPKEMQRPLktMDKSTQRMLRLINQLL 960
Cdd:PRK10815  248 LVRNLNRLLKN---ERErYTKYRTTL-TDLTHSLKTPLAVLQSTLRSLRSGKQMSVEQAEPI--MLEQISRISQQIGYYL 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  961 EFRKMQKNKLALSLEETDVIAFLYEIFLSFKDTSESKNIDFSFEPSqPAYKMFIDKGNLDKVTYNLLSNAFKYTpsngkI 1040
Cdd:PRK10815  322 HRASMRSEHNLLSRELHSVAPLLDNLTSALNKVYQRKGVNITLDIS-PEITFVGEKNDFMEVMGNVLDNACKYC-----L 395
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421692 1041 IF-KIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQVHKGNISYDENEGGG 1113
Cdd:PRK10815  396 EFvEISARQTDEHLHIVVEDDGPGIPESKRELIFDRGQRADTLRPGQGLGLSVAREITEQYEGKISAGDSPLGG 469
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1120 6.01e-09

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 54.77  E-value: 6.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTPS--NGKIIFKIDIQEDKQQLRiqVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHEL 1096
Cdd:cd16976     1 IQQVLMNLLQNALDAMGKveNPRIRIAARRLGGRLVLV--VRDNGPGIAEEHLSRVFDPFFTTKPVGKGTGLGLSISYGI 78
                          90       100
                  ....*....|....*....|....
gi 499421692 1097 VQVHKGNISYDENEGGGSVFTVLL 1120
Cdd:cd16976    79 VEEHGGRLSVANEEGAGARFTFDL 102
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
1172-1295 6.21e-09

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 55.40  E-value: 6.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLTAL 1251
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVADP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499421692 1252 NIEEKYQEGIESGADAYITKPFNVSLLLARifklieLRDKLRQK 1295
Cdd:cd17539    81 GDRGRLIRALEIGVNDYLVRPIDPNELLAR------VRTQIRRK 118
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1168-1284 6.65e-09

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 60.04  E-value: 6.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1168 NKRKVLIIEDD----TDIREFLReeiGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHI 1243
Cdd:PRK10365    4 DNIDILVVDDDishcTILQALLR---GWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKA--LNPAI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 499421692 1244 PIILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFK 1284
Cdd:PRK10365   79 PVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
1378-1416 6.94e-09

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 52.54  E-value: 6.94e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 499421692  1378 LTEDLTIAEVAYSVGInDPFYFSKCFKNQFGVSPSAYRK 1416
Cdd:pfam00165    5 LSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
1026-1121 9.93e-09

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 59.26  E-value: 9.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1026 LLSNAFKY--TPSNGKIIFKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHssvGVGLHLTHELVQVHKGN 1103
Cdd:COG2972   344 LVENAIEHgiEPKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKGEGR---GIGLRNVRERLKLYYGE 420
                          90       100
                  ....*....|....*....|.
gi 499421692 1104 ---ISYDENEGGGSVFTVLLP 1121
Cdd:COG2972   421 eygLEIESEPGEGTTVTIRIP 441
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1212-1276 1.01e-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: 54.68  E-value: 1.01e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421692 1212 DADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLTALNIEEKYQEGIESGADAYITKPFNVS 1276
Cdd:cd17581    53 KVNMIITDYCMPGMTGYDLLKKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLA 117
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1121 1.05e-08

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: 54.33  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTP-SNGKII--------FKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSsvGVG 1089
Cdd:cd16918     1 LIQVFLNLVRNAAQALAgSGGEIIlrtrtqrqVTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPMVSGRENGT--GLG 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499421692 1090 LHLTHELVQVHKGNISYDeNEGGGSVFTVLLP 1121
Cdd:cd16918    79 LAIAQNIVSQHGGVIECD-SQPGHTVFSVSLP 109
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1171-1282 1.41e-08

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: 54.17  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGV--YFEV-EVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIIL 1247
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQvpGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAG--HDVDVIV 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd19925    80 VTAANDVETVREALRLGVVDYLIKPFTFERLRQRL 114
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1019-1121 1.59e-08

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: 54.12  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1019 LDKVTYNLLSNAFKYTP-SNGKIIfkIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQ-----SSFSHSSvGVGLHL 1092
Cdd:cd16953     1 LGQVLRNLIGNAISFSPpDTGRIT--VSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTerpanEAFGQHS-GLGLSI 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499421692 1093 THELVQVHkGNISYDEN-----EGGGSVFTVLLP 1121
Cdd:cd16953    78 SRQIIEAH-GGISVAENhnqpgQVIGARFTVQLP 110
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1005-1120 1.77e-08

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: 54.06  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1005 PSQPAYKMfIDKGNLDKVTYNLLSNAFKYTpSNGKIIfKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHS 1084
Cdd:cd16947     8 PDRPIYAN-ANTEALQRILKNLISNAIKYG-SDGKFL-GMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRN 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499421692 1085 SV----GVGLHLTHELVQVHKGNISYDENEGGGSVFTVLL 1120
Cdd:cd16947    85 SAkqgnGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
ftrA PRK09393
transcriptional activator FtrA; Provisional
1319-1417 1.84e-08

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 57.67  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1319 KLNEVLNEHMTDtDFSVNDFAGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFY 1398
Cdd:PRK09393  222 PLIDWMRAHLAE-PHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEES 300
                          90
                  ....*....|....*....
gi 499421692 1399 FSKCFKNQFGVSPSAYRKK 1417
Cdd:PRK09393  301 LRHHFRRRAATSPAAYRKR 319
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
1172-1294 2.53e-08

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: 53.91  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshiPI-ILLTA 1250
Cdd:cd17596     3 ILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPE---VVrIIISG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499421692 1251 LNIEEKYQEGI-ESGADAYITKPFNVSLLLARIFKLIELRDKLRQ 1294
Cdd:cd17596    80 YTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRE 124
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
906-1125 2.54e-08

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 58.11  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  906 FFTNISHEFRTPLTLIQGAlNKLINIENP--PKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQKNKLALSLEETDVIAFL 983
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMA-ADVIHDSRDdfDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLV 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  984 YEIFLSFKDTSESKNIDFSFE-PSQPAyKMFIDKGNLDKVTYNLLSNAFKYtpSNGKIIfKIDIQEDKQQLRIQVIDNGI 1062
Cdd:NF040691  353 RRVVDALRQLAERAGVELRVDaPGTPV-VAEVDPRRVERVLRNLVVNAIEH--GEGKPV-VVTVAQDDTAVAVTVRDHGV 428
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1063 GIPKEKRSELFKRFMQSSFSHS----SVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNSD 1125
Cdd:NF040691  429 GLKPGEVALVFDRFWRADPARArttgGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAG 495
pleD PRK09581
response regulator PleD; Reviewed
1150-1306 2.98e-08

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 57.99  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1150 FLRNETS------EDTFQPPVDPLNKRKVLIIEDDTDIREFLREEIGVYFEVEVAADGTSGFEKASTYDADLIVCDVLMP 1223
Cdd:PRK09581  130 RLRASTNaeigvtALMIMAYANKDEDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFE 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1224 GMNGFEVTRKLKNEFTTSHIPIILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIfkLIELR-----DKLRQKysn 1298
Cdd:PRK09581  210 NYDPLRLCSQLRSKERTRYVPILLLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARV--RTQIRrkryqDALRNN--- 284

                  ....*...
gi 499421692 1299 epgLAHSI 1306
Cdd:PRK09581  285 ---LEQSI 289
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
887-1104 4.82e-08

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 57.77  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  887 NRLRNRIAVEKQL--TEYKL----------EFFTNISHEFRTPLTLIQGAL--NKLINIENPPKEMQRPLKTMDKSTQRM 952
Cdd:COG4192   405 TEIEERKRIEKNLrqTQDELiqaakmavvgQTMTSLAHELNQPLNAMSMYLfsAKKALEQENYAQLPTSLDKIEGLIERM 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  953 LRLINQLLEFRKmqknKLALSLEETDviafLYEIFLSFKDTSESKNIDFSFEPSQPAYKM-FIDKGNLDKVTYNLLSNAF 1031
Cdd:COG4192   485 DKIIKSLRQFSR----KSDTPLQPVD----LRQVIEQAWELVESRAKPQQITLHIPDDLMvQGDQVLLEQVLVNLLVNAL 556
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421692 1032 KYTPSNGKIifKIDIQEDKQQLRIQVIDNGIGIPKEKRseLFKRFmqssFSHSSVGVGLHLT--HELVQVHKGNI 1104
Cdd:COG4192   557 DAVATQPQI--SVDLLSNAENLRVAISDNGNGWPLVDK--LFTPF----TTTKEVGLGLGLSicRSIMQQFGGDL 623
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1214-1282 5.79e-08

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 55.46  E-value: 5.79e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1214 DLIVCDVLMPGMNGFEVTRKLKNeftTSHIPIILLTAlNIEE-KYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK10710   56 DLILLDLMLPGTDGLTLCREIRR---FSDIPIVMVTA-KIEEiDRLLGLEIGADDYICKPYSPREVVARV 121
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1181-1272 7.51e-08

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 51.60  E-value: 7.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1181 IREFLREEIgvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLTAlniEEKYQEG 1260
Cdd:cd17602    14 IEYFLEKQG---FRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG---KDGLVDR 87
                          90
                  ....*....|....*
gi 499421692 1261 IES---GADAYITKP 1272
Cdd:cd17602    88 IRAkmaGASGYLTKP 102
PRK15369 PRK15369
two component system response regulator;
1171-1282 1.04e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 53.93  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVYFEVEVAA---DGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIIL 1247
Cdd:PRK15369    5 KILLVDDHELIINGIKNMLAPYPRYKIVGqvdNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRW--PAMNILV 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1248 LTAlNIEEKY-QEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK15369   83 LTA-RQEEHMaSRTLAAGALGYVLKKSPQQILLAAI 117
PRK10816 PRK10816
two-component system response regulator PhoP;
1171-1286 1.12e-07

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 54.36  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshIPIIL 1247
Cdd:PRK10816    2 RVLVVEDNALLRHHLKvqlQDAG--HQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499421692 1248 LTAlniEEKYQEGI---ESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:PRK10816   78 LTA---RESWQDKVevlSAGADDYVTKPFHIEEVMARMQALM 116
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
1364-1419 1.13e-07

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 55.04  E-value: 1.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499421692 1364 YLRVMRMKKAAEML--LTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKKLS 1419
Cdd:PRK09685  245 YIRNRRLDRCADDLrpAADDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRRKFR 302
PLN03029 PLN03029
type-a response regulator protein; Provisional
1212-1276 1.31e-07

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 53.88  E-value: 1.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421692 1212 DADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPIILLTALNIEEKYQEGIESGADAYITKPFNVS 1276
Cdd:PLN03029   72 EVNLIITDYCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLS 136
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
890-1124 1.35e-07

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 56.22  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  890 RNRIAVEKQLTEYKLE----------FFTNISHEFRTPLTLIQG----ALNKLinieNPPKEMQRPLKTMDKSTQRMLRL 955
Cdd:PRK13837  427 RRRLETERDALERRLEharrleavgtLASGIAHNFNNILGAILGyaemALNKL----ARHSRAARYIDEIISAGARARLI 502
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  956 INQLLEFRKmqknKLALSLEETDVIAFLYEIfLSFKDTSESKNIDFSFEpsQPAYKMFIDkGN---LDKVTYNLLSNAFK 1032
Cdd:PRK13837  503 IDQILAFGR----KGERNTKPFDLSELVTEI-APLLRVSLPPGVELDFD--QDQEPAVVE-GNpaeLQQVLMNLCSNAAQ 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1033 YTPSNGKIifkiDIQEDKQQLR-----------------IQVIDNGIGIPKEKRSELFKRFmqssFSHSSVGVGLHL--T 1093
Cdd:PRK13837  575 AMDGAGRV----DISLSRAKLRapkvlshgvlppgryvlLRVSDTGAGIDEAVLPHIFEPF----FTTRAGGTGLGLatV 646
                         250       260       270
                  ....*....|....*....|....*....|.
gi 499421692 1094 HELVQVHKGNISYDENEGGGSVFTVLLPTNS 1124
Cdd:PRK13837  647 HGIVSAHAGYIDVQSTVGRGTRFDVYLPPSS 677
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
1331-1425 1.45e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 54.91  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1331 TDFSVNDFAGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVS 1410
Cdd:PRK13501  191 AYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMT 270
                          90       100
                  ....*....|....*....|
gi 499421692 1411 PSAYRKKLSE-----DENEP 1425
Cdd:PRK13501  271 PRDYRQRFIRspvlpAKNEP 290
PRK13557 PRK13557
histidine kinase; Provisional
910-1249 2.07e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 55.45  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  910 ISHEFRTPLTLIQGALNKL-INIENP---PKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQK--------NKLALSLEEt 977
Cdd:PRK13557  170 IAHDFNNLLQVMSGYLDVIqAALSHPdadRGRMARSVENIRAAAERAATLTQQLLAFARKQRlegrvlnlNGLVSGMGE- 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  978 dviaflyeifLSFKDTSESKNIDFSFEPSQPAYKmfIDKGNLDKVTYNLLSNAFKYTPSNGKIIFK---IDIQEDK---- 1050
Cdd:PRK13557  249 ----------LAERTLGDAVTIETDLAPDLWNCR--IDPTQAEVALLNVLINARDAMPEGGRVTIRtrnVEIEDEDlamy 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1051 QQLR------IQVIDNGIGIPKEKRSELFKRFMQSSFSHSSVGVGLHLTHELVQVHKGNISYDENEGGGSVFTVLLPTNS 1124
Cdd:PRK13557  317 HGLPpgryvsIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASD 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1125 DIyqekdflipnqlLTEEEEQHSKDFLR--NETsedtfqppvdplnkrkVLIIEDDTDIREFLR---EEIGvyFEVEVAA 1199
Cdd:PRK13557  397 QA------------ENPEQEPKARAIDRggTET----------------ILIVDDRPDVAELARmilEDFG--YRTLVAS 446
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499421692 1200 DGTSGFEK-ASTYDADLIVCDVLMPG-MNGFEVTRKLKNEFTTSHipiILLT 1249
Cdd:PRK13557  447 NGREALEIlDSHPEVDLLFTDLIMPGgMNGVMLAREARRRQPKIK---VLLT 495
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
1172-1272 2.33e-07

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: 50.20  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIG-VYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPIILLTA 1250
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGrAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKA--RPDLPIIVMSA 78
                          90       100
                  ....*....|....*....|..
gi 499421692 1251 LNIEEKYQEGIESGADAYITKP 1272
Cdd:cd19928    79 QNTLMTAVKAAERGAFEYLPKP 100
glnL PRK11073
nitrogen regulation protein NR(II);
1003-1121 2.61e-07

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 54.32  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1003 FEPSQPAYKMfiDKGNLDKVTYNLLSNAFK-YTPSNGKII------FKIDIQEDKQQL--RIQVIDNGIGIPKEKRSELF 1073
Cdd:PRK11073  224 YDPSLPELAH--DPDQIEQVLLNIVRNALQaLGPEGGTITlrtrtaFQLTLHGERYRLaaRIDIEDNGPGIPPHLQDTLF 301
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499421692 1074 krFMQSSFSHSSVGVGLHLTHELVQVHKGNISYdENEGGGSVFTVLLP 1121
Cdd:PRK11073  302 --YPMVSGREGGTGLGLSIARNLIDQHSGKIEF-TSWPGHTEFSVYLP 346
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
1357-1415 2.73e-07

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 53.91  E-value: 2.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499421692 1357 TGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYR 1415
Cdd:PRK13503  212 TGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
299-541 4.25e-07

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 53.10  E-value: 4.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  299 VTRDNKGNAWVHNY-TGNVWYVNTSTGDIKHFQFLSSEHLgyidverYSIIHDSRDIIWITTYGNG-LFAYDLNTGDLQH 376
Cdd:COG4257    22 VAVDPDGAVWFTDQgGGRIGRLDPATGEFTEYPLGGGSGP-------HGIAVDPDGNLWFTDNGNNrIGRIDPKTGEITT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  377 FTFEVSHSshinsnYLQYIIEDRSGGIWVSSEFSG-LSHLEiLNKGTLRIYPNGEDASDrsntIRMLLRGKNGNVYMANR 455
Cdd:COG4257    95 FALPGGGS------NPHGIAFDPDGNLWFTDQGGNrIGRLD-PATGEVTEFPLPTGGAG----PYGIAVDPDGNLWVTDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  456 MG-TLYEYDAD---LKNILRREKFTHNVYsMCEDNEGQLWLGMrgiglrIGADQWYRYNSKDNN------SLSNDNVYLI 525
Cdd:COG4257   164 GAnAIGRIDPDtgtLTEYALPTPGAGPRG-LAVDPDGNLWVAD------TGSGRIGRFDPKTGTvteyplPGGGARPYGV 236
                         250
                  ....*....|....*.
gi 499421692  526 YRDRKGRMWIGTFGGG 541
Cdd:COG4257   237 AVDGDGRVWFAESGAN 252
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1015-1121 7.48e-07

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 49.07  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1015 DKGNLDKVTYNLLSNAFKYTPS--NGKIIFKIDIQEDK-QQLRIQVIDNGIGIPKEKRSELFKRFMQSSfsHSSVGVGLH 1091
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGrpSDVGEVRIRVEADQdGRIVLIVCDNGKGFPREMRHRATEPYVTTR--PKGTGLGLA 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 499421692 1092 LTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:cd16944    79 IVKKIMEEHGGRISLSNREAGGACIRIILP 108
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1171-1272 9.37e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 52.58  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEfttSHIPIIL 1247
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALARDPDHEVvwvATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAE---RPCPILI 78
                          90       100
                  ....*....|....*....|....*...
gi 499421692 1248 LTAL---NIEEKYqEGIESGADAYITKP 1272
Cdd:PRK12555   79 VTSLterNASRVF-EAMGAGALDAVDTP 105
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
1172-1282 9.56e-07

receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus pneumoniae RitR (Repressor of iron transport Regulator, formerly RR489) is an orphan two-component signal transduction response regulator that is required for lung pathogenicity. It acts to repress iron uptake via binding the pneumococcal iron uptake (Piu) transporter promoter. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. However, members of this family do not contain the phosphorylatable aspartic acid residue and are phosphorylation-independent.


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 49.01  E-value: 9.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVY-FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLkNEFTTSHIPIILLTA 1250
Cdd:cd19922     1 ILLLEKERNLAHFLSLELQKEgYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKL-SRIKPASVIIVLDHW 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499421692 1251 LNIEEkYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:cd19922    80 EDLQE-ELEEVQRFAVSYVVKPVLISNLVDKI 110
PRK10337 PRK10337
sensor protein QseC; Provisional
906-1118 1.14e-06

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 52.73  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  906 FFTNISHEFRTPLTL--IQGALNKLIniENPPKEMQRPLKTMDKSTQRMLRLINQLLEFRKMQknklALS-LEETDVIAF 982
Cdd:PRK10337  240 FTSDAAHELRSPLAAlkVQTEVAQLS--DDDPQARKKALLQLHAGIDRATRLVDQLLTLSRLD----SLDnLQDVAEIPL 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  983 ---LYEIFLSFKDTSESKNIDFSFE-PSQPAykmfIDKGN---LDKVTYNLLSNAFKYTPSNGKIIFKIDIQedkqqlRI 1055
Cdd:PRK10337  314 edlLQSAVMDIYHTAQQAGIDVRLTlNAHPV----IRTGQpllLSLLVRNLLDNAIRYSPQGSVVDVTLNAR------NF 383
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421692 1056 QVIDNGIGIPKEKRSELFKRFMQSSFSHSS-VGVGLHLTHELVQVHKGNISYDENEGGGSVFTV 1118
Cdd:PRK10337  384 TVRDNGPGVTPEALARIGERFYRPPGQEATgSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKV 447
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1171-1282 1.16e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 51.01  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLRE--EIGVYFEVEV-AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHipIIL 1247
Cdd:PRK10403    8 QVLIVDDHPLMRRGVRQllELDPGFEVVAeAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQ--III 85
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499421692 1248 LTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK10403   86 LTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAI 120
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
1171-1273 1.63e-06

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: 47.88  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGvyFEVEVAADGTSGFEKA-STYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPII 1246
Cdd:cd18160     1 TILLADDEPSVRKFIVttlKKAG--YAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARK--IDPDVKIL 76
                          90       100
                  ....*....|....*....|....*..
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPF 1273
Cdd:cd18160    77 FISGGAAAAPELLSDAVGDNATLKKPF 103
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
1026-1121 1.70e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 52.21  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1026 LLSNAFKYT-PSN--GKIifKIDIQEDKQQLRIQVIDNGIGIPKEkrselFKRFMQSSFshssvgvGLHLTHELVQVHKG 1102
Cdd:COG3920   407 LVTNALKHAfLSGegGRI--RVSWRREDGRLRLTVSDNGVGLPED-----VDPPARKGL-------GLRLIRALVRQLGG 472
                          90
                  ....*....|....*....
gi 499421692 1103 NISYDENEggGSVFTVLLP 1121
Cdd:COG3920   473 TLELDRPE--GTRVRITFP 489
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1172-1289 1.90e-06

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: 48.35  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIR----EFLREEigvYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKL-KNEFTTshiPII 1246
Cdd:cd17572     1 VLLVEDSPSLAalyqEYLSDE---GYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIqERSLPT---SVI 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 499421692 1247 LLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLIELR 1289
Cdd:cd17572    75 VITAHGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHR 117
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1167-1286 2.02e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 52.18  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1167 LNKRKVLIIEDDTDIREFLREEI-GVYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshIPI 1245
Cdd:PRK10923    1 MQRGIVWVVDDDSSIRWVLERALaGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARIFKLI 1286
Cdd:PRK10923   79 IIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 119
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
1014-1121 2.20e-06

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 52.14  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1014 IDKGNLDKVTYNLLSNAFK---YTPSNGKIIfKIDIQEDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSSFSHSSV-GVG 1089
Cdd:PRK15053  428 LDSTEFAAIVGNLLDNAFEaslRSDEGNKIV-ELFLSDEGDDVVIEVADQGCGVPESLRDKIFEQGVSTRADEPGEhGIG 506
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499421692 1090 LHLTHELVQVHKGNISYDENEGGGSVFTVLLP 1121
Cdd:PRK15053  507 LYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
1320-1418 2.88e-06

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 47.23  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1320 LNEVLNEHMtDTDFSVNDFAGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYF 1399
Cdd:PRK10219   10 LIAWIDEHI-DQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTF 88
                          90
                  ....*....|....*....
gi 499421692 1400 SKCFKNQFGVSPSAYRKKL 1418
Cdd:PRK10219   89 SRVFRRQFDRTPSDYRHRL 107
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
1170-1282 4.63e-06

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 49.12  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1170 RKVLIIEDD----TDIREFL-REEIGVYFEVEvaaDGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKL-KNEFTTShi 1243
Cdd:PRK09958    1 MNAIIIDDHplaiAAIRNLLiKNDIEILAELT---EGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLrKRQYSGI-- 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499421692 1244 pIILLTALNIEEKYQEGIESGADAYITKPFNVSLLLARI 1282
Cdd:PRK09958   76 -IIIVSAKNDHFYGKHCADAGANGFVSKKEGMNNIIAAI 113
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
1171-1277 4.68e-06

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: 47.01  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLR---EEIGVyfEVEVAadgTSGFEKASTYDA-----DLIVCDVLMPGMNGFEVTRKLKNEFTTSH 1242
Cdd:cd19933     2 KVLLVDDNAVNRMVTKgllEKLGC--EVTTV---SSGEECLNLLASaehsfQLVLLDLCMPEMDGFEVALRIRKLFGRRE 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499421692 1243 IP-IILLTALNIEEKYQEGIESGADAYITKPfnVSL 1277
Cdd:cd19933    77 RPlIVALTANTDDSTREKCLSLGMNGVITKP--VSL 110
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1171-1293 7.94e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 49.76  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1171 KVLIIEDDTDIREFLREEIGVYFEVEV---AADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshiPIIL 1247
Cdd:PRK00742    5 RVLVVDDSAFMRRLISEILNSDPDIEVvgtAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPT---PVVM 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499421692 1248 LTALNieekyQEG-------IESGADAYITKPFNVSLLLARIFKLiELRDKLR 1293
Cdd:PRK00742   82 VSSLT-----ERGaeitlraLELGAVDFVTKPFLGISLGMDEYKE-ELAEKVR 128
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1172-1271 2.48e-05

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 44.96  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIGVYFEVEVAADGTSGFE---KASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHipIILL 1248
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDDLEVVAQASNGQEalrLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTK--VLIV 78
                          90       100
                  ....*....|....*....|...
gi 499421692 1249 TALNIEEKYQEGIESGADAYITK 1271
Cdd:cd19930    79 TTFGRPGYFRRALAAGVDGYVLK 101
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
1172-1272 2.77e-05

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 44.45  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLREEIG-VYFEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFttSHIPIILLTA 1250
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGrMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRL--PQTPVAVITA 78
                          90       100
                  ....*....|....*....|..
gi 499421692 1251 LNIEEKYQEGIESGADAYITKP 1272
Cdd:cd19926    79 YGSLDTAIEALKAGAFDFLTKP 100
PRK10693 PRK10693
two-component system response regulator RssB;
1197-1252 4.76e-05

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 46.91  E-value: 4.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499421692 1197 VAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTshIPIILLTALN 1252
Cdd:PRK10693    2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQ--TPVLVISATE 55
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
1333-1415 6.65e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 46.59  E-value: 6.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1333 FSVNDFAGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPS 1412
Cdd:PRK13502  193 FALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPS 272

                  ...
gi 499421692 1413 AYR 1415
Cdd:PRK13502  273 QWR 275
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
1172-1282 1.40e-04

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 43.17  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDDTDIREFLR------EEIGVYFevevAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEFTTSHIPI 1245
Cdd:cd17575     3 VLLVDDQAIIGEAVRraladeEDIDFHY----CSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPI 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499421692 1246 ILLTALNIEEKYQEGIESGADAYITK-PFNVSlLLARI 1282
Cdd:cd17575    79 IVLSTKEEPEVKSEAFALGANDYLVKlPDKIE-LVARI 115
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
394-635 1.70e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 45.01  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  394 YIIEDRSGGIWVSSEFSG-LSHLEILNkGTLRIYPNGEDasdrsNTIRMLLRGKNGNVYMA-NRMGTLYEYDADLKNILR 471
Cdd:COG4257    21 DVAVDPDGAVWFTDQGGGrIGRLDPAT-GEFTEYPLGGG-----SGPHGIAVDPDGNLWFTdNGNNRIGRIDPKTGEITT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  472 RE--KFTHNVYSMCEDNEGQLWLGMRGIGlRIGadqwyRYNSKDNN------SLSNDNVYLIYRDRKGRMWIGTFGGGLN 543
Cdd:COG4257    95 FAlpGGGSNPHGIAFDPDGNLWFTDQGGN-RIG-----RLDPATGEvtefplPTGGAGPYGIAVDPDGNLWVTDFGANAI 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692  544 LAVKTGNGyQFKHF--FQDSYGEKRVRViqeDRNGMMWVG--TNNGIYIFHPDSliNSPKNYVLYNhvNETFPSNeircL 619
Cdd:COG4257   169 GRIDPDTG-TLTEYalPTPGAGPRGLAV---DPDGNLWVAdtGSGRIGRFDPKT--GTVTEYPLPG--GGARPYG----V 236
                         250
                  ....*....|....*.
gi 499421692  620 VNDHEGNMWIGTTGAG 635
Cdd:COG4257   237 AVDGDGRVWFAESGAN 252
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
1333-1415 1.98e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 45.09  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1333 FSVNDFAGIMGLGRTVFYKKVRGVTGYSPYEYLRVMRMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPS 1412
Cdd:PRK13500  223 FALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPS 302

                  ...
gi 499421692 1413 AYR 1415
Cdd:PRK13500  303 QWR 305
PRK09483 PRK09483
response regulator; Provisional
1172-1271 2.13e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 44.33  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1172 VLIIEDD----TDIREFLREEIGVYFEVEvAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNefTTSHIPIIL 1247
Cdd:PRK09483    4 VLLVDDHelvrAGIRRILEDIKGIKVVGE-ACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILR--YTPDVKIIM 80
                          90       100
                  ....*....|....*....|....*
gi 499421692 1248 LTaLNIEEKYQEGI-ESGADAYITK 1271
Cdd:PRK09483   81 LT-VHTENPLPAKVmQAGAAGYLSK 104
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
1313-1417 5.80e-04

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 43.38  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1313 DQKFSVKLNEVLNEHMTD-----------TDFSVNDFAGIMGLGRTVFYKKVRGV-TGYSpyEYLRVMRMKKAAEMLLTE 1380
Cdd:PRK09978  128 DEHFIPLLLNVLQPNMRTrvctvinnniaHEWTLARIASELLMSPSLLKKKLREEeTSYS--QLLTECRMQRALQLIVIH 205
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499421692 1381 DLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKK 1417
Cdd:PRK09978  206 GFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQER 242
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
1026-1121 7.23e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 43.07  E-value: 7.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1026 LLSNAFKYtpSNGKIIfKIDIQEDKQQLRIQVIDNGIGIPKEKRselfkrfmqssfshSSVGVGLHLTHELVQVHKGNIS 1105
Cdd:COG4585   170 ALTNALKH--AGATRV-TVTLEVDDGELTLTVRDDGVGFDPEAA--------------PGGGLGLRGMRERAEALGGTLT 232
                          90
                  ....*....|....*.
gi 499421692 1106 YDENEGGGSVFTVLLP 1121
Cdd:COG4585   233 IGSAPGGGTRVRATLP 248
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
1025-1121 8.58e-04

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 43.75  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1025 NLLSNAF---KYTPsNGKIIFKIDIQEDkqQLRIQVIDNGIGIPKEKRSELFKRfmqsSFSH--SSVGVGLHLTHELVQV 1099
Cdd:PRK11086  440 NLIENALeavGGEE-GGEISVSLHYRNG--WLHCEVSDDGPGIAPDEIDAIFDK----GYSTkgSNRGVGLYLVKQSVEN 512
                          90       100
                  ....*....|....*....|..
gi 499421692 1100 HKGNISYDENEGGGSVFTVLLP 1121
Cdd:PRK11086  513 LGGSIAVESEPGVGTQFFVQIP 534
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
516-539 1.02e-03

Two component regulator propeller; A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats. These repeats show homology to pfam01011 and pfam00400 indicating that they are likely to form a beta-propeller. This family has been built with artificially high cut-offs in order to avoid overlaps with other beta-propeller families. The fourteen repeats are likely to form two propellers; it is not clear if these structures are likely to recruit other proteins or interact with DNA.


Pssm-ID: 400050 [Multi-domain]  Cd Length: 24  Bit Score: 37.68  E-value: 1.02e-03
                           10        20
                   ....*....|....*....|....
gi 499421692   516 SLSNDNVYLIYRDRKGRMWIGTFG 539
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTNG 24
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
1369-1427 1.29e-03

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 42.36  E-value: 1.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499421692 1369 RMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRKKLSEDENEPIN 1427
Cdd:PRK15186  233 RMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEFLAFLSSSRHQYVN 291
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1193-1274 1.33e-03

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: 39.83  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421692 1193 FEVEVAADGTSGFEKASTYDADLIVCDVLMPGMNGFEVTRKLKNEftTSHIPIILLTALNIEEKYQEGIESGADAYITKP 1272
Cdd:cd17593    26 VEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVE--QLETKVIVVSGDVQPEAKERVLELGALAFLKKP 103

                  ..
gi 499421692 1273 FN 1274
Cdd:cd17593   104 FD 105
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
1369-1416 1.38e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 42.67  E-value: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 499421692 1369 RMKKAAEMLLTEDLTIAEVAYSVGINDPFYFSKCFKNQFGVSPSAYRK 1416
Cdd:PRK15185  258 RMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPSTFIK 305
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1026-1080 1.43e-03

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


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 39.72  E-value: 1.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499421692 1026 LLSNAFKYTPSNGKIIFKIDIQ--EDKQQLRIQVIDNGIGIPKEKRSELFKRFMQSS 1080
Cdd:cd16957     9 LVENAIRHAFPKRKENNEVRVVvkKDQHKVHVSVSDNGQGIPEERLDLLGKTTVTSE 65
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
610-633 4.53e-03

Two component regulator propeller; A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats. These repeats show homology to pfam01011 and pfam00400 indicating that they are likely to form a beta-propeller. This family has been built with artificially high cut-offs in order to avoid overlaps with other beta-propeller families. The fourteen repeats are likely to form two propellers; it is not clear if these structures are likely to recruit other proteins or interact with DNA.


Pssm-ID: 400050 [Multi-domain]  Cd Length: 24  Bit Score: 35.75  E-value: 4.53e-03
                           10        20
                   ....*....|....*....|....
gi 499421692   610 TFPSNEIRCLVNDHEGNMWIGTTG 633
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTNG 24
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
658-681 9.36e-03

Two component regulator propeller; A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats. These repeats show homology to pfam01011 and pfam00400 indicating that they are likely to form a beta-propeller. This family has been built with artificially high cut-offs in order to avoid overlaps with other beta-propeller families. The fourteen repeats are likely to form two propellers; it is not clear if these structures are likely to recruit other proteins or interact with DNA.


Pssm-ID: 400050 [Multi-domain]  Cd Length: 24  Bit Score: 34.98  E-value: 9.36e-03
                           10        20
                   ....*....|....*....|....
gi 499421692   658 GLPNGVIQSIVEDQDNKMWIATEY 681
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTNG 24
 
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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