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Conserved domains on  [gi|145357869|ref|NP_196633|]
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histidine kinase 5 [Arabidopsis thaliana]

Protein Classification

sensor histidine kinase family protein( domain architecture ID 1001650)

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
371-922 1.64e-70

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 251.69  E-value: 1.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 371 LATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKFRPREVVKHVL 450
Cdd:PRK11107 297 LANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVV 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 451 QTAAASL-KKSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGNVGIKLqvisepsfvrdnalnadteehEQ 529
Cdd:PRK11107 377 TLLAHSAhEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILV---------------------EL 435
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 530 NGLTETSVWICCDVWDTGIGIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFI 609
Cdd:PRK11107 436 RALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFH 515
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 610 LPYKVGR---SDDYSDDQ-----------DEFSDMADQQ----------SEPDDTAEGYFQFKPLLGSIYSNGgpgiSND 665
Cdd:PRK11107 516 LPLDLNPnpiIDGLPTDClagkrllyvepNSAAAQATLDilsetplevtYSPTLSQLPEAHYDILLLGLPVTF----REP 591
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 666 FLPHKVMLtSPIKLINGFVADPSNNTGQSEMLQLENGGYMdeskletssgHC---PESAHQYengngrcfskesescsss 742
Cdd:PRK11107 592 LTMLHERL-AKAKSMTDFLILALPCHEQVLAEQLKQDGAD----------AClskPLSHTRL------------------ 642
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 743 qasseggtlemeSELTVSSHREEEKAETEVKETSK-P-KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSS 820
Cdd:PRK11107 643 ------------LPALLEPCHHKQPPLLPPTDESRlPlTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQR 710
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 821 SYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaaieagvdiSTSENEQVcmrptnrlPIIAMTANTLAESSEECYANGM 900
Cdd:PRK11107 711 PFDLILMDIQMPGMDGIRACELIR------------------QLPHNQNT--------PIIAVTAHAMAGERERLLSAGM 764
                        570       580
                 ....*....|....*....|..
gi 145357869 901 DSFISKPVTLQKLRECLQQYLH 922
Cdd:PRK11107 765 DDYLAKPIDEAMLKQVLLRYKP 786
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
90-611 8.45e-42

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


:

Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 160.72  E-value: 8.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  90 AVRLLKEELKNLDRQREEAEAKELKIIEEYKFESNEPENVPVLDETSDLFRRFRQKKRDALVDSKKIEIYEEFDTVAYWK 169
Cdd:COG4251   11 LLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 170 QKALSLEKMLEASTERERRLMEKLSESLKTMESQSAPVQELTQNLKRAEGFLHFILQNAPIVMGHQDKDLRYLFIYNKYP 249
Cdd:COG4251   91 LVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILAL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 250 SLREQDILGKTDVEIFHGGGVKESEDFKREVLEKGKASKREITFTTDLFGSKTFLIYVEPVYNKAGEKIGINYMGMEVTD 329
Cdd:COG4251  171 LLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLIL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 330 QVVKREKMAKLREDNAVRKAMESELnktihitEETMRAKQMLA-TMSHEIRSPLSGVVGMAEILST---TKLDKEQRQLL 405
Cdd:COG4251  251 VLELLELRLELEELEEELEERTAEL-------ERSNEELEQFAyVASHDLREPLRKISGFSQLLEEdygDKLDEEGREYL 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 406 NVMISSGDLVLQLINDILDLSKVESGVMRLEatKFRPREVVKHVLQTAAASLK-KSLTLEgniADDVPiEVVGDVLRIRQ 484
Cdd:COG4251  324 ERIRDAAERMQALIDDLLAYSRVGRQELEFE--PVDLNELLEEVLEDLEPRIEeRGAEIE---VGPLP-TVRGDPTLLRQ 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 485 ILTNLISNAIKFTHEGNVG-IKLQVISEPS----FVRDNalnadteeheqngltetsvwiccdvwdtGIGIPENALPCLF 559
Cdd:COG4251  398 VFQNLISNAIKYSRPGEPPrIEIGAEREGGewvfSVRDN----------------------------GIGIDPEYAEKIF 449
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145357869 560 KkyMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:COG4251  450 E--IFQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
371-922 1.64e-70

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 251.69  E-value: 1.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 371 LATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKFRPREVVKHVL 450
Cdd:PRK11107 297 LANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVV 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 451 QTAAASL-KKSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGNVGIKLqvisepsfvrdnalnadteehEQ 529
Cdd:PRK11107 377 TLLAHSAhEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILV---------------------EL 435
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 530 NGLTETSVWICCDVWDTGIGIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFI 609
Cdd:PRK11107 436 RALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFH 515
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 610 LPYKVGR---SDDYSDDQ-----------DEFSDMADQQ----------SEPDDTAEGYFQFKPLLGSIYSNGgpgiSND 665
Cdd:PRK11107 516 LPLDLNPnpiIDGLPTDClagkrllyvepNSAAAQATLDilsetplevtYSPTLSQLPEAHYDILLLGLPVTF----REP 591
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 666 FLPHKVMLtSPIKLINGFVADPSNNTGQSEMLQLENGGYMdeskletssgHC---PESAHQYengngrcfskesescsss 742
Cdd:PRK11107 592 LTMLHERL-AKAKSMTDFLILALPCHEQVLAEQLKQDGAD----------AClskPLSHTRL------------------ 642
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 743 qasseggtlemeSELTVSSHREEEKAETEVKETSK-P-KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSS 820
Cdd:PRK11107 643 ------------LPALLEPCHHKQPPLLPPTDESRlPlTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQR 710
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 821 SYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaaieagvdiSTSENEQVcmrptnrlPIIAMTANTLAESSEECYANGM 900
Cdd:PRK11107 711 PFDLILMDIQMPGMDGIRACELIR------------------QLPHNQNT--------PIIAVTAHAMAGERERLLSAGM 764
                        570       580
                 ....*....|....*....|..
gi 145357869 901 DSFISKPVTLQKLRECLQQYLH 922
Cdd:PRK11107 765 DDYLAKPIDEAMLKQVLLRYKP 786
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
340-611 1.77e-67

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 228.25  E-value: 1.77e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 340 LREDNAVRKAMESELNKTIHITEETMRAK-QMLATMSHEIRSPLSGVVGMAEILSTTkLDKEQRQLLNVMISSGDLVLQL 418
Cdd:COG0642   82 LLLLLLLLLLLLLLLLALLLLLEEANEAKsRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 419 INDILDLSKVESGVMRLEATKFRPREVVKHVLQTAAASL-KKSLTLEGNIADDVPIeVVGDVLRIRQILTNLISNAIKFT 497
Cdd:COG0642  161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAeEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYT 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 498 HEGNVgIKLQVisepsfvrdnalnadteeheqnglTETSVWICCDVWDTGIGIPENALPCLFKKYMQAsaDHARKYGGTG 577
Cdd:COG0642  240 PEGGT-VTVSV------------------------RREGDRVRISVEDTGPGIPPEDLERIFEPFFRT--DPSRRGGGTG 292
                        250       260       270
                 ....*....|....*....|....*....|....
gi 145357869 578 LGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:COG0642  293 LGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLP 326
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
362-921 8.93e-64

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: 232.75  E-value: 8.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  362 EETMRAK-QMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKF 440
Cdd:TIGR02956 458 EEANRAKsAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPF 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  441 RPREVVKHVLQ-TAAASLKKSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGNVGIKLQVISEPSfvrdna 519
Cdd:TIGR02956 538 DLNALLDDVHHlMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSS------ 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  520 lnadteeheqngltetsvwICCDVWDTGIGIPENALPCLFKKYMQAsaDHARKYGGTGLGLAICKQLVELMGGQLTVTSR 599
Cdd:TIGR02956 612 -------------------LLFEVEDTGCGIAEEEQATLFDAFTQA--DGRRRSGGTGLGLAISQRLVEAMDGELGVESE 670
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  600 VSEGSTFTFILPykvgrsddysddqdefsdmadqqsepddtaegyfqfkpllgsiysnggpgisndfLPHkvmltspikl 679
Cdd:TIGR02956 671 LGVGSCFWFTLP-------------------------------------------------------LTR---------- 685
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  680 ingfvADPSNNTGQSEMLQLenggymdeskletssghcpesahqyengngrcfskesescsssqasseggtlemeseltv 759
Cdd:TIGR02956 686 -----GKPAEDSATLTVIDL------------------------------------------------------------ 700
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  760 sshreeekaetevketSKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKA 839
Cdd:TIGR02956 701 ----------------PPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTL 764
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  840 TRLIRSYEETgnwnaaieagvdistseneqvcmrpTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQ 919
Cdd:TIGR02956 765 LQQLRAIYGA-------------------------KNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819

                  ..
gi 145357869  920 YL 921
Cdd:TIGR02956 820 IL 821
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
482-611 1.78e-49

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: 169.98  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFTHEGNVGIKLQVISEpsfvrdnalnadteeheqnglTETSVWICCDVWDTGIGIPENALPCLFKK 561
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEE---------------------EEDGVQLRFSVEDTGIGIPEEQQARLFEP 59
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145357869 562 YMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16922   60 FSQADSSTTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
90-611 8.45e-42

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 160.72  E-value: 8.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  90 AVRLLKEELKNLDRQREEAEAKELKIIEEYKFESNEPENVPVLDETSDLFRRFRQKKRDALVDSKKIEIYEEFDTVAYWK 169
Cdd:COG4251   11 LLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 170 QKALSLEKMLEASTERERRLMEKLSESLKTMESQSAPVQELTQNLKRAEGFLHFILQNAPIVMGHQDKDLRYLFIYNKYP 249
Cdd:COG4251   91 LVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILAL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 250 SLREQDILGKTDVEIFHGGGVKESEDFKREVLEKGKASKREITFTTDLFGSKTFLIYVEPVYNKAGEKIGINYMGMEVTD 329
Cdd:COG4251  171 LLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLIL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 330 QVVKREKMAKLREDNAVRKAMESELnktihitEETMRAKQMLA-TMSHEIRSPLSGVVGMAEILST---TKLDKEQRQLL 405
Cdd:COG4251  251 VLELLELRLELEELEEELEERTAEL-------ERSNEELEQFAyVASHDLREPLRKISGFSQLLEEdygDKLDEEGREYL 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 406 NVMISSGDLVLQLINDILDLSKVESGVMRLEatKFRPREVVKHVLQTAAASLK-KSLTLEgniADDVPiEVVGDVLRIRQ 484
Cdd:COG4251  324 ERIRDAAERMQALIDDLLAYSRVGRQELEFE--PVDLNELLEEVLEDLEPRIEeRGAEIE---VGPLP-TVRGDPTLLRQ 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 485 ILTNLISNAIKFTHEGNVG-IKLQVISEPS----FVRDNalnadteeheqngltetsvwiccdvwdtGIGIPENALPCLF 559
Cdd:COG4251  398 VFQNLISNAIKYSRPGEPPrIEIGAEREGGewvfSVRDN----------------------------GIGIDPEYAEKIF 449
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145357869 560 KkyMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:COG4251  450 E--IFQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
477-613 6.97e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 122.76  E-value: 6.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869   477 GDVLRIRQILTNLISNAIKFTHEGNVgIKLQVISEPSfvrdnalnadteeheqngltetsvWICCDVWDTGIGIPENALP 556
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGR-ITVTLERDGD------------------------HVEITVEDNGPGIPPEDLE 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869   557 CLFKKYMQASaDHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILPYK 613
Cdd:smart00387  56 KIFEPFFRTD-KRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
477-611 7.30e-30

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: 114.00  E-value: 7.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  477 GDVLRIRQILTNLISNAIKFT-HEGNVGIKLqvisepsfvrdnalnadteeheqngltETSVWICCDVWDTGIGIPENAL 555
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTL---------------------------SEGGELTLTVEDNGIGIPPEDL 53
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869  556 PCLFKKYMQASAdhaRKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:pfam02518  54 PRIFEPFSTADK---RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
371-922 1.64e-70

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 251.69  E-value: 1.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 371 LATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKFRPREVVKHVL 450
Cdd:PRK11107 297 LANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVV 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 451 QTAAASL-KKSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGNVGIKLqvisepsfvrdnalnadteehEQ 529
Cdd:PRK11107 377 TLLAHSAhEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILV---------------------EL 435
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 530 NGLTETSVWICCDVWDTGIGIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFI 609
Cdd:PRK11107 436 RALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFH 515
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 610 LPYKVGR---SDDYSDDQ-----------DEFSDMADQQ----------SEPDDTAEGYFQFKPLLGSIYSNGgpgiSND 665
Cdd:PRK11107 516 LPLDLNPnpiIDGLPTDClagkrllyvepNSAAAQATLDilsetplevtYSPTLSQLPEAHYDILLLGLPVTF----REP 591
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 666 FLPHKVMLtSPIKLINGFVADPSNNTGQSEMLQLENGGYMdeskletssgHC---PESAHQYengngrcfskesescsss 742
Cdd:PRK11107 592 LTMLHERL-AKAKSMTDFLILALPCHEQVLAEQLKQDGAD----------AClskPLSHTRL------------------ 642
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 743 qasseggtlemeSELTVSSHREEEKAETEVKETSK-P-KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSS 820
Cdd:PRK11107 643 ------------LPALLEPCHHKQPPLLPPTDESRlPlTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQR 710
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 821 SYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaaieagvdiSTSENEQVcmrptnrlPIIAMTANTLAESSEECYANGM 900
Cdd:PRK11107 711 PFDLILMDIQMPGMDGIRACELIR------------------QLPHNQNT--------PIIAVTAHAMAGERERLLSAGM 764
                        570       580
                 ....*....|....*....|..
gi 145357869 901 DSFISKPVTLQKLRECLQQYLH 922
Cdd:PRK11107 765 DDYLAKPIDEAMLKQVLLRYKP 786
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
340-611 1.77e-67

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 228.25  E-value: 1.77e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 340 LREDNAVRKAMESELNKTIHITEETMRAK-QMLATMSHEIRSPLSGVVGMAEILSTTkLDKEQRQLLNVMISSGDLVLQL 418
Cdd:COG0642   82 LLLLLLLLLLLLLLLLALLLLLEEANEAKsRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 419 INDILDLSKVESGVMRLEATKFRPREVVKHVLQTAAASL-KKSLTLEGNIADDVPIeVVGDVLRIRQILTNLISNAIKFT 497
Cdd:COG0642  161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAeEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYT 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 498 HEGNVgIKLQVisepsfvrdnalnadteeheqnglTETSVWICCDVWDTGIGIPENALPCLFKKYMQAsaDHARKYGGTG 577
Cdd:COG0642  240 PEGGT-VTVSV------------------------RREGDRVRISVEDTGPGIPPEDLERIFEPFFRT--DPSRRGGGTG 292
                        250       260       270
                 ....*....|....*....|....*....|....
gi 145357869 578 LGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:COG0642  293 LGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLP 326
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
343-920 2.84e-66

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 239.49  E-value: 2.84e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 343 DNAVRKAMESELNKTIHITEETMRAKQM-LATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLIND 421
Cdd:PRK10841 422 DVSARVKMEESLQEMAQAAEQASQSKSMfLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISD 501
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 422 ILDLSKVESGVMRLEATKFRPREVVKHVlqTA---AASLKKSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTH 498
Cdd:PRK10841 502 ILDFSKIESEQLKIEPREFSPREVINHI--TAnylPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTD 579
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 499 EGnvGIKLQVisepsFVRDNALnadteeheqngltetsvwiCCDVWDTGIGIPENALPCLFKKYMQASADHARKYGGTGL 578
Cdd:PRK10841 580 TG--CIVLHV-----RVDGDYL-------------------SFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGL 633
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 579 GLAICKQLVELMGGQLTVTSRVSEGSTFTFILP-YKV-GRSDDYSDD-QDEFSDMADQQSEPDDTAEGYFQFKPLLGSIY 655
Cdd:PRK10841 634 GLAICEKLINMMDGDISVDSEPGMGSQFTIRIPlYGAqYPQKKGVEGlQGKRCWLAVRNASLEQFLETLLQRSGIQVQRY 713
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 656 SNGGPGisndflPHKVMLTspiklingfvaDPSNNTGQSEMLQLENGGYMDESKLETSSG---HCPESAHQYENGNGRCF 732
Cdd:PRK10841 714 EGQEPT------PEDVLIT-----------DDPVQKKWQGRAVITFCRRHIGIPLEIAPGewvHSTATPHELPALLARIY 776
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 733 SkesescsssqassegGTLEMESELTVSShreeeKAETEVKETSKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVE 812
Cdd:PRK10841 777 R---------------IELESDDSANALP-----STDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVD 836
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 813 AITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETgnwnaaieagvdistseneqvcmrptnrLPIIAMTANTLAESS 892
Cdd:PRK10841 837 ALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLT----------------------------LPVIGVTANALAEEK 888
                        570       580
                 ....*....|....*....|....*...
gi 145357869 893 EECYANGMDSFISKPVTLQKLRECLQQY 920
Cdd:PRK10841 889 QRCLEAGMDSCLSKPVTLDVLKQTLTVY 916
PRK15347 PRK15347
two component system sensor kinase;
345-917 1.34e-64

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 234.54  E-value: 1.34e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 345 AVRKAMESELNKTIHITeetmrakqmlaTMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILD 424
Cdd:PRK15347 387 AKQRAEQANKRKSEHLT-----------TISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLD 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 425 LSKVESGVMRLEATKFRPREVVKHVLQT-AAASLKKSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGnvG 503
Cdd:PRK15347 456 FSRIESGQMTLSLEETALLPLLDQAMLTiQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETG--G 533
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 504 IKLQVisepsfvrdnalnadteEHEQNGLtetsvwiCCDVWDTGIGIPENALPCLFKKYMQASaDHArkyGGTGLGLAIC 583
Cdd:PRK15347 534 IRLRV-----------------KRHEQQL-------CFTVEDTGCGIDIQQQQQIFTPFYQAD-THS---QGTGLGLTIA 585
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 584 KQLVELMGGQLTVTSRVSEGSTFTFILPykvgrsddysddqdeFSDMAdqqsEPddtaegyfqfKPLLGSIysnggpgis 663
Cdd:PRK15347 586 SSLAKMMGGELTLFSTPGVGSCFSLVLP---------------LNEYA----PP----------EPLKGEL--------- 627
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 664 ndflphkvmlTSPIKLINgfvadpsnntgqsemlQLENGGYMDESKLETSSGHCPESAHQyengNGRCFSKesescsssq 743
Cdd:PRK15347 628 ----------SAPLALHR----------------QLSAWGITCQPGHQNPALLDPELAYL----PGRLYDL--------- 668
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 744 asseggtleMESELTVSSHREEEKAETEvketskP---KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSS 820
Cdd:PRK15347 669 ---------LQQIIQGAPNEPVINLPLQ------PwqlQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQH 733
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 821 SYDLVLMDVCMPVLDGLKATRLIRSYeetgnwnaaiEAGVDistSEneqvCMrptnrlpIIAMTANTLAESSEECYANGM 900
Cdd:PRK15347 734 RFDLVLMDIRMPGLDGLETTQLWRDD----------PNNLD---PD----CM-------IVALTANAAPEEIHRCKKAGM 789
                        570
                 ....*....|....*..
gi 145357869 901 DSFISKPVTLQKLRECL 917
Cdd:PRK15347 790 NHYLTKPVTLAQLARAL 806
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
362-921 8.93e-64

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: 232.75  E-value: 8.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  362 EETMRAK-QMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKF 440
Cdd:TIGR02956 458 EEANRAKsAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPF 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  441 RPREVVKHVLQ-TAAASLKKSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGNVGIKLQVISEPSfvrdna 519
Cdd:TIGR02956 538 DLNALLDDVHHlMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSS------ 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  520 lnadteeheqngltetsvwICCDVWDTGIGIPENALPCLFKKYMQAsaDHARKYGGTGLGLAICKQLVELMGGQLTVTSR 599
Cdd:TIGR02956 612 -------------------LLFEVEDTGCGIAEEEQATLFDAFTQA--DGRRRSGGTGLGLAISQRLVEAMDGELGVESE 670
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  600 VSEGSTFTFILPykvgrsddysddqdefsdmadqqsepddtaegyfqfkpllgsiysnggpgisndfLPHkvmltspikl 679
Cdd:TIGR02956 671 LGVGSCFWFTLP-------------------------------------------------------LTR---------- 685
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  680 ingfvADPSNNTGQSEMLQLenggymdeskletssghcpesahqyengngrcfskesescsssqasseggtlemeseltv 759
Cdd:TIGR02956 686 -----GKPAEDSATLTVIDL------------------------------------------------------------ 700
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  760 sshreeekaetevketSKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKA 839
Cdd:TIGR02956 701 ----------------PPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTL 764
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  840 TRLIRSYEETgnwnaaieagvdistseneqvcmrpTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQ 919
Cdd:TIGR02956 765 LQQLRAIYGA-------------------------KNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819

                  ..
gi 145357869  920 YL 921
Cdd:TIGR02956 820 IL 821
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
360-611 3.74e-61

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 212.88  E-value: 3.74e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 360 ITE----ETMRaKQMLATMSHEIRSPLSGVVGMAEILST--TKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVM 433
Cdd:COG5002  155 ITElerlEQMR-REFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGEL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 434 RLEATKFRPREVVKHVLQTAAASL-KKSLTLEGNIADDvPIEVVGDVLRIRQILTNLISNAIKFTHEGNVgIKLQVISEP 512
Cdd:COG5002  234 KLEKEPVDLAELLEEVVEELRPLAeEKGIELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTPEGGT-ITVSLREED 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 513 SFVRdnalnadteeheqngltetsvwicCDVWDTGIGIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGG 592
Cdd:COG5002  312 DQVR------------------------ISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGG 367
                        250
                 ....*....|....*....
gi 145357869 593 QLTVTSRVSEGSTFTFILP 611
Cdd:COG5002  368 RIWVESEPGKGTTFTITLP 386
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
353-611 9.14e-61

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 206.68  E-value: 9.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 353 ELNKTIHITEETMRAK-QMLATMSHEIRSPLSGVVGMAEIL--STTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVE 429
Cdd:COG2205    1 ELEEALEELEELERLKsEFLANVSHELRTPLTSILGAAELLldEEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 430 SGVMRLEATKFRPREVVKHVLQTAAASL-KKSLTLEGNIADDvPIEVVGDVLRIRQILTNLISNAIKFTHEG-NVGIKLQ 507
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAeEKGIRLELDLPPE-LPLVYADPELLEQVLANLLDNAIKYSPPGgTITISAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 508 VISEpsfvrdnalnadteeheqngltetsvWICCDVWDTGIGIPENALPCLFKKYMQAsaDHARKYGGTGLGLAICKQLV 587
Cdd:COG2205  160 REGD--------------------------GVRISVSDNGPGIPEEELERIFERFYRG--DNSRGEGGTGLGLAIVKRIV 211
                        250       260
                 ....*....|....*....|....
gi 145357869 588 ELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:COG2205  212 EAHGGTIWVESEPGGGTTFTVTLP 235
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
309-922 1.60e-49

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 188.23  E-value: 1.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 309 PVYNKAGEKIGINYMGMEVTDQvvKREKMAKlreDNAVRkameselNKTIHIteetmrakqmlATMSHEIRSPLSGVVGM 388
Cdd:PRK11091 248 PFYDRVGKRHGLMGFGRDITER--KRYQDAL---EKASR-------DKTTFI-----------STISHELRTPLNGIVGL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 389 AEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKFRPREVVKHvLQTAAASL--KKSLTLEGN 466
Cdd:PRK11091 305 SRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLAD-LENLSGLQaeQKGLRFDLE 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 467 IADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGnvGIKLQVISEPsfvrdnalNADteeheqngltetsvwICCDVWDT 546
Cdd:PRK11091 384 PLLPLPHKVITDGTRLRQILWNLISNAVKFTQQG--GVTVRVRYEE--------GDM---------------LTFEVEDS 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 547 GIGIPENALPCLFKKYMQASADHARKYG-GTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILPykvgrsddysddqd 625
Cdd:PRK11091 439 GIGIPEDELDKIFAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIH-------------- 504
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 626 efsdmadqqsepddtaegyfqfkpllgsiysnggpgisndflphkvmltspiklingfvadpsnntgqsemlqlenggym 705
Cdd:PRK11091     --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 706 deskletssghcpesahqyengngrcfskesescsssqasseggtlemeseLTVSSHREEEKAETEVKETSKPKILLVED 785
Cdd:PRK11091 505 ---------------------------------------------------APAVAEEVEDAFDEDDMPLPALNILLVED 533
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 786 NKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwnaaiEAGVDists 865
Cdd:PRK11091 534 IELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRE-----------RYPRE---- 598
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 866 eneqvcmrptNRLPIIAMTANTLAEsSEECYANGMDSFISKPVTLQKLRECLQQYLH 922
Cdd:PRK11091 599 ----------DLPPLVALTANVLKD-KKEYLDAGMDDVLSKPLSVPALTAMIKKFWD 644
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
482-611 1.78e-49

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: 169.98  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFTHEGNVGIKLQVISEpsfvrdnalnadteeheqnglTETSVWICCDVWDTGIGIPENALPCLFKK 561
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEE---------------------EEDGVQLRFSVEDTGIGIPEEQQARLFEP 59
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145357869 562 YMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16922   60 FSQADSSTTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
780-917 1.19e-43

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: 153.78  E-value: 1.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETGnwnaaieag 859
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGG--------- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145357869 860 vdistseneqvcmrptNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECL 917
Cdd:cd17546   72 ----------------RRTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
362-616 4.03e-43

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 169.70  E-value: 4.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 362 EETMRAKQ-MLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESG--VMRLEAT 438
Cdd:PRK11466 438 EKASQAKSaFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDE 517
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 439 KFRPREVVKHVLQTAAASLK-KSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGNVGIKlqvisepsfvrd 517
Cdd:PRK11466 518 PFEPRPLLESTLQLMSGRVKgRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLR------------ 585
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 518 nalnadteeheqNGLTETSVWIccDVWDTGIGIPENALPCLFKKYMQASAdharKYGGTGLGLAICKQLVELMGGQLTVT 597
Cdd:PRK11466 586 ------------SRTDGEQWLV--EVEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTISSRLAQAMGGELSAT 647
                        250
                 ....*....|....*....
gi 145357869 598 SRVSEGSTFTFILPYKVGR 616
Cdd:PRK11466 648 STPEVGSCFCLRLPLRVAT 666
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
214-611 4.40e-42

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 157.70  E-value: 4.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 214 LKRAEGFLHFILQNAPIVMGHQDKDLRYLFIyNkyPS------LREQDILGKTDVEIFHGGgvKESEDFKREVLEKGKAS 287
Cdd:COG3852    2 LRESEELLRAILDSLPDAVIVLDADGRITYV-N--PAaerllgLSAEELLGRPLAELFPED--SPLRELLERALAEGQPV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 288 K-REITFTTDLFGSKTFLIYVEPVYNKAGEkIGINYMGMEVTDQVvkrekmaKLREDNAVRKAMESelnktihiteetmr 366
Cdd:COG3852   77 TeREVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERK-------RLERELRRAEKLAA-------------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 367 AKQMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVEsgvmRLEATKFRPREVV 446
Cdd:COG3852  135 VGELAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPR----PPEREPVNLHEVL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 447 KHVLQTAAASLKKSLTLEGNIADDVPiEVVGDVLRIRQILTNLISNAIKFTHEGNVgIKLQvisepsfvrdnalnADTEE 526
Cdd:COG3852  211 ERVLELLRAEAPKNIRIVRDYDPSLP-EVLGDPDQLIQVLLNLVRNAAEAMPEGGT-ITIR--------------TRVER 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 527 HEQNGLTETSVWICCDVWDTGIGIPENALPCLF------KKymqasadharkyGGTGLGLAICKQLVELMGGQLTVTSRV 600
Cdd:COG3852  275 QVTLGGLRPRLYVRIEVIDNGPGIPEEILDRIFepffttKE------------KGTGLGLAIVQKIVEQHGGTIEVESEP 342
                        410
                 ....*....|.
gi 145357869 601 SEGSTFTFILP 611
Cdd:COG3852  343 GKGTTFRIYLP 353
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
212-613 6.11e-42

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: 160.91  E-value: 6.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 212 QNLKRAEGFLHFILQNAPIVMGHQDKDLRYLFIYNKYPSL---REQDILGKTDVEIFHGGGVKESEDFKREVLEKGKASK 288
Cdd:COG5809  134 EALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLlgiSIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQ 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 289 REITFTTdlfgSKTFLIYVEPVYNKAGEKIGINYMGMevtdqVVKrekmaklreDNAVRKAMESELNKTihitEETMRAK 368
Cdd:COG5809  214 GEVRFWT----KDGRWRLLEASGAPIKKNGEVDGIVI-----IFR---------DITERKKLEELLRKS----EKLSVVG 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 369 QMLATMSHEIRSPLSGVVGMAEILSTTKlDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRleatKFRPREVVKH 448
Cdd:COG5809  272 ELAAGIAHEIRNPLTSLKGFIQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE----PKDLNTLIEE 346
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 449 V---LQTAAASLKKSLTLEgnIADDVPIeVVGDVLRIRQILTNLISNAIKFTHE-GNVGIKLQVIsEPSFVRdnalnadt 524
Cdd:COG5809  347 ViplLQPQALLKNVQIELE--LEDDIPD-ILGDENQLKQVFINLLKNAIEAMPEgGNITIETKAE-DDDKVV-------- 414
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 525 eeheqngltetsvwicCDVWDTGIGIPENALPCLFKKYmqasadHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGS 604
Cdd:COG5809  415 ----------------ISVTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGT 472

                 ....*....
gi 145357869 605 TFTFILPYK 613
Cdd:COG5809  473 TFSITLPIK 481
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
90-611 8.45e-42

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 160.72  E-value: 8.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  90 AVRLLKEELKNLDRQREEAEAKELKIIEEYKFESNEPENVPVLDETSDLFRRFRQKKRDALVDSKKIEIYEEFDTVAYWK 169
Cdd:COG4251   11 LLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 170 QKALSLEKMLEASTERERRLMEKLSESLKTMESQSAPVQELTQNLKRAEGFLHFILQNAPIVMGHQDKDLRYLFIYNKYP 249
Cdd:COG4251   91 LVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILAL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 250 SLREQDILGKTDVEIFHGGGVKESEDFKREVLEKGKASKREITFTTDLFGSKTFLIYVEPVYNKAGEKIGINYMGMEVTD 329
Cdd:COG4251  171 LLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLIL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 330 QVVKREKMAKLREDNAVRKAMESELnktihitEETMRAKQMLA-TMSHEIRSPLSGVVGMAEILST---TKLDKEQRQLL 405
Cdd:COG4251  251 VLELLELRLELEELEEELEERTAEL-------ERSNEELEQFAyVASHDLREPLRKISGFSQLLEEdygDKLDEEGREYL 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 406 NVMISSGDLVLQLINDILDLSKVESGVMRLEatKFRPREVVKHVLQTAAASLK-KSLTLEgniADDVPiEVVGDVLRIRQ 484
Cdd:COG4251  324 ERIRDAAERMQALIDDLLAYSRVGRQELEFE--PVDLNELLEEVLEDLEPRIEeRGAEIE---VGPLP-TVRGDPTLLRQ 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 485 ILTNLISNAIKFTHEGNVG-IKLQVISEPS----FVRDNalnadteeheqngltetsvwiccdvwdtGIGIPENALPCLF 559
Cdd:COG4251  398 VFQNLISNAIKYSRPGEPPrIEIGAEREGGewvfSVRDN----------------------------GIGIDPEYAEKIF 449
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145357869 560 KkyMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:COG4251  450 E--IFQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
774-922 1.78e-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: 133.82  E-value: 1.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 774 ETSKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETGNwn 853
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPD-- 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 854 aaieagvdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYLH 922
Cdd:COG0784   80 ------------------------IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
349-922 8.27e-35

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 144.11  E-value: 8.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  349 AMESELNKTIHiteETMRAKQMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQR-QLLNVMISSGDLVLQLINDILDLSK 427
Cdd:PRK09959  697 ALEVERNKAIN---ATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDK 773
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  428 VESGVMRLEATKFRPREVVK---HVLQTAAASLKKSLTLEGNIADDVPIEVvgDVLRIRQILTNLISNAIKFTHEGNVGI 504
Cdd:PRK09959  774 IESGNYQLQPQWVDIPTLVQntcHSFGAIAASKSIALSCSSTFPDHYLVKI--DPQAFKQVLSNLLSNALKFTTEGAVKI 851
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  505 KLQVISepsfVRDNalnadteeHEQNGLTetsvwiccdVWDTGIGIPENALPCLFKKYMQASAdhARKYGGTGLGLAICK 584
Cdd:PRK09959  852 TTSLGH----IDDN--------HAVIKMT---------IMDSGSGLSQEEQQQLFKRYSQTSA--GRQQTGSGLGLMICK 908
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  585 QLVELMGGQLTVTSRVSEGSTFTfilpykvgrsddysddqdefsdmadqqsepddtaegyfqfkpllgsiysnggpgisn 664
Cdd:PRK09959  909 ELIKNMQGDLSLESHPGIGTTFT--------------------------------------------------------- 931
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  665 dflphkvmLTSPIKLINGFVAdpsnntgqsemlqlenggymdeskletssghcpesahqyengngrcfskesescsssqa 744
Cdd:PRK09959  932 --------ITIPVEISQQVAT----------------------------------------------------------- 944
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  745 sseggtlemeseltvsshrEEEKAETEVKETSKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDL 824
Cdd:PRK09959  945 -------------------VEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDL 1005
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  825 VLMDVCMPVLDGLKATRLIRsyeetgnwnaaieagvdistsenEQvcmrpTNRLPIIAMTANTLAESSEECYANGMDSFI 904
Cdd:PRK09959 1006 LITDVNMPNMDGFELTRKLR-----------------------EQ-----NSSLPIWGLTANAQANEREKGLSCGMNLCL 1057
                         570
                  ....*....|....*...
gi 145357869  905 SKPVTLQKLRECLQQyLH 922
Cdd:PRK09959 1058 FKPLTLDVLKTHLSQ-LH 1074
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
193-611 2.50e-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: 133.93  E-value: 2.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 193 LSESLKTMESQsapVQELTQNLKRAEGFLHFILQNAPIVMGHQDKDLRYLFIyNKYPS----LREQDILGKTDVEIFhgg 268
Cdd:COG5000   67 LARAFNRMTDQ---LKEQREELEERRRYLETILENLPAGVIVLDADGRITLA-NPAAErllgIPLEELIGKPLEELL--- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 269 gvkeSEDFKREVLEKGKASKREITFTTDLFGSKTFLIYVEPVYNkAGEKIGINymgmEVTDqVVKREKMAKLREdnavrk 348
Cdd:COG5000  140 ----PELDLAELLREALERGWQEEIELTRDGRRTLLVRASPLRD-DGYVIVFD----DITE-LLRAERLAAWGE------ 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 349 ameselnktihiteetmrakqMLATMSHEIRSPLSGVVGMAEILSTTKLDK------EQRQLLNVMISSGDLVLQLINDI 422
Cdd:COG5000  204 ---------------------LARRIAHEIKNPLTPIQLSAERLRRKLADKleedreDLERALDTIIRQVDRLKRIVDEF 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 423 LDLSkvesgvmRLEATKFRP---REVVKHVLQTAAASLK-KSLTLEGNIADDVPiEVVGDVLRIRQILTNLISNAIKFTH 498
Cdd:COG5000  263 LDFA-------RLPEPQLEPvdlNELLREVLALYEPALKeKDIRLELDLDPDLP-EVLADRDQLEQVLINLLKNAIEAIE 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 499 E-GNVGIKLQVISEpsfvrdnalnadteeheqngltetsvWICCDVWDTGIGIPENALPCLF------KKymqasadhar 571
Cdd:COG5000  335 EgGEIEVSTRREDG--------------------------RVRIEVSDNGPGIPEEVLERIFepffttKP---------- 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 145357869 572 kyGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:COG5000  379 --KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLP 416
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
325-611 3.11e-33

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 132.23  E-value: 3.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 325 MEVTDQVVKREKMAKLREDNAVRKAMESELNKTihitEETMR--AK-----QMLATMSHEIRSPLSGVVGMAEILS---T 394
Cdd:COG4191   97 LLAALDAEENAELEELERDITELERAEEELREL----QEQLVqsEKlaalgELAAGIAHEINNPLAAILGNAELLRrrlE 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 395 TKLDKEQ-RQLLNVMISSGDLVLQLINDILDLSKVESGVMRleatKFRPREVVKHVLQTAAASLKKS-LTLEGNIADDVP 472
Cdd:COG4191  173 DEPDPEElREALERILEGAERAAEIVRSLRAFSRRDEEERE----PVDLNELIDEALELLRPRLKARgIEVELDLPPDLP 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 473 iEVVGDVLRIRQILTNLISNAIKFTHEGNVG-IKLQvisepsfvrdnalnadTEEHEQngltetsvWICCDVWDTGIGIP 551
Cdd:COG4191  249 -PVLGDPGQLEQVLLNLLINAIDAMEEGEGGrITIS----------------TRREGD--------YVVISVRDNGPGIP 303
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869 552 ENALPCLF------KkymqasadhaRKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:COG4191  304 PEVLERIFepffttK----------PVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
477-613 6.97e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 122.76  E-value: 6.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869   477 GDVLRIRQILTNLISNAIKFTHEGNVgIKLQVISEPSfvrdnalnadteeheqngltetsvWICCDVWDTGIGIPENALP 556
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGR-ITVTLERDGD------------------------HVEITVEDNGPGIPPEDLE 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869   557 CLFKKYMQASaDHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILPYK 613
Cdd:smart00387  56 KIFEPFFRTD-KRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
369-613 1.43e-30

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: 126.02  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 369 QMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKFRPREVVKH 448
Cdd:COG5808  243 TFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFDIIQEEIQRINQIVSEFLVLGKPTAKKLELDDLNELIEEILSI 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 449 VLQTAAaslKKSLTLEGNIADDvPIEVVGDVLRIRQILTNLISNAIKFTHEGNvgiKLQVISEPsfvrdnalnadteehe 528
Cdd:COG5808  323 IDSEAN---LKNIRVEKQSLDE-PLHIKCDKDRIKQVLLNLIKNAIEAMKEGG---KLTISIEN---------------- 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 529 qnglTETSVWIccDVWDTGIGIPENALPCLFKKYMqasadhARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTF 608
Cdd:COG5808  380 ----DDEKAVI--EVIDNGEGIPEDIIDEIFEPFV------TTKEGGTGLGLSVCKRIVEMHGGEIDIESEEGKGTTFTI 447

                 ....*
gi 145357869 609 ILPYK 613
Cdd:COG5808  448 RLPLK 452
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
477-611 7.30e-30

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: 114.00  E-value: 7.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  477 GDVLRIRQILTNLISNAIKFT-HEGNVGIKLqvisepsfvrdnalnadteeheqngltETSVWICCDVWDTGIGIPENAL 555
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTL---------------------------SEGGELTLTVEDNGIGIPPEDL 53
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869  556 PCLFKKYMQASAdhaRKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:pfam02518  54 PRIFEPFSTADK---RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
777-914 4.43e-29

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: 114.62  E-value: 4.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 777 KPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEEtgnwnaai 856
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPR-------- 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145357869 857 eagvdistseneqvcmrpTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLR 914
Cdd:COG3706   73 ------------------TADIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELL 112
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
482-610 8.03e-28

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: 108.07  E-value: 8.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFTHEGNVgIKLQVISEPSfvrdnalnadteeheqngltetsvWICCDVWDTGIGIPENALPCLFKK 561
Cdd:cd00075    1 LEQVLSNLLDNALKYSPPGGT-IEISLRQEGD------------------------GVVLEVEDNGPGIPEEDLERIFER 55
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 145357869 562 YmqASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFIL 610
Cdd:cd00075   56 F--YRGDKSREGGGTGLGLAIVRRIVEAHGGRITVESEPGGGTTFTVTL 102
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
214-611 1.10e-26

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: 115.21  E-value: 1.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 214 LKRAEGFLHFILQNAPIVMGHQDKDLRYLFIYNKYPSL---REQDILGKTDVEIFHgggVKESEDFKrEVLEKGKASKRE 290
Cdd:COG5805  152 LQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLfgaPREELIGKNLLELLH---PCDKEEFK-ERIESITEVWQE 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 291 ITFTTDLFGSKTFLIYVE----PVYNKAGEKIGINYMGMEVTDqvvkrekmaklrednavRKAMESELNKTihiteETMR 366
Cdd:COG5805  228 FIIEREIITKDGRIRYFEavivPLIDTDGSVKGILVILRDITE-----------------KKEAEELMARS-----EKLS 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 367 -AKQMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQrqLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKFRPREV 445
Cdd:COG5805  286 iAGQLAAGIAHEIRNPLTSIKGFLQLLQPGIEDKEE--YFDIMLSELDRIESIISEFLALAKPQAVNKEKENINELIQDV 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 446 VkhVLQTAAASLK-KSLTLEGNiaDDVPiEVVGDVLRIRQILTNLISNAIKFTHEGNVgIKLQVISEPSFVRdnalnadt 524
Cdd:COG5805  364 V--TLLETEAILHnIQIRLELL--DEDP-FIYCDENQIKQVFINLIKNAIEAMPNGGT-ITIHTEEEDNSVI-------- 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 525 eeheqngltetsvwicCDVWDTGIGIPENALPCLFKKYMQAsadharKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGS 604
Cdd:COG5805  430 ----------------IRVIDEGIGIPEERLKKLGEPFFTT------KEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGT 487

                 ....*..
gi 145357869 605 TFTFILP 611
Cdd:COG5805  488 TFTITLP 494
PRK10490 PRK10490
sensor protein KdpD; Provisional
350-611 1.24e-26

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 117.06  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 350 MESELNKTIHITEETMRaKQMLATMSHEIRSPLSGVVGMAEILsTTKLDKEQ-----------RQLLNVMissgdlvlQL 418
Cdd:PRK10490 648 TASEEQARLASEREQLR-NALLAALSHDLRTPLTVLFGQAEIL-TLDLASEGspharqaseirQQVLNTT--------RL 717
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 419 INDILDLSKVESGVMRLEATKFRPREVVKHVLQTAAASLKKSlTLEGNIADDVPIeVVGDVLRIRQILTNLISNAIKFTH 498
Cdd:PRK10490 718 VNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGH-PINLSLPEPLTL-IHVDGPLFERVLINLLENAVKYAG 795
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 499 EG-NVGIKLQVISEpsfvrdnalnadteeheqngltetsvWICCDVWDTGIGIPENALPCLFKKYMQASADHArkYGGTG 577
Cdd:PRK10490 796 AQaEIGIDAHVEGE--------------------------RLQLDVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVG 847
                        250       260       270
                 ....*....|....*....|....*....|....
gi 145357869 578 LGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:PRK10490 848 LGLAICRAIVEVHGGTIWAENRPEGGACFRVTLP 881
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
363-611 9.02e-26

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 111.86  E-value: 9.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 363 ETMRAK--------QMLATMSHEIRSPLSGVVGMAEILSTTkLDKEQRQLLNVMISSGDLVLQ-LINDILDLSKVESGVM 433
Cdd:PRK11100 244 ESMRVKlegkayveQYVQTLTHELKSPLAAIRGAAELLQED-PPPEDRARFTGNILTQSARLQqLIDRLLELARLEQRQE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 434 RLEATKFRPREVVKHVLQTAAASL-KKSLTLEGNIADdvpIEVVGDVLRIRQILTNLISNAIKFTHEGN-VGIKLQVISE 511
Cdd:PRK11100 323 LEVLEPVALAALLEELVEAREAQAaAKGITLRLRPDD---ARVLGDPFLLRQALGNLLDNAIDFSPEGGtITLSAEVDGE 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 512 PSFVRdnalnadteeheqngltetsvwiccdVWDTGIGIPENALPCLFKK-YMQASADHARKygGTGLGLAICKQLVELM 590
Cdd:PRK11100 400 QVALS--------------------------VEDQGPGIPDYALPRIFERfYSLPRPANGRK--STGLGLAFVREVARLH 451
                        250       260
                 ....*....|....*....|.
gi 145357869 591 GGQLTVTSRVSEGSTFTFILP 611
Cdd:PRK11100 452 GGEVTLRNRPEGGVLATLTLP 472
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
362-619 1.25e-25

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 111.42  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 362 EETMRAKQMLATM-------SHEIRSPLSGVVGMAEILST-TKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESgvM 433
Cdd:PRK10364 225 QDEMKRKEKLVALghlaagvAHEIRNPLSSIKGLAKYFAErAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTH--L 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 434 RLEATkfRPREVVKHVLQTAAASL-KKSLTLEGNIADDVPiEVVGDVLRIRQILTNLISNAIKFTHEGNVgiklqvisep 512
Cdd:PRK10364 303 ALQAV--DLNDLINHSLQLVSQDAnSREIQLRFTANDTLP-EIQADPDRLTQVLLNLYLNAIQAIGQHGV---------- 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 513 sfvrdnaLNADTEEHEQNgltetsvwICCDVWDTGIGIPENALPCLFKKYMQASADharkygGTGLGLAICKQLVELMGG 592
Cdd:PRK10364 370 -------ISVTASESGAG--------VKISVTDSGKGIAADQLEAIFTPYFTTKAE------GTGLGLAVVHNIVEQHGG 428
                        250       260
                 ....*....|....*....|....*..
gi 145357869 593 QLTVTSRVSEGSTFTFILPYKVGRSDD 619
Cdd:PRK10364 429 TIQVASQEGKGATFTLWLPVNITRRDP 455
PRK09303 PRK09303
histidine kinase;
369-611 4.33e-25

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 108.50  E-value: 4.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 369 QMLATMSHEIRSPLSGVVGMAEIL-------STTKLDKEQRQLLNVMISSGDLVLQLINDILdlskvESGVMRLEATKFR 441
Cdd:PRK09303 153 RVLAMLAHDLRTPLTAASLALETLelgqideDTELKPALIEQLQDQARRQLEEIERLITDLL-----EVGRTRWEALRFN 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 442 PREVV------KHVLQTAAASLKKSLTLEGNIADDVPiEVVGDVLRIRQILTNLISNAIKFTHEGNVgIKLqvisepsfv 515
Cdd:PRK09303 228 PQKLDlgslcqEVILELEKRWLAKSLEIQTDIPSDLP-SVYADQERIRQVLLNLLDNAIKYTPEGGT-ITL--------- 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 516 rdnalnadteeheqNGLTETSVWICCDVWDTGIGIPENALPCLFKkymqasaDHAR-----KYGGTGLGLAICKQLVELM 590
Cdd:PRK09303 297 --------------SMLHRTTQKVQVSICDTGPGIPEEEQERIFE-------DRVRlprdeGTEGYGIGLSVCRRIVRVH 355
                        250       260
                 ....*....|....*....|.
gi 145357869 591 GGQLTVTSRVSEGSTFTFILP 611
Cdd:PRK09303 356 YGQIWVDSEPGQGSCFHFTLP 376
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
776-922 5.12e-22

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: 95.62  E-value: 5.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 776 SKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwnaa 855
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRA---------- 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 856 ieagvdistseneqvcMRPTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYLH 922
Cdd:COG3437   75 ----------------DPSTRDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
777-921 1.58e-20

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: 90.79  E-value: 1.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 777 KPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEetgnwnaai 856
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--------- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 857 eagvdistseneqvcmrptNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYL 921
Cdd:COG0745   72 -------------------SDIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
278-618 1.78e-20

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 96.58  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 278 REVLEKGKASK-REITFTTDlfgSKTFLIYV--EPVYNKAGEKIGINYMGMEVTDQVVKREKMAKlrednAVRKAMESEL 354
Cdd:PRK11360 322 LDTLEHGTEHVdLEISFPGR---DRTIELSVstSLLHNTHGEMIGALVIFSDLTERKRLQRRVAR-----QERLAALGEL 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 355 nktihiteetmrakqmLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMR 434
Cdd:PRK11360 394 ----------------VAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQ 457
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 435 leatKFRPREVVKHVLQTAAASLKKS-LTLEGNIADDVPiEVVGDVLRIRQILTNLISNAikfthegnvgikLQVISEps 513
Cdd:PRK11360 458 ----PVSLNALVEEVLQLFQTAGVQArVDFETELDNELP-PIWADPELLKQVLLNILINA------------VQAISA-- 518
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 514 fvrdnalnadteeheqNGLTETSVWICCD------VWDTGIGIPENALPCLFKKYMQAsadharKYGGTGLGLAICKQLV 587
Cdd:PRK11360 519 ----------------RGKIRIRTWQYSDgqvavsIEDNGCGIDPELLKKIFDPFFTT------KAKGTGLGLALSQRII 576
                        330       340       350
                 ....*....|....*....|....*....|.
gi 145357869 588 ELMGGQLTVTSRVSEGSTFTFILPYKVGRSD 618
Cdd:PRK11360 577 NAHGGDIEVESEPGVGTTFTLYLPINPQGNQ 607
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
781-907 1.07e-19

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: 84.59  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 781 LLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEetgnwnaaieagv 860
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP------------- 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 145357869 861 distseneqvcmrptNRLPIIAMTANTLAESSEECYANGMDSFISKP 907
Cdd:cd00156   68 ---------------PDIPVIVLTAKADEEDAVRALELGADDYLVKP 99
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
354-613 1.44e-19

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: 92.24  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 354 LNKTIHITEETMRAK------QMLATMSHEIRSPLSGVVGMAEILSTTKL-DKEQRQLLNVMISSGDLVLQLINDILDLS 426
Cdd:COG5806  182 LIENILLRKELQRAEklevvsELAASIAHEVRNPLTVVRGFIQLLQEPELsDEKRKQYIRIALEELDRAEAIITDYLTFA 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 427 KVESGVMrleaTKFRPREVVKHVLQTAAA-SLKKSLTLEGNIADdvPIEVVGDVLRIRQILTNLISNAIKFTHEGNVgik 505
Cdd:COG5806  262 KPQPEKL----EKIDVSEELEHVIDVLSPyANMNNVEIQTELEP--GLYIEGDRQKLQQCLINIIKNGIEAMPNGGT--- 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 506 lqvisepsfvrdnaLNADTEEHEQNgltetsVWICcdVWDTGIGipenalpclfkkyMqaSADHARKYG---------GT 576
Cdd:COG5806  333 --------------LTIDVSIDKNK------VIIS--IKDTGVG-------------M--TKEQLERLGepyfstkekGT 375
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 145357869 577 GLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILPYK 613
Cdd:COG5806  376 GLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLPLA 412
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
368-612 2.01e-19

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 93.84  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 368 KQMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKFRPREVVK 447
Cdd:PRK10618 451 KAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLID 530
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 448 HVLQTAAASLK-KSLTLEGNIADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGNVGiklqvisepsfvrdnaLNADTEE 526
Cdd:PRK10618 531 EVLPEVLPAIKrKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKIT----------------LEVDQDE 594
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 527 HEQNGLTetsvwicCDVWDTGIGIPENALPCLFKKYM-QASADharKYG-GTGLGLAICKQLVELMGGQLTVTSRVSEGS 604
Cdd:PRK10618 595 SSPDRLT-------IRILDTGAGVSIKELDNLHFPFLnQTQGD---RYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGT 664

                 ....*...
gi 145357869 605 TFTFILPY 612
Cdd:PRK10618 665 RYSIHLKM 672
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
369-431 3.66e-19

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 82.26  E-value: 3.66e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145357869  369 QMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESG 431
Cdd:pfam00512   4 EFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
368-431 9.81e-19

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 80.69  E-value: 9.81e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145357869   368 KQMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESG 431
Cdd:smart00388   3 REFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
482-611 1.43e-18

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: 81.60  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFTHEG---NVGIKLQVISEPS--FVRDNalnadteeheqngltetsvwiccdvwdtGIGIPENALP 556
Cdd:cd16921    1 LGQVLTNLLGNAIKFRRPRrppRIEVGAEDVGEEWtfYVRDN----------------------------GIGIDPEYAE 52
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 557 CLFKKYMQASADHArkYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16921   53 KVFGIFQRLHSREE--YEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
779-917 3.67e-18

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: 80.91  E-value: 3.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINS--SSYDLVLMDVCMPVLDGLKATRLIRSYEETGNWnaai 856
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaeHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRER---- 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 857 eagvdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECL 917
Cdd:cd19933   78 ---------------------PLIVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
776-922 3.69e-18

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 88.10  E-value: 3.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 776 SKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwnaa 855
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA---------- 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 856 ieagvdistseneqvcMRPtnRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYLH 922
Cdd:COG2204   71 ----------------LDP--DLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE 119
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
780-915 4.02e-18

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: 80.66  E-value: 4.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869  780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETgnwnaaieag 859
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT---------- 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869  860 vdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRE 915
Cdd:pfam00072  71 ------------------TPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLA 108
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
375-611 4.57e-18

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 89.35  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 375 SHEIRSPLSGVVGMAEI-LSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRleatKFRPREVVKHVLQTA 453
Cdd:PRK13837 458 AHNFNNILGAILGYAEMaLNKLARHSRAARYIDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSELVTEIAPLL 533
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 454 AASLKKSLTLEGNIADDvPIEVVGDVLRIRQILTNLISNAIK-FTHEGNVGIKLQVISEPSFVRDNALNADTEEHeqngl 532
Cdd:PRK13837 534 RVSLPPGVELDFDQDQE-PAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKLRAPKVLSHGVLPPGRY----- 607
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 533 tetsVWICcdVWDTGIGIPENALPCLFKKYMQASAdharkyGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:PRK13837 608 ----VLLR--VSDTGAGIDEAVLPHIFEPFFTTRA------GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLP 674
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
775-921 1.07e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 80.40  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 775 TSKPKILLVEDNKINIMVAKSMMKQLG--HTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnw 852
Cdd:COG4565    1 MKMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELR-------- 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 853 naaiEAGVDIstseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYL 921
Cdd:COG4565   73 ----ARGPDV----------------DVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYL 121
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
478-611 1.58e-17

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: 79.07  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 478 DVLRIRQILTNLISNAIKFTHEGNvgiklqvisepsfvrdnALNADTEEHEQNGLTETsvwiccdVWDTGIGIPENALPC 557
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGG-----------------RIRCILEKFRLNRFLLT-------VSDSGPGIPPNLREE 56
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 145357869 558 LFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16925   57 IFERFRQGDGSSTRAHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
779-913 1.23e-16

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: 76.42  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaaiea 858
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLK-------------- 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 859 gvdistsENEQvcmrpTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKL 913
Cdd:cd17548   67 -------EDPA-----TRDIPVIALTAYAMKGDREKILEAGCDGYISKPIDTREF 109
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
363-611 4.32e-16

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 81.60  E-value: 4.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 363 ETMRaKQMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQ-LLNVMISSGDLVLQLINDILDLSKVESG-VMRLEatkf 440
Cdd:PRK11006 201 EGAR-RNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREkALHTMREQTQRMEGLVKQLLTLSKIEAApTIDLN---- 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 441 rprEVVK-----HVLQTAAASL-KKSLTLEGNIadDVPIEVVGDVLRIRQILTNLISNAIKFTHEG-NVGIKLQviseps 513
Cdd:PRK11006 276 ---EKVDvpmmlRVLEREAQTLsQGKHTITFEV--DNSLKVFGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQ------ 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 514 fvrdnalnadteeheqngltETSVWICCDVWDTGIGIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQ 593
Cdd:PRK11006 345 --------------------RVPQGAEFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSR 404
                        250
                 ....*....|....*...
gi 145357869 594 LTVTSRVSEGSTFTFILP 611
Cdd:PRK11006 405 LEIESEVGKGTRFSFVLP 422
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
372-611 9.42e-16

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 80.97  E-value: 9.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 372 ATMSHEIRSPLSGVVGMAEI-LSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKVESGVMRLEATKFRPREVVKHVL 450
Cdd:PRK09835 267 ADIAHEIRTPITNLITQTEIaLSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADEVGKVF 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 451 QTAAA-SLKKSLTLEgniADDVPIEVVGDVLRIRQILTNLISNAIKFTHEGN-VGIKLQVisepsfvrdnalnadteehe 528
Cdd:PRK09835 347 DFFEAwAEERGVELR---FVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQE-------------------- 403
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 529 qnglTETSVWICcdVWDTGIGIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVsEGSTFTF 608
Cdd:PRK09835 404 ----VDHQVQLV--VENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVI 476

                 ...
gi 145357869 609 ILP 611
Cdd:PRK09835 477 SLP 479
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
470-610 8.42e-15

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


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 71.78  E-value: 8.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 470 DVPIEVVGDVLRIRQILTNLISNAIKFTHEGN-VGIklqvisepsFVRDNalnadteeheqngltETSVWIccDVWDTGI 548
Cdd:cd16947    9 DRPIYANANTEALQRILKNLISNAIKYGSDGKfLGM---------TLRED---------------EKHVYI--DIWDKGK 62
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145357869 549 GIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFIL 610
Cdd:cd16947   63 GISETEKDHVFERLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
482-611 2.35e-14

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: 69.73  E-value: 2.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFTHEGNV-GIKLQVISEPSfvrdnalnadteeheqnglTETSVWICcdVWDTGIGIPENALPCLFK 560
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGGCeRRELTIRTSPA-------------------DDRAVTIS--VKDTGPGIAEEVAGQLFD 59
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145357869 561 KYMQASADharkygGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16920   60 PFYTTKSE------GLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
482-611 2.39e-14

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 69.92  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFTHEGNVgIKLQVISEPSFVRdnalnadteeheqngltetsvwicCDVWDTGIGIPENALPCLFKK 561
Cdd:cd16952    1 LRSAFSNLVSNAVKYTPPSDT-ITVRWSQEESGAR------------------------LSVEDTGPGIPPEHIPRLTER 55
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145357869 562 YMQASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16952   56 FYRVDIERCRNTGGTGLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFP 105
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
779-907 2.96e-14

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 69.42  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLG--HTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwnaai 856
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE----------- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145357869 857 eagvdistseneqvcMRPtnRLPIIAMTANTLAESSEECYANGMDSFISKP 907
Cdd:COG4753   70 ---------------LDP--DTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
481-594 4.36e-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: 69.03  E-value: 4.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 481 RIRQILTNLISNAIKFTHEGNVgIKLQVISEPSFVRdnalnadteeheqngltetsvwicCDVWDTGIGIPENALPCLFK 560
Cdd:cd16946    4 RLQQLFVNLLENSLRYTDTGGK-LRIRAAQTPQEVR------------------------LDVEDSAPGVSDDQLARLFE 58
                         90       100       110
                 ....*....|....*....|....*....|....
gi 145357869 561 KYMQASADHARKYGGTGLGLAICKQLVELMGGQL 594
Cdd:cd16946   59 RFYRVESSRNRASGGSGLGLAICHNIALAHGGTI 92
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
363-612 1.30e-13

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 74.28  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 363 ETMRAKQMlATMSHEIRSPLSGVVGMAEILS--TTKLDKEQrqlLNVMISSGDLVLQLINDILDLSKVESGVMrleATKF 440
Cdd:PRK10549 237 EQMRRDFM-ADISHELRTPLAVLRGELEAIQdgVRKFTPES---VASLQAEVGTLTKLVDDLHQLSLSDEGAL---AYRK 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 441 RPREVVkHVLQTAAASLK-----KSLTLEGNIADDVPieVVGDVLRIRQILTNLISNAIKFTHEGNvgiKLQVISEpsfv 515
Cdd:PRK10549 310 TPVDLV-PLLEVAGGAFRerfasRGLTLQLSLPDSAT--VFGDPDRLMQLFNNLLENSLRYTDSGG---SLHISAE---- 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 516 rdnalnadtEEHEQNGLTetsvWIccdvwDTGIGIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQLT 595
Cdd:PRK10549 380 ---------QRDKTLRLT----FA-----DSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRII 441
                        250
                 ....*....|....*..
gi 145357869 596 VTSRVSEGSTFTFILPY 612
Cdd:PRK10549 442 AAHSPFGGVSITVELPL 458
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
779-908 1.56e-13

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: 67.52  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETGNwnaaiea 858
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRH------- 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145357869 859 gvdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKPV 908
Cdd:cd17538   74 -------------------IPVIMITALDDREDRIRGLEAGADDFLSKPI 104
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
368-427 1.73e-13

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 66.08  E-value: 1.73e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 368 KQMLATMSHEIRSPLSGVVGMAEIL-STTKLDKEQRQLLNVMISSGDLVLQLINDILDLSK 427
Cdd:cd00082    5 GEFLANVSHELRTPLTAIRGALELLeEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
780-917 3.26e-13

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: 66.71  E-value: 3.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwnaaieag 859
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRE-------------- 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145357869 860 vdistseneqvcMRPTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECL 917
Cdd:cd17580   67 ------------LPWLANTPAIALTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
779-919 6.36e-13

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: 66.29  E-value: 6.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLG--HTMDIANNGVEAI-------TAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEET 849
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALdflrgegEYADAPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 850 gnwnaaieagvdistseneqvcmrptNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQ 919
Cdd:cd17557   81 --------------------------RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
472-603 8.45e-13

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: 65.50  E-value: 8.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 472 PIEVVGDVLRIRQILTNLISNAIKFTHEG-NVGIKLQVisepsfvRDNALNAdteeheqngltetsvwiccdVWDTGIGI 550
Cdd:cd16940    4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGsRVEIKLSA-------DDGAVIR--------------------VEDNGPGI 56
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145357869 551 PENALPCLFKKYMQASADHarkYGGTGLGLAICKQLVELMGGQLTVTSRVSEG 603
Cdd:cd16940   57 DEEELEALFERFYRSDGQN---YGGSGLGLSIVKRIVELHGGQIFLGNAQGGG 106
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
778-832 1.67e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 62.97  E-value: 1.67e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 145357869   778 PKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMP 832
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
781-907 1.75e-12

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: 64.35  E-value: 1.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 781 LLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaaiEAGV 860
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLR------------EKGS 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 145357869 861 DIstseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKP 907
Cdd:cd17574   69 DI----------------PIIMLTAKDEEEDKVLGLELGADDYITKP 99
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
780-908 2.00e-12

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 64.07  E-value: 2.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETgnwnaaieag 859
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPAT---------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 145357869 860 VDIstseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKPV 908
Cdd:cd19920   71 RHI----------------PVIFLTALTDTEDKVKGFELGAVDYITKPF 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
441-613 1.16e-11

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 67.57  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 441 RPREVVKHVLQTAAASLKKSLTLEGNIADDVpievvgdvlrIRQILTNLISNA----IKFTHEGNVGIKLQVISEPSFVR 516
Cdd:COG3290  215 EYDEALEYIDEISEELQELIDSLLSRIGNPV----------LAALLLGKAARArergIDLTIDIDSDLPDLPLSDTDLVT 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 517 ------DNALNADTEEHEQNG-----LTETSVWICCDVWDTGIGIPENALPCLFKKYMQASADHarkygGTGLGLAICKQ 585
Cdd:COG3290  285 ilgnllDNAIEAVEKLPEEERrvelsIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLGE-----GRGLGLALVKQ 359
                        170       180
                 ....*....|....*....|....*...
gi 145357869 586 LVELMGGQLTVTSRVSEGSTFTFILPYK 613
Cdd:COG3290  360 IVEKYGGTIEVESEEGEGTVFTVRLPKE 387
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
778-917 2.01e-11

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 61.69  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 778 PKILLVEDNKINIMVAKSMMKQLG-HTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaAI 856
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLR----------AL 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 857 EAGVDIstseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKPVtlqKLRECL 917
Cdd:cd17551   71 PGLEDV----------------PIVMITADTDREVRLRALEAGATDFLTKPF---DPVELL 112
envZ PRK09467
osmolarity sensor protein; Provisional
370-603 2.33e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 66.86  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 370 MLATMSHEIRSPLSGVvgmaeilsttKLDKEqrqllnvMISSGDLVLQ--LINDILDLSKVESGVM---RLEATKFRPRE 444
Cdd:PRK09467 232 LMAGVSHDLRTPLTRI----------RLATE-------MMSEEDGYLAesINKDIEECNAIIEQFIdylRTGQEMPMEMA 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 445 VVKHVLQTAAASLKKSltlEGNIADDV---PIEVVGDVLRIRQILTNLISNAIKFtheGNVGIKlqvISepsfvrdnaln 521
Cdd:PRK09467 295 DLNALLGEVIAAESGY---EREIETALqpgPIEVPMNPIAIKRALANLVVNAARY---GNGWIK---VS----------- 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 522 adteeheqNGLTETSVWICcdVWDTGIGIPENALPCLFKKYMQAsaDHARKYGGTGLGLAICKQLVELMGGQLTVTSRvS 601
Cdd:PRK09467 355 --------SGTEGKRAWFQ--VEDDGPGIPPEQLKHLFQPFTRG--DSARGSSGTGLGLAIVKRIVDQHNGKVELGNS-E 421

                 ..
gi 145357869 602 EG 603
Cdd:PRK09467 422 EG 423
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
482-603 4.27e-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: 4.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFtheGNVGIKLQVISEPSFVrdnalnadteeheqngltetsvWIccDVWDTGIGIPENALPCLFKK 561
Cdd:cd16950    1 LKRVLSNLVDNALRY---GGGWVEVSSDGEGNRT----------------------RI--QVLDNGPGIAPEEVDELFQP 53
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 145357869 562 YMQAsaDHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEG 603
Cdd:cd16950   54 FYRG--DNARGTSGTGLGLAIVQRISDAHGGSLTLANRAGGG 93
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
485-618 1.54e-10

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 64.55  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 485 ILTNLISN---AIKFTHEGNVGIKLqvisepsfvrdnalnadteeHEQNGltetsvWICCDVWDTGIGIPENALPCLFKK 561
Cdd:PRK11086 437 ILGNLIENaleAVGGEEGGEISVSL--------------------HYRNG------WLHCEVSDDGPGIAPDEIDAIFDK 490
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 562 ymqasaDHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILPYKVGRSD 618
Cdd:PRK11086 491 ------GYSTKGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIPWDGERSN 541
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
779-920 3.90e-10

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 57.93  E-value: 3.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKiniMVAKSMMKQLGHTMDI----ANNGVEAITAINSSSYDLVLMDVCMPVLDG---LKATRlIRSYEetgn 851
Cdd:cd17593    2 KVLICDDSS---MARKQLARALPADWDVeitfAENGEEALEILREGRIDVLFLDLTMPVMDGyevLEALP-VEQLE---- 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 852 wnaaieagvdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQY 920
Cdd:cd17593   74 --------------------------TKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
780-919 5.26e-10

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 57.91  E-value: 5.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKInIMVAKSMMKQLGHTMDI---ANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaai 856
Cdd:cd17535    1 VLIVDDHPL-VREGLRRLLESEPDIEVvgeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLR------------ 67
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145357869 857 eagvdistseneqvcmRPTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQ 919
Cdd:cd17535   68 ----------------RRYPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRA 114
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
484-611 5.84e-10

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: 57.34  E-value: 5.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 484 QILTNLISNAIKFThegnvgiklqvisePSFVRDNAlnadTEEHEQngltetsvWICcDVWDTGIGIPENALPCLFKKYM 563
Cdd:cd16949    3 RALENVLRNALRYS--------------PSKILLDI----SQDGDQ--------WTI-TITDDGPGVPEDQLEQIFLPFY 55
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 145357869 564 QASADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16949   56 RVDSARDRESGGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
778-918 7.36e-10

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: 57.42  E-value: 7.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 778 PKILLVEDNKINIMVAKSMMKQLGHTM-DIANNGVEAITAINSSSYDLVLMDVCMP-VLDGLKATRLIRSYeetgnwnaa 855
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK--------- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 856 ieagvdistseneqvcmrptNRLPIIAMTAN----TLaESSEECYANGmdsFISKPVTLQKLRECLQ 918
Cdd:cd17534   72 --------------------FDIPVIFLTAYsdeeTL-ERAKETNPYG---YLVKPFNERELKAAIE 114
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
780-919 7.80e-10

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: 57.25  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAI--NSSSYDLVLMDVCMPVLDGLKATRLIRSYEEtgnwnaaie 857
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIRLEMD--------- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145357869 858 agvdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQ 919
Cdd:cd17584   72 --------------------LPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQH 113
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
775-921 8.28e-10

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 62.17  E-value: 8.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 775 TSKPKILLVEDNK-INIMVAKSMMKQlGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEEtgnwn 853
Cdd:PRK11361   2 TAINRILIVDDEDnVRRMLSTAFALQ-GFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHET----- 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145357869 854 aaieagvdistseneqvcmrptnRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYL 921
Cdd:PRK11361  76 -----------------------RTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
517-611 1.65e-09

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: 55.76  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 517 DNALNADTEEHEQNG-----LTETSVWICCDVWDTGIGIPENALPCLFKKYMQASADharkyGGTGLGLAICKQLVELMG 591
Cdd:cd16915   10 DNALDALAATGAPNKqvevfLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQ-----GERGIGLALVRQSVERLG 84
                         90       100
                 ....*....|....*....|
gi 145357869 592 GQLTVTSRVSEGSTFTFILP 611
Cdd:cd16915   85 GSITVESEPGGGTTFSIRIP 104
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
779-918 1.69e-09

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 58.43  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTM-DIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwnaaie 857
Cdd:COG3707    5 RVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISE------------ 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 858 agvdistseneqvcmrpTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQ 918
Cdd:COG3707   73 -----------------ERPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALE 116
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
777-921 1.79e-09

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 61.20  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 777 KPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYeetgnwNAAI 856
Cdd:PRK10365   5 NIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL------NPAI 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 857 eagvdistseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYL 921
Cdd:PRK10365  79 ----------------------PVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
482-611 3.11e-09

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: 55.12  E-value: 3.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKfthegnvgiklqvisepsfvrdnALNADTEEHEQNGLTETSVWIccDVWDTGIGIPENALPCLFKK 561
Cdd:cd16943    4 LNQVLLNLLVNAAQ-----------------------AMEGRGRITIRTWAHVDQVLI--EVEDTGSGIDPEILGRIFDP 58
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145357869 562 YMQAsadhaRKYG-GTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16943   59 FFTT-----KPVGeGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
482-599 3.70e-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: 55.16  E-value: 3.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFTHEGNVgIKLQvisepsfvrdnaLNADTEEheqngltetsvwICCDVWDTGIGIPENALPCLFKK 561
Cdd:cd16945    5 LRQAINNLLDNAIDFSPEGGL-IALQ------------LEADTEG------------IELLVFDEGSGIPDYALNRVFER 59
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145357869 562 YMQASADHARKYGgTGLGLAICKQLVELMGGQLTVTSR 599
Cdd:cd16945   60 FYSLPRPHSGQKS-TGLGLAFVQEVAQLHGGRITLRNR 96
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
780-845 3.85e-09

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 54.75  E-value: 3.85e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 780 ILLVEDNKiniMVAKSMMKQL---GHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:cd19935    1 ILVVEDEK---KLAEYLKKGLteeGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA 66
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
781-844 5.36e-09

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: 54.92  E-value: 5.36e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 781 LLVEDNK-INIMVAKsMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIR 844
Cdd:cd17625    1 LVVEDEKdLSEAITK-HLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLR 64
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
778-846 5.52e-09

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: 54.98  E-value: 5.52e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 778 PKILLVEDNKINIMVAKSMMKQLG-HTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSY 846
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKI 70
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
482-611 6.98e-09

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: 54.21  E-value: 6.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQIltnlISNAIKFTHEGNvgiKLQVISEpsfvrdnalnaDTEEHeqngltetsVWICcdVWDTGIGIPENALPCLFKK 561
Cdd:cd16948   10 IGQI----VSNALKYSKQGG---KIEIYSE-----------TNEQG---------VVLS--IKDFGIGIPEEDLPRVFDK 60
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145357869 562 YMQASADHaRKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16948   61 GFTGENGR-NFQESTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
779-921 8.44e-09

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: 54.27  E-value: 8.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHT-MDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEEtgnwnaaie 857
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGA--------- 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145357869 858 agvdistseneqvcmrpTNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYL 921
Cdd:cd19923   73 -----------------LSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
471-610 9.69e-09

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


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 54.77  E-value: 9.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 471 VPIEVVGDVLRIRQILTNLISNAIKFTHEGNVgIKLQVISEP-SFVRDNALNADTEEHEQNGltetSVWICCDVWDTGIG 549
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGN-ITFRVFLEGgSEDRSDRDWGPWRPSMSDE----SVEIRFEVEINDSG 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 550 IPENALPCLFKKymQASADHARKYGGtGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFIL 610
Cdd:cd16938   76 SPSIESASMRNS--LNRRYNLSELGE-HLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
PRK10604 PRK10604
sensor protein RstB; Provisional
368-611 1.57e-08

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 58.08  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 368 KQMLATMSHEIRSPLSGV---VGMAEILSTtkldkEQRQLLNVMISSGDlvlQLINDILDLSkvesgvmRLEatkfRPRE 444
Cdd:PRK10604 213 KQLIDGIAHELRTPLVRLryrLEMSDNLSA-----AESQALNRDIGQLE---ALIEELLTYA-------RLD----RPQN 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 445 VVKHVLQTAAASLKKSLTLEGNIADDVPIEVV----GDVLR-----IRQILTNLISNAIKFTHeGNVGIKLqvisepSFV 515
Cdd:PRK10604 274 ELHLSEPDLPAWLSTHLADIQAVTPEKTVRLDtphqGDYGAldmrlMERVLDNLLNNALRYAH-SRVRVSL------LLD 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 516 RDNAlnadteeheqngltetsvwiCCDVWDTGIGIPENALPCLFKKYMQASADHARKYGGTGLGLAICKQLVELMGGQLT 595
Cdd:PRK10604 347 GNQA--------------------CLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVN 406
                        250
                 ....*....|....*.
gi 145357869 596 VTSRVSEGSTFTFILP 611
Cdd:PRK10604 407 CDESELGGARFSFSWP 422
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
780-913 1.68e-08

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: 53.26  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKiniMVAKSM---MKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwnaai 856
Cdd:cd17624    1 ILLVEDDA---LLGDGLktgLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR----------- 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 857 eAGVDIstseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKPVTLQKL 913
Cdd:cd17624   67 -QGQSL----------------PVLILTARDGVDDRVAGLDAGADDYLVKPFALEEL 106
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
779-847 2.58e-08

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 52.80  E-value: 2.58e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHT-MDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYE 847
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEvVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSEN 71
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
780-845 3.17e-08

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: 52.72  E-value: 3.17e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDI---ANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGFEVvgeAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRE 69
glnL PRK11073
nitrogen regulation protein NR(II);
367-613 3.84e-08

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 56.24  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 367 AKQMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQLLNVMISSGDLVLQLINDILDLSKveSGVMRLEATkfrpREVV 446
Cdd:PRK11073 130 ARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLLGPQR--PGTHVTESI----HKVA 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 447 KHVLQTAAASLKKSLTLEGNIADDVPiEVVGDVLRIRQILTNLISNAIKFTHEGNVGIKLQviSEPSFvrdnALNADTEE 526
Cdd:PRK11073 204 ERVVQLVSLELPDNVRLIRDYDPSLP-ELAHDPDQIEQVLLNIVRNALQALGPEGGTITLR--TRTAF----QLTLHGER 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 527 HEqnglteTSVWIccDVWDTGIGIPENALPCLFkkYMQASAdharKYGGTGLGLAICKQLVELMGGQLTVTSRvsEGST- 605
Cdd:PRK11073 277 YR------LAARI--DIEDNGPGIPPHLQDTLF--YPMVSG----REGGTGLGLSIARNLIDQHSGKIEFTSW--PGHTe 340

                 ....*...
gi 145357869 606 FTFILPYK 613
Cdd:PRK11073 341 FSVYLPIR 348
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
483-611 5.06e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 51.62  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 483 RQILTNLISNAIKFTHEgNVGIKLQvisepSFVRDNALNADteeheqngltetsvwiccdVWDTGIGIPENALPCLFKKY 562
Cdd:cd16923    2 QRVFSNLLSNAIKYSPE-NTRIYIT-----SFLTDDVVNIM-------------------FKNPSSHPLDFKLEKLFERF 56
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 145357869 563 MQAsaDHARKYGGTGLGLAICKQLVELMGGQLTVTSRvSEGSTFTFILP 611
Cdd:cd16923   57 YRG--DNSRNTEGAGLGLSIAKAIIELHGGSASAEYD-DNHDLFKVRLP 102
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
779-845 6.79e-08

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 52.01  E-value: 6.79e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHT--MDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMA 70
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
366-599 1.06e-07

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 54.97  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 366 RAKQMLATMSHEIRSPLSGVVGMAEILsttkldkEQRQLLNVM--ISSGDLVLQLINDILDLSKVESgvmRLEATKFRPR 443
Cdd:PRK10755 136 QERLFTADVAHELRTPLAGIRLHLELL-------EKQHHIDVAplIARLDQMMHTVEQLLQLARAGQ---SFSSGHYQTV 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 444 EVVKHVLQTAAASLKKSLTLEGN----IADDVPIEVVGDVLRIRQILTNLISNAIKFTHEG-NVGIKLqvisepsfvrdn 518
Cdd:PRK10755 206 KLLEDVILPSQDELSEMLEQRQQtlllPESAADITVQGDATLLRLLLRNLVENAHRYSPEGsTITIKL------------ 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 519 alnadteeHEQNGLTETSVWiccdvwDTGIGIPENALPCLFKKYMQASadhaRKYGGTGLGLAICKQLVELMGGQLTVTS 598
Cdd:PRK10755 274 --------SQEDGGAVLAVE------DEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHGQFFLQN 335

                 .
gi 145357869 599 R 599
Cdd:PRK10755 336 R 336
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
347-582 1.08e-07

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 55.32  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 347 RKAMESeLNKTIHITEETMRAKQ-MLATMSHEIRSPLSGvVGMAEILST---------TKLDKEQRQLlnvmissgDlvl 416
Cdd:PRK09470 223 RQAGAS-FNQMVTALERMMTSQQrLLSDISHELRTPLTR-LQLATALLRrrqgeskelERIETEAQRL--------D--- 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 417 QLINDILDLSK--VESGVMRleaTKFRPREVVKHVLQTA---AASLKKSLTLEgniADDVPIEVVGDVLRIRQILTNLIS 491
Cdd:PRK09470 290 SMINDLLVLSRnqQKNHLER---ETFKANSLWSEVLEDAkfeAEQMGKSLTVS---APPGPWPINGNPNALASALENIVR 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 492 NAIKFTHEgnvgiKLQVisepSFVRDNalnadteeheqNGLTetsvwICCDvwDTGIGIPENALPCLFKKYMQASADHAR 571
Cdd:PRK09470 364 NALRYSHT-----KIEV----AFSVDK-----------DGLT-----ITVD--DDGPGVPEEEREQIFRPFYRVDEARDR 416
                        250
                 ....*....|.
gi 145357869 572 KYGGTGLGLAI 582
Cdd:PRK09470 417 ESGGTGLGLAI 427
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
486-611 1.10e-07

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: 50.89  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 486 LTNLISNAIKFTHegnvgiklQVISEPSFVRDNalnadteeheqngltetsvWICCDVWDTGIGIPENALPCLFKKYMQA 565
Cdd:cd16939    5 LDNLLRNALRYAH--------RTVRIALLVSGG-------------------RLTLIVEDDGPGIPAAARERVFEPFVRL 57
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 145357869 566 SADHARKYGGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16939   58 DPSRDRATGGFGLGLAIVHRVALWHGGHVECDDSELGGACFRLTWP 103
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
478-608 1.15e-07

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: 50.92  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 478 DVLRIRQILTNLISNAIKFTHEGNVgiklqvisepsfvrdnalnadteeheqnglteTSVWICCD-------VWDTGIGI 550
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGT--------------------------------VSISIYDEeeylyfeIWDNGHGF 48
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 551 PENALPCLFKK-YMQASADHARKYggTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTF 608
Cdd:cd16975   49 SEQDLKKALELfYRDDTSRRSGGH--YGMGLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
777-843 1.33e-07

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 51.43  E-value: 1.33e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145357869 777 KPKILLVEDNkinIMVAKSMMKQLGHTMDI-----ANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLI 843
Cdd:COG2197    1 MIRVLIVDDH---PLVREGLRALLEAEPDIevvgeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
778-845 1.48e-07

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: 50.68  E-value: 1.48e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 778 PKILLVEDNKiNI-MVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:cd17554    1 KKILVVDDEE-NIrELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE 68
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
482-610 1.51e-07

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: 50.15  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 482 IRQILTNLISNAIKFTHE---GNVGIKLQVISEPSFVRdnalnadteeheqngltetsvwiccdVWDTGIGIPENALPCL 558
Cdd:cd16976    1 IQQVLMNLLQNALDAMGKvenPRIRIAARRLGGRLVLV--------------------------VRDNGPGIAEEHLSRV 54
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145357869 559 FKKYMQAsadhaRKYG-GTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFIL 610
Cdd:cd16976   55 FDPFFTT-----KPVGkGTGLGLSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
780-907 1.66e-07

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 50.07  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaaieag 859
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLR--------------- 65
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 145357869 860 vdistsENEQVCmrptnRLPIIAMTANTLAESSEECYANGMDSFISKP 907
Cdd:cd19927   66 ------KNADFD-----TIPVIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
780-913 1.94e-07

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 50.46  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKiniMVAKSMMKQL---GHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaai 856
Cdd:cd17627    1 ILVVDDDR---AVRESLRRSLrfeGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLR------------ 65
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 857 EAGvdistseneqvcmrptNRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKL 913
Cdd:cd17627   66 AAG----------------NDLPILVLTARDSVSDRVAGLDAGADDYLVKPFALEEL 106
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
484-611 2.29e-07

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: 49.88  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 484 QILTNLISNAIKFTHEGNVGIKLQVISEPSFVRdnalnadteeheqngltetsvwicCDVWDTGIGIPENALPCLFKK-Y 562
Cdd:cd16953    3 QVLRNLIGNAISFSPPDTGRITVSAMPTGKMVT------------------------ISVEDEGPGIPQEKLESIFDRfY 58
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 145357869 563 MQASADHArkYG-GTGLGLAICKQLVELMGGQLTVTSR----VSEGSTFTFILP 611
Cdd:cd16953   59 TERPANEA--FGqHSGLGLSISRQIIEAHGGISVAENHnqpgQVIGARFTVQLP 110
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
779-844 2.69e-07

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 52.51  E-value: 2.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLG--HTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIR 844
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKYPdlEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLR 70
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
780-861 2.69e-07

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: 49.97  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNK-INIMVAKSMMKQlGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEET--------- 849
Cdd:cd19934    1 LLLVEDDAlLAAQLKEQLSDA-GYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRAtpvliltar 79
                         90
                 ....*....|....*
gi 145357869 850 GNWN---AAIEAGVD 861
Cdd:cd19934   80 DSWQdkvEGLDAGAD 94
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
478-611 2.71e-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: 49.84  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 478 DVLRIRQILTNLISNAIKFTHEGNVG-IKLQVISEPSFVRDnalnadteeheqngltetsvwICCDVWDTGIGIPENALP 556
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEGRPSDvGEVRIRVEADQDGR---------------------IVLIVCDNGKGFPREMRH 59
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 557 CLFKKYMQASADharkygGTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16944   60 RATEPYVTTRPK------GTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
779-921 4.46e-07

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 49.61  E-value: 4.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDN-KINIMVAKSMmKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGL---KATRLIRSYEETgnwna 854
Cdd:cd17562    2 KILAVDDSaSIRQMVSFTL-RGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIeliKELRKLPAYKFT----- 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 855 aieagvdistseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQYL 921
Cdd:cd17562   76 ------------------------PILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
780-845 6.54e-07

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 48.84  E-value: 6.54e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK 66
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
780-914 7.20e-07

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: 48.73  E-value: 7.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaaieag 859
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQ--------------- 65
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 860 vdistsENEQVCmrptnrlPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLR 914
Cdd:cd17572   66 ------ERSLPT-------SVIVITAHGSVDIAVEAMRLGAYDFLEKPFDADRLR 107
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
780-907 7.54e-07

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 48.86  E-value: 7.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETGNwnaaieag 859
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKD-------- 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145357869 860 vdistseneqvcmrptnrLPIIAMTanTLAESSE-----ECyanGMDSFISKP 907
Cdd:cd17598   73 ------------------IPVILLT--TLSDPRDvirglEC---GADNFITKP 102
PRK10610 PRK10610
chemotaxis protein CheY;
779-919 8.46e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 48.82  E-value: 8.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLG-HTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwNAAIE 857
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRA-------DGAMS 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145357869 858 agvdistseneqvcmrptnRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQ 919
Cdd:PRK10610  80 -------------------ALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNK 122
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
779-920 1.39e-06

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: 48.01  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKiniMVA---KSMMKQLG--HTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETGNwn 853
Cdd:cd19925    2 NVLIVEDDP---MVAeihRAYVEQVPgfTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVD-- 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 854 aaieagvdistseneqvcmrptnrlpIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQQY 920
Cdd:cd19925   77 --------------------------VIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
801-846 1.86e-06

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: 47.49  E-value: 1.86e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 145357869 801 GHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSY 846
Cdd:cd17550   22 GYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK 67
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
778-850 1.91e-06

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: 47.38  E-value: 1.91e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145357869 778 PKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETG 850
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVG 73
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
781-849 5.66e-06

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: 46.11  E-value: 5.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 781 LLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEET 849
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKT 69
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
806-843 6.36e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 49.11  E-value: 6.36e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 145357869 806 IANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLI 843
Cdd:PRK12555  31 VATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRI 68
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
538-611 1.06e-05

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


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 45.45  E-value: 1.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 538 WICCDVWDTGIGIPENALPCLFKKYMQAsadhaRKYG-GTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16919   47 YVCLEVSDTGSGMPAEVLRRAFEPFFTT-----KEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
779-848 1.85e-05

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: 44.68  E-value: 1.85e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEE 848
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSD 70
PRK10336 PRK10336
two-component system response regulator QseB;
779-910 1.96e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 46.81  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKatrLIRSYEETGnwnaaiea 858
Cdd:PRK10336   2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRD---ILREWREKG-------- 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145357869 859 gvdistseneqvcmrptNRLPIIAMTANTLAESSEECYANGMDSFISKPVTL 910
Cdd:PRK10336  71 -----------------QREPVLILTARDALAERVEGLRLGADDYLCKPFAL 105
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
347-603 2.21e-05

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 48.14  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 347 RKAMESELNKTIHITEetmrAKQMLATMSHEIRSPLSGvvgMAEILSTTKLDKEQRQLLNVMiSSGDLVLQLINDILDLS 426
Cdd:COG4192  417 LRQTQDELIQAAKMAV----VGQTMTSLAHELNQPLNA---MSMYLFSAKKALEQENYAQLP-TSLDKIEGLIERMDKII 488
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 427 KVESGVMRLEATKFRP---REVVKH---VLQTAAASLKKSLTLEGniaddvPIEVVGDVLRIRQILTNLISNAikftheg 500
Cdd:COG4192  489 KSLRQFSRKSDTPLQPvdlRQVIEQaweLVESRAKPQQITLHIPD------DLMVQGDQVLLEQVLVNLLVNA------- 555
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 501 nvgiklqvisepsfvrdnaLNADTEEHE-QNGLTETSVWICCDVWDTGIGIPenALPCLFKKYMQAsadharKYGGTGLG 579
Cdd:COG4192  556 -------------------LDAVATQPQiSVDLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTT------KEVGLGLG 608
                        250       260
                 ....*....|....*....|....
gi 145357869 580 LAICKQLVELMGGQLTVTSRVSEG 603
Cdd:COG4192  609 LSICRSIMQQFGGDLYLASTLERG 632
PRK13557 PRK13557
histidine kinase; Provisional
748-832 2.23e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 48.13  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 748 GGTLEMESEL----TV------SSHREEEKAETEVKETSKP---KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAI 814
Cdd:PRK13557 373 GGAVRIYSEVgegtTVrlyfpaSDQAENPEQEPKARAIDRGgteTILIVDDRPDVAELARMILEDFGYRTLVASNGREAL 452
                         90
                 ....*....|....*....
gi 145357869 815 TAINSSS-YDLVLMDVCMP 832
Cdd:PRK13557 453 EILDSHPeVDLLFTDLIMP 471
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
780-844 2.26e-05

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: 44.34  E-value: 2.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIR 844
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR 65
orf27 CHL00148
Ycf27; Reviewed
773-845 2.42e-05

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 46.63  E-value: 2.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145357869 773 KETSKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:CHL00148   2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK 74
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
780-845 3.12e-05

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: 43.91  E-value: 3.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAIN---------SSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRD 75
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
779-849 3.55e-05

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 46.33  E-value: 3.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINsSSYDLVLMDVCMPVLDGLKATRLIRSYEET 849
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTHQT 72
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
778-913 8.96e-05

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: 43.01  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 778 PKILLVEDN-KINIMVAKSMmKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETGnwnaai 856
Cdd:cd17618    1 RTILIVEDEpAIREMIAFNL-ERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTR------ 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 857 eagvdistseneqvcmrptnRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKL 913
Cdd:cd17618   74 --------------------DIPIIMLTARGEEEDKVRGLEAGADDYITKPFSPREL 110
PRK10643 PRK10643
two-component system response regulator PmrA;
779-844 9.49e-05

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 44.64  E-value: 9.49e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIR 844
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWR 67
PRK10337 PRK10337
sensor protein QseC; Provisional
346-599 1.15e-04

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 45.80  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 346 VRKAMESeLNKTIHITEETM-RAKQMLATMSHEIRSPLSGVVGMAEILSTTKLDKEQRQ--LLNvmISSG-DLVLQLIND 421
Cdd:PRK10337 216 VRPLVEA-LNQLFARTHAMMvRERRFTSDAAHELRSPLAALKVQTEVAQLSDDDPQARKkaLLQ--LHAGiDRATRLVDQ 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 422 ILDLSKVESG--VMRLEATKFRPrevvkhVLQTAAASL-------KKSLTLEgniADDVPIEVVGDVLRIRQILTNLISN 492
Cdd:PRK10337 293 LLTLSRLDSLdnLQDVAEIPLED------LLQSAVMDIyhtaqqaGIDVRLT---LNAHPVIRTGQPLLLSLLVRNLLDN 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 493 AIKFTHEGnvGIKLQVISEPSF-VRDNalnadteeheqngltetsvwiccdvwdtGIGIPENALPCLFKKYMQASADHAR 571
Cdd:PRK10337 364 AIRYSPQG--SVVDVTLNARNFtVRDN----------------------------GPGVTPEALARIGERFYRPPGQEAT 413
                        250       260
                 ....*....|....*....|....*...
gi 145357869 572 kygGTGLGLAICKQLVELMGGQLTVTSR 599
Cdd:PRK10337 414 ---GSGLGLSIVRRIAKLHGMNVSFGNA 438
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
779-844 1.24e-04

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: 42.10  E-value: 1.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINS-SSYDLVLMDVCMPVLDGLKATRLIR 844
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQgKDIDIVVTDIVMPEMDGIELAREAR 67
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
804-843 1.29e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 45.14  E-value: 1.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 145357869 804 MDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLI 843
Cdd:PRK00742  32 VGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKI 71
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
779-922 1.58e-04

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: 42.43  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGH-TMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETGnwNAAIE 857
Cdd:cd17530    2 RVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNA--AVILM 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 858 AGVDistseneqvcmrptnrlPIIAMTANTLAEsseecyANGMDSF--ISKPVTLQKLRECLQQYLH 922
Cdd:cd17530   80 SGLD-----------------GGILESAETLAG------ANGLNLLgtLSKPFSPEELTELLTKYTA 123
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
780-844 1.67e-04

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: 41.56  E-value: 1.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINS-SSYDLVLMDVCMPvlDGLKATRLIR 844
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESgPDIDLLVTDVIMP--GGMNGSQLAE 64
PRK11517 PRK11517
DNA-binding response regulator HprR;
779-920 1.76e-04

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 44.12  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETgnwnaaiea 858
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT--------- 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869 859 gvdistseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKPVT----LQKLRECLQQY 920
Cdd:PRK11517  73 --------------------PVICLTARDSVDDRVRGLDSGANDYLVKPFSfselLARVRAQLRQH 118
PRK10766 PRK10766
two-component system response regulator TorR;
779-850 1.81e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 43.87  E-value: 1.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETG 850
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRSTVG 75
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
779-845 2.43e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 43.76  E-value: 2.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS 68
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
780-861 2.87e-04

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 41.49  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKiniMVAKSMMKQLGHTMDI-----ANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIR---------- 844
Cdd:cd19930    1 VLIAEDQE---MVRGALAALLELEDDLevvaqASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELReelpdtkvli 77
                         90
                 ....*....|....*....
gi 145357869 845 --SYEETGNWNAAIEAGVD 861
Cdd:cd19930   78 vtTFGRPGYFRRALAAGVD 96
PRK10816 PRK10816
two-component system response regulator PhoP;
779-918 3.01e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 43.19  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEEtgnwnaaiea 858
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDV---------- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 859 gvdistseneqvcmrptnRLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKLRECLQ 918
Cdd:PRK10816  72 ------------------SLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQ 113
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
779-844 3.60e-04

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: 41.35  E-value: 3.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 779 KILLVEDNKinimVAKSMMKQL--GHTMDI--ANNGVEAITAINS-SSYDLVLMDVCMPVLDGLKATRLIR 844
Cdd:cd17544    2 KVLVVDDSA----TSRNHLRALlrRHNFQVleAANGQEALEVLEQhPDIKLVITDYNMPEMDGFELVREIR 68
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
779-908 4.84e-04

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 40.82  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLkatrlirsyeetgnwnaaiea 858
Cdd:cd17622    2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGL--------------------- 60
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 859 gvdistseneQVC--MRPTNRLPIIAMTANtlaESSEECYA---NGMDSFISKPV 908
Cdd:cd17622   61 ----------TLCrdLRPKYQGPILLLTAL---DSDIDHILgleLGADDYVVKPV 102
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
779-907 6.07e-04

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: 40.53  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSyeetgnwnaaiEA 858
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-----------ES 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 145357869 859 GVdistseneqvcmrptnrlPIIAMTANTLAESSEECYANGMDSFISKP 907
Cdd:cd17626   71 GV------------------PIVMLTAKSDTVDVVLGLESGADDYVAKP 101
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
781-913 7.07e-04

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: 40.41  E-value: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 781 LLVEDNKINIMVAKSM-MKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRsyeetgnwnaaiEAG 859
Cdd:cd17615    2 VLVVDDEPNITELLSMaLRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLR------------ADG 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 145357869 860 VDistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKL 913
Cdd:cd17615   70 PD----------------VPVLFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEV 107
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
542-611 7.89e-04

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: 40.08  E-value: 7.89e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 542 DVWDTGIGIPENALPCLFKKYMQAsadharKYGGTGLGLAICKQLVELMGGQLTVTSRvsEGST-FTFILP 611
Cdd:cd16918   47 SVIDNGPGIPPDLQDTIFYPMVSG------RENGTGLGLAIAQNIVSQHGGVIECDSQ--PGHTvFSVSLP 109
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
807-848 1.00e-03

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: 39.83  E-value: 1.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 145357869 807 ANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEE 848
Cdd:cd17532   30 AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAK 71
PRK15479 PRK15479
transcriptional regulator TctD;
779-913 1.10e-03

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 41.63  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETgnwnaaiea 858
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQT--------- 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145357869 859 gvdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKPVTLQKL 913
Cdd:PRK15479  73 -------------------LPVLLLTARSAVADRVKGLNVGADDYLPKPFELEEL 108
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
779-907 1.22e-03

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: 39.46  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 779 KILLVEDNK-INIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEETGNwnaaie 857
Cdd:cd17552    3 RILVIDDEEdIREVVQACLEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQS------ 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145357869 858 agvdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKP 907
Cdd:cd17552   77 --------------------IPVILLTAKAQPSDRQRFASLGVAGVIAKP 106
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
775-844 1.26e-03

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 40.67  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 775 TSKPKILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIR 844
Cdd:COG4567    2 AEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALR 71
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
778-844 1.47e-03

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: 39.11  E-value: 1.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 778 PKILLVEDNKInimVAKSMMKQL---GHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIR 844
Cdd:cd17555    1 ATILVIDDDEV---VRESIAAYLedsGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQIT 67
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
780-837 1.65e-03

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: 39.40  E-value: 1.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 780 ILLVEDNKInimVAKSMMKQL---GHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGL 837
Cdd:cd17549    1 VLLVDDDAD---VREALQQTLelaGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGL 58
PAS COG2202
PAS domain [Signal transduction mechanisms];
209-342 1.85e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 41.16  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 209 ELTQNLKRAEGFLHFILQNAPIVMGHQDKDLRYLFIYNKYPSL---REQDILGKTDVEIFHGGGVKESEDFKREVLEKGK 285
Cdd:COG2202    1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLtgySAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145357869 286 ASKREITFTTDLFGSKTFLIYVEPVYNKAGEKIGINYMGMEVTDQvvkREKMAKLRE 342
Cdd:COG2202   81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITER---KRAEEALRE 134
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
777-837 2.17e-03

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 38.74  E-value: 2.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145357869 777 KPKILLVEDNK--INIMvakSMMKQLGHTMDI---ANNGVEAITAINSSSYDLVLMDVCMPVLDGL 837
Cdd:cd17561    1 KIKVLIADDNRefVQLL---EEYLNSQPDMEVvgvAHNGQEALELIEEKEPDVLLLDIIMPHLDGI 63
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
484-606 3.28e-03

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: 38.77  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 484 QILTNLISNAIKFTHEgnvgiklqvisepsFVRDNALNADteeheqNGLTetsvwICCDvwDTGIGIPENALPCLFKKYM 563
Cdd:cd16954   40 ELLGNLLDNACKWCLE--------------FVEVTARQTD------GGLH-----LIVD--DDGPGVPESQRSKIFQRGQ 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 145357869 564 QASADHArkygGTGLGLAICKQLVELMGGQLTVTSRVSEGSTF 606
Cdd:cd16954   93 RLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
446-611 3.33e-03

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 41.04  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 446 VKHVLQTAAASLKKSLTlegniADDVPIEVVGD--VLRIRQ------ILTNLISNAIKF----THEGNVGIKLQViseps 513
Cdd:COG3920  361 LRDYLRELLEPLRDSYG-----GRGIRIELDGPdvELPADAavplglILNELVTNALKHaflsGEGGRIRVSWRR----- 430
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 514 fvrdnalnadteehEQNGLTetsvwicCDVWDTGIGIPENALPclfkkymqasadharkYGGTGLGLAICKQLVELMGGQ 593
Cdd:COG3920  431 --------------EDGRLR-------LTVSDNGVGLPEDVDP----------------PARKGLGLRLIRALVRQLGGT 473
                        170
                 ....*....|....*...
gi 145357869 594 LTVTSrvSEGSTFTFILP 611
Cdd:COG3920  474 LELDR--PEGTRVRITFP 489
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
780-845 4.48e-03

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 37.53  E-value: 4.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145357869 780 ILLVEDNKiniMVAKSMMKQL---GHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRS 845
Cdd:cd17620    1 ILVIEDEP---QIRRFLRTALeahGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLRE 66
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
780-907 4.76e-03

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 37.38  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 780 ILLVEDNKINIMVAKSMMKQLGHTMDIANNGVEAITAIN--SSSYDLVLMDVCMPVLDGLKATRLIRSYEETGNwnaaie 857
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEdeQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKN------ 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145357869 858 agvdistseneqvcmrptnrLPIIAMTANTLAESSEECYANGMDSFISKP 907
Cdd:cd17582   75 --------------------IPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
774-919 5.25e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 39.67  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 774 ETSKPKILLVEDN-KI-NIMVakSMMKQLGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEEtgn 851
Cdd:PRK10710   7 DENTPRILIVEDEpKLgQLLI--DYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSD--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 852 wnaaieagvdistseneqvcmrptnrLPIIAMTANTlaessEEC-----YANGMDSFISKP------VTLQK--LRECLQ 918
Cdd:PRK10710  82 --------------------------IPIVMVTAKI-----EEIdrllgLEIGADDYICKPysprevVARVKtiLRRCKP 130

                 .
gi 145357869 919 Q 919
Cdd:PRK10710 131 Q 131
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
575-611 9.79e-03

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 37.95  E-value: 9.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 145357869 575 GTGLGLAICKQLVELMGGQLTVTSRVSEGSTFTFILP 611
Cdd:cd16916  142 GRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
779-848 9.81e-03

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 37.15  E-value: 9.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145357869 779 KILLVED-NKINIMVAKSMMKQlGHTMDIANNGVEAITAINSSSYDLVLMDVCMPVLDGLKATRLIRSYEE 848
Cdd:cd17553    2 KILIVDDqYGIRILLNEVFNKE-GYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDE 71
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
538-615 9.88e-03

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 39.62  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145357869 538 WICCDVWDTGIGIPENALPCLFKKYmqasadhARKYGGTGLGLAICKQLVELM---GGQLTVTSRVSEGSTFTFILPYKV 614
Cdd:COG2972  372 RLVITVEDNGVGMPEEKLEKLLEEL-------SSKGEGRGIGLRNVRERLKLYygeEYGLEIESEPGEGTTVTIRIPLEE 444

                 .
gi 145357869 615 G 615
Cdd:COG2972  445 E 445
 
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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