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Conserved domains on  [gi|494040517|ref|WP_006982642|]
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PAS domain S-box protein [Chthoniobacter flavus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
380-746 7.27e-93

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


:

Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 297.53  E-value: 7.27e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 380 EERMREQAAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSADETLGNHFREFIDIDSaQLEQRNAELLIKDE--WHGE 457
Cdd:COG3852    3 RESEELLRAILDSLPDAVIVLDA-DGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS-PLRELLERALAEGQpvTERE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 458 IIQTDRQGKKVIVNSRATLVRDERGKPKSVFLIHaDMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPL 537
Cdd:COG3852   81 VTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLR-DITERKRLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 538 LRRNLEKETFENVISTIELSATRGAEIVKQVLTFGRGLDGVRRPTSLASIIQEIIKILGQTFPKDIRIETELAPDLWRVV 617
Cdd:COG3852  160 LERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPSLPEVL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 618 GDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKNAMVDssyagMLPGATAGPNVILEVQDEGTGIPPEIVERIFDPFFttk 697
Cdd:COG3852  240 GDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQV-----TLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF--- 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 698 glgkgtglglST-----------VLGIIKSHHGHVGVSSQTGFGTTFRIHLPAMGQESED 746
Cdd:COG3852  312 ----------TTkekgtglglaiVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
PAS COG2202
PAS domain [Signal transduction mechanisms];
134-383 6.42e-36

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 136.69  E-value: 6.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 134 AQLRESEERFREVVQNIEQVFWMTNVEKTeMLFVSDAYEKIWGHTCESLYAspKQWLEAIHPEDRERVLAA-ALTRQVDG 212
Cdd:COG2202    4 EALEESERRLRALVESSPDAIIITDLDGR-ILYVNPAFERLTGYSAEELLG--KTLRDLLPPEDDDEFLELlRAALAGGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 213 SYQEEYRIVRPDGAVRWISDRAFPVRDADGNVYRVAGISEDVTERRQAQFDLQ----LFRKLVDASNDTFEVIDPEsGRF 288
Cdd:COG2202   81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALReseeRLRLLVENAPDGIFVLDLD-GRI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 289 LDVSAKGPAESGFTREEYLKMRVFDINPDIPPSVWSRYMEQMQAGEAVTGEARHYCKDGTAYPIEFNGKLVQL----EKP 364
Cdd:COG2202  160 LYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLrdggEVI 239
                        250
                 ....*....|....*....
gi 494040517 365 YVVAVIRDISTRKLSEERM 383
Cdd:COG2202  240 GVLGIVRDITERKRAEEAL 258
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
757-882 1.13e-29

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: 114.18  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 757 PRGNGECLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRKI--RP 834
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRA--GPPDLILLDINMPGMDGLELLRRIRALprLP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 494040517 835 GIPIVGSTGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:COG0784   79 DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
AtoC super family cl34427
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
3-153 2.37e-22

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


The actual alignment was detected with superfamily member COG2204:

Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 100.81  E-value: 2.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   3 SPLNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWLS-PSLDLIISDYEMPGFGGMRAL-ELKQLAeIDVPF 80
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEV--ETAASGEEALALLReEPPDLVLLDLRMPGMDGLELLrELRALD-PDLPV 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517  81 IIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVAQLRESeERFREVVQNIEQV 153
Cdd:COG2204   78 ILLTGYGDVETAVEAIKAGAFDYLTKPFdLEELLAAVERALERRRLRRENAEDSGLIGRS-PAMQEVRRLIEKV 150
 
Name Accession Description Interval E-value
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
380-746 7.27e-93

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 297.53  E-value: 7.27e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 380 EERMREQAAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSADETLGNHFREFIDIDSaQLEQRNAELLIKDE--WHGE 457
Cdd:COG3852    3 RESEELLRAILDSLPDAVIVLDA-DGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS-PLRELLERALAEGQpvTERE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 458 IIQTDRQGKKVIVNSRATLVRDERGKPKSVFLIHaDMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPL 537
Cdd:COG3852   81 VTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLR-DITERKRLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 538 LRRNLEKETFENVISTIELSATRGAEIVKQVLTFGRGLDGVRRPTSLASIIQEIIKILGQTFPKDIRIETELAPDLWRVV 617
Cdd:COG3852  160 LERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPSLPEVL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 618 GDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKNAMVDssyagMLPGATAGPNVILEVQDEGTGIPPEIVERIFDPFFttk 697
Cdd:COG3852  240 GDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQV-----TLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF--- 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 698 glgkgtglglST-----------VLGIIKSHHGHVGVSSQTGFGTTFRIHLPAMGQESED 746
Cdd:COG3852  312 ----------TTkekgtglglaiVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
PRK13557 PRK13557
histidine kinase; Provisional
404-879 1.81e-75

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 256.91  E-value: 1.81e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 404 DGLITFWNKGAENLYGWSADETLGNHFReFI---DIDSAQLEQRNAELLIKDEWHGEIIQTDRQGKKVIVNSRATLVRDE 480
Cdd:PRK13557  52 DNPIVFANRAFLEMTGYAAEEIIGNNCR-FLqgpETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYND 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 481 RGKPKSVFLIHADMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFE-----NVISTIE 555
Cdd:PRK13557 131 AGDLVYFFGSQLDVSRRRDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYLDVIQAALSHPDADrgrmaRSVENIR 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 556 LSATRGAEIVKQVLTFGRG--LDGvrRPTSLASIIQEIIKILGQTFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVN 633
Cdd:PRK13557 211 AAAERAATLTQQLLAFARKqrLEG--RVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLIN 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 634 ARDAMPTGGKLRIRGKNAMVDS----SYAGMLPGATagpnVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLGLST 709
Cdd:PRK13557 289 ARDAMPEGGRVTIRTRNVEIEDedlaMYHGLPPGRY----VSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSM 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 710 VLGIIKSHHGHVGVSSQTGFGTTFRIHLPAMGQEsEDARASQPLNGLPRGNGECLLVVDDEEHVRRLVQLSLEASGYTVL 789
Cdd:PRK13557 365 VYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQA-ENPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTL 443
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 790 VATDGTEALTTFAQNvGRIDLVITDLMMP-YMGGVALIHALRKIRPGIPIVGSTGLAEkrqlAELEQMNIQA----LLNK 864
Cdd:PRK13557 444 VASNGREALEILDSH-PEVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVLLTTGYAE----ASIERTDAGGsefdILNK 518
                        490
                 ....*....|....*
gi 494040517 865 PYGSDTLLQTVREAL 879
Cdd:PRK13557 519 PYRRAELARRVRMVL 533
PAS COG2202
PAS domain [Signal transduction mechanisms];
134-383 6.42e-36

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 136.69  E-value: 6.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 134 AQLRESEERFREVVQNIEQVFWMTNVEKTeMLFVSDAYEKIWGHTCESLYAspKQWLEAIHPEDRERVLAA-ALTRQVDG 212
Cdd:COG2202    4 EALEESERRLRALVESSPDAIIITDLDGR-ILYVNPAFERLTGYSAEELLG--KTLRDLLPPEDDDEFLELlRAALAGGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 213 SYQEEYRIVRPDGAVRWISDRAFPVRDADGNVYRVAGISEDVTERRQAQFDLQ----LFRKLVDASNDTFEVIDPEsGRF 288
Cdd:COG2202   81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALReseeRLRLLVENAPDGIFVLDLD-GRI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 289 LDVSAKGPAESGFTREEYLKMRVFDINPDIPPSVWSRYMEQMQAGEAVTGEARHYCKDGTAYPIEFNGKLVQL----EKP 364
Cdd:COG2202  160 LYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLrdggEVI 239
                        250
                 ....*....|....*....
gi 494040517 365 YVVAVIRDISTRKLSEERM 383
Cdd:COG2202  240 GVLGIVRDITERKRAEEAL 258
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
623-738 8.22e-30

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: 114.40  E-value: 8.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAMPTGGKLRIRGKNAMVDSSYAGMLPGATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKG 702
Cdd:cd16919    1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494040517 703 TGLGLSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16919   81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
757-882 1.13e-29

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: 114.18  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 757 PRGNGECLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRKI--RP 834
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRA--GPPDLILLDINMPGMDGLELLRRIRALprLP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 494040517 835 GIPIVGSTGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:COG0784   79 DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
165-250 1.06e-23

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 95.87  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  165 LFVSDAYEKIWGHTCESLYASPKQWLEAIHPEDRERV---LAAALTRqvDGSYQEEYRIVRPDGAVRWISDRAFPVRDAD 241
Cdd:pfam08447   2 IYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVreaLWEALKG--GEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                  ....*....
gi 494040517  242 GNVYRVAGI 250
Cdd:pfam08447  80 GKPVRVIGV 88
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
765-865 6.60e-23

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 93.83  E-value: 6.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGL 844
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE--RPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78
                         90       100
                 ....*....|....*....|.
gi 494040517 845 AEKRQLAELEQMNIQALLNKP 865
Cdd:cd00156   79 ADEEDAVRALELGADDYLVKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
3-153 2.37e-22

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: 100.81  E-value: 2.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   3 SPLNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWLS-PSLDLIISDYEMPGFGGMRAL-ELKQLAeIDVPF 80
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEV--ETAASGEEALALLReEPPDLVLLDLRMPGMDGLELLrELRALD-PDLPV 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517  81 IIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVAQLRESeERFREVVQNIEQV 153
Cdd:COG2204   78 ILLTGYGDVETAVEAIKAGAFDYLTKPFdLEELLAAVERALERRRLRRENAEDSGLIGRS-PAMQEVRRLIEKV 150
T2SS_HK NF038348
histidine kinase;
430-738 1.32e-21

histidine kinase;


Pssm-ID: 439642 [Multi-domain]  Cd Length: 574  Bit Score: 100.02  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 430 FREFIDIDSAQLEQRNAEL---LIKDEWHGEIIQ-TDRQGKKVIVNSRATLVRDERGKPKSVFLIHadmtEQRELEARFL 505
Cdd:NF038348 244 LRGITDALEDLVQLRTAELegaLRQYELTTETLQrTRVHMEREIEERKAAQARLEQEKDEQRRLIH----ELEETHVQLL 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 506 RAQRMESIGTLASGVAHDLNNILSPIMMSVPLLR--------------------------------RNLEKETFENVIST 553
Cdd:NF038348 320 QSEKLASIGQLAAGVAHEINNPIGFVSANLNTLKgwvhslldviaaqeaatpahaaqtraplaaagRDADLDYVRGDIMT 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 554 IELSATRGAEIVKQVLtfgRGLDGVRRPTSLASIIQEIIKILGQTFpKDIRIETELAPDLWRVVGD-------STQLHQV 626
Cdd:NF038348 400 LIDESIDGAMRVRRIV---QDLRDFSRPSGDEWSFADLHAGLESTL-NVVHNELKYKADVVREYGDlplvecnAAQLNQV 475
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 627 MLNLCVNARDAMPTGGKLRIRGknamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLG 706
Cdd:NF038348 476 FMNLLVNAAQAIPGRGTITIRT---------------TCDGDHASIAISDTGKGIPPDVMGRIFDPFFTTKPVGQGTGLG 540
                        330       340       350
                 ....*....|....*....|....*....|..
gi 494040517 707 LSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:NF038348 541 LSISHGIVEHHRGRIDVASEPGRGSTFTITLP 572
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
618-738 2.00e-21

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 90.02  E-value: 2.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   618 GDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKnamvdssyagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPFFTTK 697
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLE---------------RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 494040517   698 GLGKGTGLG---LSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:smart00387  66 KRSRKIGGTglgLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
618-738 5.43e-19

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: 83.19  E-value: 5.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  618 GDSTQLHQVMLNLCVNARDAMPTGGKLRIRgknamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTK 697
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITVT----------------LSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 494040517  698 GLGKGTGLG-LSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:pfam02518  65 KRGGGGTGLgLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
PRK13560 PRK13560
hypothetical protein; Provisional
132-427 7.02e-19

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 92.04  E-value: 7.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 132 TVAQLRESEERF-REVVQNIEQVFWMTNVE---KTEMLFVSDAYEKIWGhTCESLYASPKQWLE-AIHPEDRERVLAA-- 204
Cdd:PRK13560  58 AEAEAQDCREQCeRNLKANIPGGMFLFALDgdgTFSFPSLLDANGELAA-IAKHDLMADKGLLAmLIGGDDGDFFFANpf 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 205 ------ALTRQVDGSYQEEYRIVRPDGavRWISDRAFPVRDADGNVyRVAGISEDVTERRQAQF----DLQLFRKLVDAS 274
Cdd:PRK13560 137 rsaetiAMALQSDDWQEEEGHFRCGDG--RFIDCCLRFERHAHADD-QVDGFAEDITERKRAEErideALHFLQQLLDNI 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 275 NDTFEVIDpESGRFLDVSAKGPAESGFTREEYLKMRVFDINPDIPPSVW-SRYMEQMQAGEAVTGEARHYCKDGTAYPIE 353
Cdd:PRK13560 214 ADPAFWKD-EDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYqEADAAKFDADGSQIIEAEFQNKDGRTRPVD 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 354 FNGKLVQLEKP-----YVVAVIRDISTRKLSEERMREQAAMLNLAHDAIFVHGY---YDGLITF-WNKGAENLYGWSADE 424
Cdd:PRK13560 293 VIFNHAEFDDKenhcaGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIAAIgldADGNICFvNNNAAERMLGWSAAE 372

                 ...
gi 494040517 425 TLG 427
Cdd:PRK13560 373 VMG 375
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
8-106 7.11e-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: 82.28  E-value: 7.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWLS-PSLDLIISDYEMPGFGGMRALE-LKQLaEIDVPFIIISG 85
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEV--DTAADGEEALELLReERPDLVLLDLMMPGMDGLELLRkLREL-PPDIPVIVLTA 77
                         90       100
                 ....*....|....*....|.
gi 494040517  86 SIGEEMAVEAMRRGATDYLLK 106
Cdd:cd00156   78 KADEEDAVRALELGADDYLVK 98
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
765-876 1.09e-17

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: 79.50  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGL 844
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE--RPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAH 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 494040517  845 AEKRQLAELEQMNIQALLNKPYGSDTLLQTVR 876
Cdd:pfam00072  80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK15115 PRK15115
response regulator GlrR; Provisional
764-882 2.98e-14

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 76.03  E-value: 2.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:PRK15115   8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNRE--KVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTA 85
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:PRK15115  86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQS 124
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
139-261 3.88e-14

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 69.63  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  139 SEERFREVVQNIEQVFWMTNvEKTEMLFVSDAYEKIWGHTCESLYAspKQWLEAIHPEDRERVLA---AALTRQVDGsYQ 215
Cdd:TIGR00229   1 SEERYRAIFESSPDAIIVID-LEGNILYVNPAFEEIFGYSAEELIG--RNVLELIPEEDREEVRErieRRLEGEPEP-VS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 494040517  216 EEYRIVRPDGAVRWISDRAFPVRdADGNVYRVAGISEDVTERRQAQ 261
Cdd:TIGR00229  77 EERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAE 121
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
764-818 5.06e-13

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: 64.13  E-value: 5.06e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 494040517   764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMP 818
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE--KPDLILLDIMMP 55
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
8-116 5.20e-13

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: 66.02  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517    8 LIAEDNPDDADLLIWALRGAGFEFEyhVVSKEEDFLRWLSP-SLDLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGS 86
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVA--EADDGKEALELLKEeRPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAH 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 494040517   87 IGEEMAVEAMRRGATDYLLKGC-LSRLESAV 116
Cdd:pfam00072  80 GDEDDAVEALEAGADDFLSKPFdPDELLAAI 110
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
379-504 4.78e-11

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 60.77  E-value: 4.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  379 SEERMReqaAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEQRNAELLIKDEWHGEI 458
Cdd:TIGR00229   1 SEERYR---AIFESSPDAIIVIDL-EGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 494040517  459 IQT---DRQGKKVIVNSRATLVRDErGKPKSVFLIHADMTEQRELEARF 504
Cdd:TIGR00229  77 EERrvrRKDGSEIWVEVSVSPIRTN-GGELGVVGIVRDITERKEAEEAL 124
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
154-254 1.70e-09

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 55.72  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 154 FWMTNvEKTEMLFVSDAYEKIWGHTCESLYAspKQWLEAIHPEDRERVLAAALTRQVDGS-YQEEYRIVRPDGAVRWISD 232
Cdd:cd00130    5 VIVLD-LDGRILYANPAAEQLLGYSPEELIG--KSLLDLIHPEDREELRERLENLLSGGEpVTLEVRLRRKDGSVIWVLV 81
                         90       100
                 ....*....|....*....|..
gi 494040517 233 RAFPVRDADGNVYRVAGISEDV 254
Cdd:cd00130   82 SLTPIRDEGGEVIGLLGVVRDI 103
fixJ PRK09390
response regulator FixJ; Provisional
9-146 4.75e-07

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 51.16  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   9 IAEDNPDDADLLIWALRGAGFEFEYHvvSKEEDFLRWLsPSLDL--IISDYEMPGFGGMRAL-ELKQLAeIDVPFIIISG 85
Cdd:PRK09390   8 VVDDDEAMRDSLAFLLDSAGFEVRLF--ESAQAFLDAL-PGLRFgcVVTDVRMPGIDGIELLrRLKARG-SPLPVIVMTG 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517  86 SIGEEMAVEAMRRGATDYLLKG-----CLSRLESAVTQAISQRRLRHEQLKTVAQLRESEERFREV 146
Cdd:PRK09390  84 HGDVPLAVEAMKLGAVDFIEKPfederLIGAIERALAQAPEAAKSEAVAADIRARIASLSERERQV 149
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
217-257 7.07e-07

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 46.41  E-value: 7.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 494040517   217 EYRIVRPDGAVRWISDRAFPVRDADGNVYRVAGISEDVTER 257
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
5-60 3.80e-03

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: 36.39  E-value: 3.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517     5 LNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWL-SPSLDLIISDYEMP 60
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEV--DEATDGEEALELLkEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
380-746 7.27e-93

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 297.53  E-value: 7.27e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 380 EERMREQAAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSADETLGNHFREFIDIDSaQLEQRNAELLIKDE--WHGE 457
Cdd:COG3852    3 RESEELLRAILDSLPDAVIVLDA-DGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS-PLRELLERALAEGQpvTERE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 458 IIQTDRQGKKVIVNSRATLVRDERGKPKSVFLIHaDMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPL 537
Cdd:COG3852   81 VTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLR-DITERKRLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 538 LRRNLEKETFENVISTIELSATRGAEIVKQVLTFGRGLDGVRRPTSLASIIQEIIKILGQTFPKDIRIETELAPDLWRVV 617
Cdd:COG3852  160 LERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPSLPEVL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 618 GDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKNAMVDssyagMLPGATAGPNVILEVQDEGTGIPPEIVERIFDPFFttk 697
Cdd:COG3852  240 GDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQV-----TLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF--- 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 698 glgkgtglglST-----------VLGIIKSHHGHVGVSSQTGFGTTFRIHLPAMGQESED 746
Cdd:COG3852  312 ----------TTkekgtglglaiVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
PRK13557 PRK13557
histidine kinase; Provisional
404-879 1.81e-75

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 256.91  E-value: 1.81e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 404 DGLITFWNKGAENLYGWSADETLGNHFReFI---DIDSAQLEQRNAELLIKDEWHGEIIQTDRQGKKVIVNSRATLVRDE 480
Cdd:PRK13557  52 DNPIVFANRAFLEMTGYAAEEIIGNNCR-FLqgpETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYND 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 481 RGKPKSVFLIHADMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFE-----NVISTIE 555
Cdd:PRK13557 131 AGDLVYFFGSQLDVSRRRDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYLDVIQAALSHPDADrgrmaRSVENIR 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 556 LSATRGAEIVKQVLTFGRG--LDGvrRPTSLASIIQEIIKILGQTFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVN 633
Cdd:PRK13557 211 AAAERAATLTQQLLAFARKqrLEG--RVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLIN 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 634 ARDAMPTGGKLRIRGKNAMVDS----SYAGMLPGATagpnVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLGLST 709
Cdd:PRK13557 289 ARDAMPEGGRVTIRTRNVEIEDedlaMYHGLPPGRY----VSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSM 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 710 VLGIIKSHHGHVGVSSQTGFGTTFRIHLPAMGQEsEDARASQPLNGLPRGNGECLLVVDDEEHVRRLVQLSLEASGYTVL 789
Cdd:PRK13557 365 VYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQA-ENPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTL 443
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 790 VATDGTEALTTFAQNvGRIDLVITDLMMP-YMGGVALIHALRKIRPGIPIVGSTGLAEkrqlAELEQMNIQA----LLNK 864
Cdd:PRK13557 444 VASNGREALEILDSH-PEVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVLLTTGYAE----ASIERTDAGGsefdILNK 518
                        490
                 ....*....|....*
gi 494040517 865 PYGSDTLLQTVREAL 879
Cdd:PRK13557 519 PYRRAELARRVRMVL 533
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
490-739 2.28e-65

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 223.52  E-value: 2.28e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 490 IHADMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLE----KETFENVISTIELSATRGAEIV 565
Cdd:COG4191  119 LERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILGNAELLRRRLEdepdPEELREALERILEGAERAAEIV 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 566 KQVLTFGRGLDGVRRPTSLASIIQEIIKILGQTFPK-DIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTG--G 642
Cdd:COG4191  199 RSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKArGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEGegG 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 643 KLRIRGKnamvdssyagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPFFttkglgkgtglglST------------- 709
Cdd:COG4191  279 RITISTR---------------REGDYVVISVRDNGPGIPPEVLERIFEPFF-------------TTkpvgkgtglglsi 330
                        250       260       270
                 ....*....|....*....|....*....|
gi 494040517 710 VLGIIKSHHGHVGVSSQTGFGTTFRIHLPA 739
Cdd:COG4191  331 SYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
376-743 1.76e-59

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: 209.05  E-value: 1.76e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 376 RKLSEERMREQAAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSADETLGnhfREFIDIDSAQLEQRNAELLIKDEWH 455
Cdd:COG5000   82 REELEERRRYLETILENLPAGVIVLDA-DGRITLANPAAERLLGIPLEELIG---KPLEELLPELDLAELLREALERGWQ 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 456 GEIIQTDRQGKKVIVnsRATLVRDErgkpkSVFLIHADMTEQrelearfLRAQRMESIGTLASGVAHDLNNILSPIMMSV 535
Cdd:COG5000  158 EEIELTRDGRRTLLV--RASPLRDD-----GYVIVFDDITEL-------LRAERLAAWGELARRIAHEIKNPLTPIQLSA 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 536 PLLRRNLEK------ETFENVISTIELSATRGAEIVKQVLTFGRGLDGVRRPTSLASIIQEIIKILGQTFP-KDIRIETE 608
Cdd:COG5000  224 ERLRRKLADkleedrEDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVDLNELLREVLALYEPALKeKDIRLELD 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 609 LAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRgknAMVDSSYagmlpgatagpnVILEVQDEGTGIPPEIVER 688
Cdd:COG5000  304 LDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVS---TRREDGR------------VRIEVSDNGPGIPEEVLER 368
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 689 IFDPFFttkglgkgtglglST-----------VLGIIKSHHGHVGVSSQTGFGTTFRIHLPAMGQE 743
Cdd:COG5000  369 IFEPFF-------------TTkpkgtglglaiVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEA 421
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
264-747 4.64e-57

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: 204.44  E-value: 4.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 264 LQLFRKLVDASNDTFEVIDPEsGRFLDVSAKGPAESGFTREEYLKMRVFDINPDIPPSVWSRYMEQMQAGEAVTG-EARH 342
Cdd:COG5809   14 EQRFRSLFENAPDAILILDLE-GKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDElEFEL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 343 YCKDGTAypIEFNGKLV-----QLEKPYVVAVIRDISTRKLSEERMREQAA----MLNLAHDAIFVHGYyDGLITFWNKG 413
Cdd:COG5809   93 RHKNGKR--LEFSSKLSpifdqNGDIEGMLAISRDITERKRMEEALRESEEkfrlIFNHSPDGIIVTDL-DGRIIYANPA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 414 AENLYGWSADETLGNHFREFIDIDSAQLEQRNAELLIKD--EWHGEIIQTDRQGKKVIVNSRATLVrDERGKPKSVFLIH 491
Cdd:COG5809  170 ACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDggIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 492 ADMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNL---EKETFENVISTIElsatRGAEIVKQV 568
Cdd:COG5809  249 RDITERKKLEELLRKSEKLSVVGELAAGIAHEIRNPLTSLKGFIQLLKDTIdeeQKTYLDIMLSELD----RIESIISEF 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 569 LTFGRGLDGVRRPTSLASIIQEIIKILG-QTFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIR 647
Cdd:COG5809  325 LVLAKPQAIKYEPKDLNTLIEEVIPLLQpQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIE 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 648 GKnamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKGLgkgtglglSTVLG------IIKSHHGHV 721
Cdd:COG5809  405 TK--------------AEDDDKVVISVTDEGCGIPEERLKKLGEPFYTTKEK--------GTGLGlmvsykIIEEHGGKI 462
                        490       500
                 ....*....|....*....|....*.
gi 494040517 722 GVSSQTGFGTTFRIHLPAMGQESEDA 747
Cdd:COG5809  463 TVESEVGKGTTFSITLPIKLSEQVSM 488
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
270-738 4.75e-52

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: 190.33  E-value: 4.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 270 LVDASNDTFEVIDPEsGRFLDVSAKGPAESGFTREEYLKMRVFD-INPDIPPSVWSRYmEQMQAGEAVTGEARHYCKDG- 347
Cdd:COG5805   39 ILENLPDAIIAVNRE-GKVIYINPAMEKLLGYTSEEIIGKTIFDfLEKEYHYRVKTRI-ERLQKGYDVVMIEQIYCKDGe 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 348 ------TAYPIEFNGKLVQLEkpyvvaVIRDISTRKLSEERMREQAAMLNL----AHDAIFVHGYyDGLITFWNKGAENL 417
Cdd:COG5805  117 liyvevKLFPIYNQNGQAAIL------ALRDITKKKKIEEILQEQEERLQTlienSPDLICVIDT-DGRILFINESIERL 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 418 YGWSADETLGNHFREFI----DIDSAQLEQRNAELLIKDEWHGEIIqtDRQGKKVIVNSRATLVRDERGKPKSVFLIHAD 493
Cdd:COG5805  190 FGAPREELIGKNLLELLhpcdKEEFKERIESITEVWQEFIIEREII--TKDGRIRYFEAVIVPLIDTDGSVKGILVILRD 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 494 MTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLE--KETFENVISTIElsatRGAEIVKQVLTF 571
Cdd:COG5805  268 ITEKKEAEELMARSEKLSIAGQLAAGIAHEIRNPLTSIKGFLQLLQPGIEdkEEYFDIMLSELD----RIESIISEFLAL 343
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 572 GRGLDGVRRPTSLASIIQEIIKILG-QTFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKn 650
Cdd:COG5805  344 AKPQAVNKEKENINELIQDVVTLLEtEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTE- 422
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 651 amvdssyagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPFFttkglgkgTGLGLSTVLG------IIKSHHGHVGVS 724
Cdd:COG5805  423 --------------EEDNSVIIRVIDEGIGIPEERLKKLGEPFF--------TTKEKGTGLGlmvsykIIENHNGTIDID 480
                        490
                 ....*....|....
gi 494040517 725 SQTGFGTTFRIHLP 738
Cdd:COG5805  481 SKVGKGTTFTITLP 494
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
495-883 1.51e-51

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 194.90  E-value: 1.51e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 495 TEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIM----MSVPLLRRN-LEKETFENVIStielSATRGAEIVKQVL 569
Cdd:PRK13837 432 TERDALERRLEHARRLEAVGTLASGIAHNFNNILGAILgyaeMALNKLARHsRAARYIDEIIS----AGARARLIIDQIL 507
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 570 TFGRGLDGVRRPTSLASIIQEIIKILGQTFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRI--- 646
Cdd:PRK13837 508 AFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGRVDIsls 587
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 647 RGKNAMVDSSYAGMLPgatAGPNVILEVQDEGTGIPPEIVERIFDPFFttKGLGKGTGLGLSTVLGIIKSHHGHVGVSSQ 726
Cdd:PRK13837 588 RAKLRAPKVLSHGVLP---PGRYVLLRVSDTGAGIDEAVLPHIFEPFF--TTRAGGTGLGLATVHGIVSAHAGYIDVQST 662
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 727 TGFGTTFRIHLPAMGQESEDARASQPLNGLPRGNGECLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVG 806
Cdd:PRK13837 663 VGRGTRFDVYLPPSSKVPVAPQAFFGPGPLPRGRGETVLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKGPE 742
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 807 RIDLVITDLmmPYMGGVALIHALRKIRPGIPIVgsTGLAEKRQLAELEQMNIQA-LLNKPYGSDTLLQTVREALATRG 883
Cdd:PRK13837 743 RFDLVLVDD--RLLDEEQAAAALHAAAPTLPII--LGGNSKTMALSPDLLASVAeILAKPISSRTLAYALRTALATAR 816
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
404-745 8.74e-46

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 174.39  E-value: 8.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 404 DGLITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEqrnaelLIKDEW-HGEII-------QTDRQGKKVIVNSraT 475
Cdd:PRK11360 281 QGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFAS------PLLDTLeHGTEHvdleisfPGRDRTIELSVST--S 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 476 LVRDERGKPKSVFLIHADMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFENVISTIE 555
Cdd:PRK11360 353 LLHNTHGEMIGALVIFSDLTERKRLQRRVARQERLAALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVL 432
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 556 LSATRGAEIVKQVLTFGRGLDGVRRPTSLASIIQEIIKILGQTFPKD-IRIETELAPDLWRVVGDSTQLHQVMLNLCVNA 634
Cdd:PRK11360 433 REVDRLNKVIDQLLEFSRPRESQWQPVSLNALVEEVLQLFQTAGVQArVDFETELDNELPPIWADPELLKQVLLNILINA 512
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 635 RDAMPTGGKLRIRGKNAMVDssyagmlpgatagpNVILEVQDEGTGIPPEIVERIFDPFFttkglgkgTGLGLSTVLG-- 712
Cdd:PRK11360 513 VQAISARGKIRIRTWQYSDG--------------QVAVSIEDNGCGIDPELLKKIFDPFF--------TTKAKGTGLGla 570
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 494040517 713 ----IIKSHHGHVGVSSQTGFGTTFRIHLPAMGQESE 745
Cdd:PRK11360 571 lsqrIINAHGGDIEVESEPGVGTTFTLYLPINPQGNQ 607
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
376-738 1.17e-44

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


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 165.34  E-value: 1.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 376 RKLSEERMREQAAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSADETLGNHFREFIDIDS-AQLEQRNAELLIKDEW 454
Cdd:COG5807   19 FKLTEDSEFKFKQLFDSILEFVFFIDS-KGEILECNDFAEDLYGLSQNEYIGKTFVEEKCILKdEQLYNKEAFDRIEISY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 455 HGEIIQTDRQGKKVIVNSratlvrderGKPKSVFLIHADMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMS 534
Cdd:COG5807   98 LTKNGEFDEIIYPIYYKD---------GVILGLITVYRDITKRKEAEDKLLRSEKLSVAGELAAGIAHEIRNPLTSIKGF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 535 VPLLRRNLEKETFENVISTIELSATRGAEIVKQVLTFGRGLDGVRRPTSLASIIQEIIKILGQTFP-KDIRIETELAPDL 613
Cdd:COG5807  169 LQLLQESREDSEREEYFNIIISEIDRINTIITELLVLSKPKKFNFKKLNLNDVLEDVIALLSTEAIlKNISIKYDLADDE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 614 WRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKnamvdssyagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPF 693
Cdd:COG5807  249 PVINGDKNQLKQVFINLIKNAIEAMETGGNITIKTY---------------VEGDFVVISVKDEGIGIPEEVLEKIGEPF 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494040517 694 FttkglgkgTGLGLSTVLG------IIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:COG5807  314 F--------TTKEEGTGLGlsickkIIEEHNGTIEVESKPGKGTTFTIYLP 356
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
416-739 6.26e-42

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 156.61  E-value: 6.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 416 NLYGWSADETLGNHFREFIDIDSAQLEQRNAELLIKDEWHGEIIQTDRQGKKVIVNSRATLVRDERGKPKSVFLIHADMT 495
Cdd:COG0642   13 LLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 496 EQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFEnVISTIELSATRGAEIVKQVLTFGR-- 573
Cdd:COG0642   93 LLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQRE-YLETILRSADRLLRLINDLLDLSRle 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 574 --GLDGVRRPTSLASIIQEIIKILGQTFP-KDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKn 650
Cdd:COG0642  172 agKLELEPEPVDLAELLEEVVELFRPLAEeKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSVR- 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 651 amvdssyagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPFFttkgLGKGTGLGLSTVLG------IIKSHHGHVGVS 724
Cdd:COG0642  251 --------------REGDRVRISVEDTGPGIPPEDLERIFEPFF----RTDPSRRGGGTGLGlaivkrIVELHGGTIEVE 312
                        330
                 ....*....|....*
gi 494040517 725 SQTGFGTTFRIHLPA 739
Cdd:COG0642  313 SEPGKGTTFTVTLPL 327
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
499-739 8.01e-38

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 141.58  E-value: 8.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 499 ELEARFLRAQRMESI-GTLASGVAHDLNNILSPIMMSVPLLRRN--LEKETFENVISTIELSATRGAEIVKQVLTFGR-- 573
Cdd:COG2205    1 ELEEALEELEELERLkSEFLANVSHELRTPLTSILGAAELLLDEedLSPEERRELLEIIRESAERLLRLIEDLLDLSRle 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 574 --GLDGVRRPTSLASIIQEIIKILGQTFP-KDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKN 650
Cdd:COG2205   81 sgKLSLELEPVDLAELLEEAVEELRPLAEeKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 651 AmvdssyagmlpgataGPNVILEVQDEGTGIPPEIVERIFDPFFttkgLGKGTGLGLSTVLG------IIKSHHGHVGVS 724
Cdd:COG2205  161 E---------------GDGVRISVSDNGPGIPEEELERIFERFY----RGDNSRGEGGTGLGlaivkrIVEAHGGTIWVE 221
                        250
                 ....*....|....*
gi 494040517 725 SQTGFGTTFRIHLPA 739
Cdd:COG2205  222 SEPGGGTTFTVTLPL 236
PAS COG2202
PAS domain [Signal transduction mechanisms];
134-383 6.42e-36

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 136.69  E-value: 6.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 134 AQLRESEERFREVVQNIEQVFWMTNVEKTeMLFVSDAYEKIWGHTCESLYAspKQWLEAIHPEDRERVLAA-ALTRQVDG 212
Cdd:COG2202    4 EALEESERRLRALVESSPDAIIITDLDGR-ILYVNPAFERLTGYSAEELLG--KTLRDLLPPEDDDEFLELlRAALAGGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 213 SYQEEYRIVRPDGAVRWISDRAFPVRDADGNVYRVAGISEDVTERRQAQFDLQ----LFRKLVDASNDTFEVIDPEsGRF 288
Cdd:COG2202   81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALReseeRLRLLVENAPDGIFVLDLD-GRI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 289 LDVSAKGPAESGFTREEYLKMRVFDINPDIPPSVWSRYMEQMQAGEAVTGEARHYCKDGTAYPIEFNGKLVQL----EKP 364
Cdd:COG2202  160 LYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLrdggEVI 239
                        250
                 ....*....|....*....
gi 494040517 365 YVVAVIRDISTRKLSEERM 383
Cdd:COG2202  240 GVLGIVRDITERKRAEEAL 258
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
365-739 7.83e-34

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 134.68  E-value: 7.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 365 YVVAVIRDISTRKLSEERMREQAAMLNLAHDAIFVHGYYDGLITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEQR 444
Cdd:COG5002   32 LLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 445 NAELLIKDEWHGEIIQTDRQGKKVIVnsratlVRDERGKPKSVFLIHADMTEQRELEarflRAQRMesigtLASGVAHDL 524
Cdd:COG5002  112 ILLAALLLLLSELLLLLLLLGRLSLR------LSALLLGLLLLAAVERDITELERLE----QMRRE-----FVANVSHEL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 525 NNILSPIMMSVPLLRRN--LEKETFENVISTIELSATRGAEIVKQVLTFGR----GLDGVRRPTSLASIIQEIIKILGQT 598
Cdd:COG5002  177 RTPLTSIRGYLELLLDGaaDDPEERREYLEIILEEAERLSRLVNDLLDLSRlesgELKLEKEPVDLAELLEEVVEELRPL 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 599 FP-KDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKNAmvdssyagmlpgataGPNVILEVQDE 677
Cdd:COG5002  257 AEeKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREE---------------DDQVRISVRDT 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 678 GTGIPPEIVERIFDPFFTTKGLGKGTGLglSTVLG------IIKSHHGHVGVSSQTGFGTTFRIHLPA 739
Cdd:COG5002  322 GIGIPEEDLPRIFERFYRVDKSRSRETG--GTGLGlaivkhIVEAHGGRIWVESEPGKGTTFTITLPL 387
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
488-739 9.58e-32

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: 129.48  E-value: 9.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 488 FLIHADMTEQRELEARFLR--AQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFENVISTIELSATRGAEIV 565
Cdd:COG5808  214 LLQYNLLKRKTLLERVIQEinTQKLELIGTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFDIIQEEIQRINQIV 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 566 KQVLTFGRGLDGVRRPTSLASIIQEIIKIL-GQTFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKL 644
Cdd:COG5808  294 SEFLVLGKPTAKKLELDDLNELIEEILSIIdSEANLKNIRVEKQSLDEPLHIKCDKDRIKQVLLNLIKNAIEAMKEGGKL 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 645 RIRGKNamvDSSYAgmlpgatagpnvILEVQDEGTGIPPEIVERIFDPFFttkglgkgTGLGLSTVLG------IIKSHH 718
Cdd:COG5808  374 TISIEN---DDEKA------------VIEVIDNGEGIPEDIIDEIFEPFV--------TTKEGGTGLGlsvckrIVEMHG 430
                        250       260
                 ....*....|....*....|.
gi 494040517 719 GHVGVSSQTGFGTTFRIHLPA 739
Cdd:COG5808  431 GEIDIESEEGKGTTFTIRLPL 451
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
623-738 8.22e-30

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: 114.40  E-value: 8.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAMPTGGKLRIRGKNAMVDSSYAGMLPGATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKG 702
Cdd:cd16919    1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494040517 703 TGLGLSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16919   81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
757-882 1.13e-29

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: 114.18  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 757 PRGNGECLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRKI--RP 834
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRA--GPPDLILLDINMPGMDGLELLRRIRALprLP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 494040517 835 GIPIVGSTGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:COG0784   79 DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
PAS COG2202
PAS domain [Signal transduction mechanisms];
255-503 4.35e-29

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 117.05  E-value: 4.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 255 TERRQAQFDLQLFRKLVDASNDTFEVIDPEsGRFLDVSAKGPAESGFTREEYLKMRVFDIN-PDIPPSVWSRYMEQMQAG 333
Cdd:COG2202    1 TAEEALEESERRLRALVESSPDAIIITDLD-GRILYVNPAFERLTGYSAEELLGKTLRDLLpPEDDDEFLELLRAALAGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 334 EAVTGEARHYCKDGTAYPIEFNGKLVQLEK---PYVVAVIRDISTRKLSEERMREQAAML----NLAHDAIFVHGYyDGL 406
Cdd:COG2202   80 GVWRGELRNRRKDGSLFWVELSISPVRDEDgeiTGFVGIARDITERKRAEEALRESEERLrllvENAPDGIFVLDL-DGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 407 ITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEQRNAELLIKDE---WHGEIIQTDRQGKKVIVNSRATLVRDErGK 483
Cdd:COG2202  159 ILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGresYELELRLKDGDGRWVWVEASAVPLRDG-GE 237
                        250       260
                 ....*....|....*....|
gi 494040517 484 PKSVFLIHADMTEQRELEAR 503
Cdd:COG2202  238 VIGVLGIVRDITERKRAEEA 257
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
622-738 2.70e-24

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: 98.26  E-value: 2.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 622 QLHQVMLNLCVNARDAMPTGGKLRIRgKNAMVDSsyagmlpgatagpnVILEVQDEGTGIPPEIVERIFDPFFTTKGLGK 701
Cdd:cd16943    3 QLNQVLLNLLVNAAQAMEGRGRITIR-TWAHVDQ--------------VLIEVEDTGSGIDPEILGRIFDPFFTTKPVGE 67
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494040517 702 GTGLGLSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16943   68 GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
764-882 8.47e-24

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: 105.05  E-value: 8.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:COG2204    5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE--PPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTG 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:COG2204   83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERR 121
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
497-748 9.24e-24

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 105.64  E-value: 9.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 497 QRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFENVISTIELS-ATRGAEIVKQVLTFGRGL 575
Cdd:PRK10364 221 RQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKeADRLNRVVSELLELVKPT 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 576 DGVRRPTSLASIIQEIIKILGQ-TFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKNAmvd 654
Cdd:PRK10364 301 HLALQAVDLNDLINHSLQLVSQdANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASES--- 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 655 ssyagmlpgataGPNVILEVQDEGTGIPPEIVERIFDPFFttKGLGKGTGLGLSTVLGIIKSHHGHVGVSSQTGFGTTFR 734
Cdd:PRK10364 378 ------------GAGVKISVTDSGKGIAADQLEAIFTPYF--TTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFT 443
                        250
                 ....*....|....
gi 494040517 735 IHLPAMGQESEDAR 748
Cdd:PRK10364 444 LWLPVNITRRDPQG 457
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
165-250 1.06e-23

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 95.87  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  165 LFVSDAYEKIWGHTCESLYASPKQWLEAIHPEDRERV---LAAALTRqvDGSYQEEYRIVRPDGAVRWISDRAFPVRDAD 241
Cdd:pfam08447   2 IYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVreaLWEALKG--GEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                  ....*....
gi 494040517  242 GNVYRVAGI 250
Cdd:pfam08447  80 GKPVRVIGV 88
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
765-865 6.60e-23

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 93.83  E-value: 6.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGL 844
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE--RPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78
                         90       100
                 ....*....|....*....|.
gi 494040517 845 AEKRQLAELEQMNIQALLNKP 865
Cdd:cd00156   79 ADEEDAVRALELGADDYLVKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
3-153 2.37e-22

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: 100.81  E-value: 2.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   3 SPLNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWLS-PSLDLIISDYEMPGFGGMRAL-ELKQLAeIDVPF 80
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEV--ETAASGEEALALLReEPPDLVLLDLRMPGMDGLELLrELRALD-PDLPV 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517  81 IIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVAQLRESeERFREVVQNIEQV 153
Cdd:COG2204   78 ILLTGYGDVETAVEAIKAGAFDYLTKPFdLEELLAAVERALERRRLRRENAEDSGLIGRS-PAMQEVRRLIEKV 150
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
764-893 4.54e-22

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: 95.02  E-value: 4.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEE--RPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTA 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPYGSDTLLQTVReALATRGGNGHVAANDL 893
Cdd:COG0745   82 RDDEEDRVRGLEAGADDYLTKPFDPEELLARIR-ALLRRRAAEVLRVGDL 130
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
765-875 7.13e-22

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: 93.82  E-value: 7.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIR--PGIPIVGST 842
Cdd:COG3706    5 LVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH--RPDLILLDLEMPDMDGLELCRRLRADPrtADIPIIFLT 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494040517 843 GLAEKRQLAELEQMNIQALLNKPYGSDTLLQTV 875
Cdd:COG3706   83 ALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
T2SS_HK NF038348
histidine kinase;
430-738 1.32e-21

histidine kinase;


Pssm-ID: 439642 [Multi-domain]  Cd Length: 574  Bit Score: 100.02  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 430 FREFIDIDSAQLEQRNAEL---LIKDEWHGEIIQ-TDRQGKKVIVNSRATLVRDERGKPKSVFLIHadmtEQRELEARFL 505
Cdd:NF038348 244 LRGITDALEDLVQLRTAELegaLRQYELTTETLQrTRVHMEREIEERKAAQARLEQEKDEQRRLIH----ELEETHVQLL 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 506 RAQRMESIGTLASGVAHDLNNILSPIMMSVPLLR--------------------------------RNLEKETFENVIST 553
Cdd:NF038348 320 QSEKLASIGQLAAGVAHEINNPIGFVSANLNTLKgwvhslldviaaqeaatpahaaqtraplaaagRDADLDYVRGDIMT 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 554 IELSATRGAEIVKQVLtfgRGLDGVRRPTSLASIIQEIIKILGQTFpKDIRIETELAPDLWRVVGD-------STQLHQV 626
Cdd:NF038348 400 LIDESIDGAMRVRRIV---QDLRDFSRPSGDEWSFADLHAGLESTL-NVVHNELKYKADVVREYGDlplvecnAAQLNQV 475
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 627 MLNLCVNARDAMPTGGKLRIRGknamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLG 706
Cdd:NF038348 476 FMNLLVNAAQAIPGRGTITIRT---------------TCDGDHASIAISDTGKGIPPDVMGRIFDPFFTTKPVGQGTGLG 540
                        330       340       350
                 ....*....|....*....|....*....|..
gi 494040517 707 LSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:NF038348 541 LSISHGIVEHHRGRIDVASEPGRGSTFTITLP 572
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
765-839 1.74e-21

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: 89.77  E-value: 1.74e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREE--QPDLIILDVMLPGMDGFEVCRRLREKGSDIPII 73
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
618-738 2.00e-21

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 90.02  E-value: 2.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   618 GDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKnamvdssyagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPFFTTK 697
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLE---------------RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 494040517   698 GLGKGTGLG---LSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:smart00387  66 KRSRKIGGTglgLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
358-739 1.03e-19

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 93.70  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 358 LVQLEKPYVVAVIRDISTRKLSEERMREQAAMLNLAHDAIFVHGYYDGLITFWNKGAENLYGWSADETLGNHFREFIDID 437
Cdd:COG4251  117 ELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLL 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 438 SAQLEQRNAELLIKDEWHGEIIQTDRQGKKVIVNSRATLVRDERGKPKSVFLIHADMTEQRELEARFLRAQRMESIGTL- 516
Cdd:COG4251  197 LLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELe 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 517 ---------ASGVAHDLNNILSPIMMSVPLLRRNLEKETFENV---ISTIELSATRGAEIVKQVLTFGR--GLDGVRRPT 582
Cdd:COG4251  277 rsneeleqfAYVASHDLREPLRKISGFSQLLEEDYGDKLDEEGreyLERIRDAAERMQALIDDLLAYSRvgRQELEFEPV 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 583 SLASIIQEIIKILGQTFP-KDIRIETELAPdlwRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRgknamVDSSyagml 661
Cdd:COG4251  357 DLNELLEEVLEDLEPRIEeRGAEIEVGPLP---TVRGDPTLLRQVFQNLISNAIKYSRPGEPPRIE-----IGAE----- 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 662 pgaTAGPNVILEVQDEGTGIPPEIVERIFDPFfttkGLGKGTGLGLSTVLG------IIKSHHGHVGVSSQTGFGTTFRI 735
Cdd:COG4251  424 ---REGGEWVFSVRDNGIGIDPEYAEKIFEIF----QRLHSRDEYEGTGIGlaivkkIVERHGGRIWVESEPGEGATFYF 496

                 ....
gi 494040517 736 HLPA 739
Cdd:COG4251  497 TLPK 500
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
764-865 1.55e-19

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: 84.44  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLE-ASGY-TVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGS 841
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEwEAGFeVVGEAENGEEALELLEEH--KPDLVITDINMPGMDGLELLEAIRELDPDTKIIIL 79
                         90       100
                 ....*....|....*....|....
gi 494040517 842 TGLAEKRQLAELEQMNIQALLNKP 865
Cdd:COG4753   80 SGYSDFEYAQEAIKLGADDYLLKP 103
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
765-882 2.02e-19

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: 87.91  E-value: 2.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPG--IPIVGST 842
Cdd:COG3437   10 LIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEA--PPDLILLDVRMPGMDGFELLRLLRADPSTrdIPVIFLT 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040517 843 GLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELR 127
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
493-865 4.13e-19

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 92.70  E-value: 4.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 493 DMTEQRELEARFLRAQRMEsiGTLASGVAHDLNNILSPIM-MSVPLLRRNLEKETFeNVISTIELSATRGAEIVKQVLTf 571
Cdd:PRK11091 265 DITERKRYQDALEKASRDK--TTFISTISHELRTPLNGIVgLSRILLDTELTAEQR-KYLKTIHVSAITLGNIFNDIID- 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 572 grgLDGVRR--------PTSLASIIQEIIKILG-QTFPKDIRIETELAPDLWR-VVGDSTQLHQVMLNLCVNARDAMPTG 641
Cdd:PRK11091 341 ---MDKMERrklqldnqPIDFTDFLADLENLSGlQAEQKGLRFDLEPLLPLPHkVITDGTRLRQILWNLISNAVKFTQQG 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 642 G-KLRIRgknamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGlglSTVLGI------- 713
Cdd:PRK11091 418 GvTVRVR----------------YEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKP---ATGTGIglavskr 478
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 714 -IKSHHGHVGVSSQTGFGTTF--RIHLPAMGQESEDARA--SQPLNGLprgngECLLVVDDEEHVrrLVQLS-LEASGYT 787
Cdd:PRK11091 479 lAQAMGGDITVTSEEGKGSCFtlTIHAPAVAEEVEDAFDedDMPLPAL-----NILLVEDIELNV--IVARSvLEKLGNS 551
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 788 VLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPG---IPIVGSTG--LAEKRqlaELEQMNIQALL 862
Cdd:PRK11091 552 VDVAMTGKEALEMFDPD--EYDLVLLDIQLPDMTGLDIARELRERYPRedlPPLVALTAnvLKDKK---EYLDAGMDDVL 626

                 ...
gi 494040517 863 NKP 865
Cdd:PRK11091 627 SKP 629
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
618-738 5.43e-19

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: 83.19  E-value: 5.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  618 GDSTQLHQVMLNLCVNARDAMPTGGKLRIRgknamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTK 697
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITVT----------------LSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 494040517  698 GLGKGTGLG-LSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:pfam02518  65 KRGGGGTGLgLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
486-739 6.48e-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: 90.31  E-value: 6.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 486 SVFLIHaDMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPI------MMSVPLLRrnlEKETFENVISTIELSat 559
Cdd:COG5806  175 AVYLIE-NLIENILLRKELQRAEKLEVVSELAASIAHEVRNPLTVVrgfiqlLQEPELSD---EKRKQYIRIALEELD-- 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 560 RGAEIVKQVLTFGRGLDGVRRPTSLASIIQEIIKILGqtfP----KDIRIETELAPDLwRVVGDSTQLHQVMLNLCVNAR 635
Cdd:COG5806  249 RAEAIITDYLTFAKPQPEKLEKIDVSEELEHVIDVLS---PyanmNNVEIQTELEPGL-YIEGDRQKLQQCLINIIKNGI 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 636 DAMPTGGKLRIrgkNAMVDSSYagmlpgatagpnVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTglGLSTVLGIIK 715
Cdd:COG5806  325 EAMPNGGTLTI---DVSIDKNK------------VIISIKDTGVGMTKEQLERLGEPYFSTKEKGTGL--GTMVSYRIIE 387
                        250       260
                 ....*....|....*....|....
gi 494040517 716 SHHGHVGVSSQTGFGTTFRIHLPA 739
Cdd:COG5806  388 AMNGTIRVESEVGKGTTFTITLPL 411
PRK13560 PRK13560
hypothetical protein; Provisional
132-427 7.02e-19

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 92.04  E-value: 7.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 132 TVAQLRESEERF-REVVQNIEQVFWMTNVE---KTEMLFVSDAYEKIWGhTCESLYASPKQWLE-AIHPEDRERVLAA-- 204
Cdd:PRK13560  58 AEAEAQDCREQCeRNLKANIPGGMFLFALDgdgTFSFPSLLDANGELAA-IAKHDLMADKGLLAmLIGGDDGDFFFANpf 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 205 ------ALTRQVDGSYQEEYRIVRPDGavRWISDRAFPVRDADGNVyRVAGISEDVTERRQAQF----DLQLFRKLVDAS 274
Cdd:PRK13560 137 rsaetiAMALQSDDWQEEEGHFRCGDG--RFIDCCLRFERHAHADD-QVDGFAEDITERKRAEErideALHFLQQLLDNI 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 275 NDTFEVIDpESGRFLDVSAKGPAESGFTREEYLKMRVFDINPDIPPSVW-SRYMEQMQAGEAVTGEARHYCKDGTAYPIE 353
Cdd:PRK13560 214 ADPAFWKD-EDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYqEADAAKFDADGSQIIEAEFQNKDGRTRPVD 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 354 FNGKLVQLEKP-----YVVAVIRDISTRKLSEERMREQAAMLNLAHDAIFVHGY---YDGLITF-WNKGAENLYGWSADE 424
Cdd:PRK13560 293 VIFNHAEFDDKenhcaGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIAAIgldADGNICFvNNNAAERMLGWSAAE 372

                 ...
gi 494040517 425 TLG 427
Cdd:PRK13560 373 VMG 375
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
8-106 7.11e-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: 82.28  E-value: 7.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWLS-PSLDLIISDYEMPGFGGMRALE-LKQLaEIDVPFIIISG 85
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEV--DTAADGEEALELLReERPDLVLLDLMMPGMDGLELLRkLREL-PPDIPVIVLTA 77
                         90       100
                 ....*....|....*....|.
gi 494040517  86 SIGEEMAVEAMRRGATDYLLK 106
Cdd:cd00156   78 KADEEDAVRALELGADDYLVK 98
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
764-849 8.93e-19

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: 82.65  E-value: 8.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:cd17554    3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESE--DPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80

                 ....*.
gi 494040517 844 LAEKRQ 849
Cdd:cd17554   81 YSEYKS 86
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
763-879 9.94e-19

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 82.60  E-value: 9.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 763 CLLVVDDEEHVRRLVQLSLE-ASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKiRP---GIPI 838
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEkLAGWEVLTASSGQEGLEKAATE--QPDAILLDVMMPDMDGLATLKKLQA-NPetqSIPV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494040517 839 VGSTGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:cd17552   80 ILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
PAS COG2202
PAS domain [Signal transduction mechanisms];
376-526 1.99e-18

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 85.85  E-value: 1.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 376 RKLSEERMREQAAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEQRNAELLIKDE-- 453
Cdd:COG2202    3 EEALEESERRLRALVESSPDAIIITDL-DGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGgv 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040517 454 WHGEIIQTDRQGKKVIVNSRATLVRDERGKPKSVFLIHADMTEQRELEARFLRAQRMESIGTLASGVAHDLNN 526
Cdd:COG2202   82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLD 154
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
764-875 2.16e-18

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: 81.36  E-value: 2.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRK---IRPGIPIVG 840
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE--PFDLVLMDLQMPVMDGLEATRRIRElegGGRRTPIIA 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494040517 841 STGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTV 875
Cdd:cd17546   79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
763-880 2.52e-18

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 81.30  E-value: 2.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 763 CLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPG-IPIVgS 841
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE--PVDVVISDQRMPGMDGAELLKRVRERYPDtVRIL-L 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494040517 842 TGLAEKRQLaeleqmnIQAL--------LNKPYGSDTLLQTVREALA 880
Cdd:cd17569   79 TGYADLDAA-------IEAInegeiyrfLTKPWDDEELKETIRQALE 118
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
765-876 1.09e-17

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: 79.50  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGL 844
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE--RPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAH 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 494040517  845 AEKRQLAELEQMNIQALLNKPYGSDTLLQTVR 876
Cdd:pfam00072  80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
765-866 1.40e-17

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: 78.93  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVgRIDLVITDLMMP-YMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:cd18161    2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGP-DIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|....*
gi 494040517 844 LAEKRQLAE--LEQMNiqaLLNKPY 866
Cdd:cd18161   81 YAENAIEGGdlAPGVD---VLSKPF 102
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
765-896 1.76e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 79.63  E-value: 1.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEA-SGYTVL-VATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGST 842
Cdd:COG4565    7 LIVEDDPMVAELLRRYLERlPGFEVVgVASSGEEALALLAEH--RPDLILLDIYLPDGDGLELLRELRARGPDVDVIVIT 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494040517 843 GLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATRGGNGHVAANDLSAA 896
Cdd:COG4565   85 AARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDLPEA 138
PAS COG2202
PAS domain [Signal transduction mechanisms];
115-264 2.64e-17

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 82.77  E-value: 2.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 115 AVTQAISQRRlRHEQlktvaQLRESEERFREVVQNIEQVFWMTNvEKTEMLFVSDAYEKIWGHTCESLYAspKQWLEAIH 194
Cdd:COG2202  117 GIARDITERK-RAEE-----ALRESEERLRLLVENAPDGIFVLD-LDGRILYVNPAAEELLGYSPEELLG--KSLLDLLH 187
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494040517 195 PEDRERVLA--AALTRQVDGSYQEEYRIVRPDGAVRWISDRAFPVRDaDGNVYRVAGISEDVTERRQAQFDL 264
Cdd:COG2202  188 PEDRERLLEllRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
2-124 4.57e-17

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: 78.35  E-value: 4.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   2 ASPLNLLIAEDNPDDADLLIWALRGAGFEFEyhVVSKEEDFLRWL-SPSLDLIISDYEMPGFGGMRALE-LKQLAEI-DV 78
Cdd:COG0784    3 LGGKRILVVDDNPDNRELLRRLLERLGYEVT--TAEDGAEALELLrAGPPDLILLDINMPGMDGLELLRrIRALPRLpDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494040517  79 PFIIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRR 124
Cdd:COG0784   81 PIIALTAYADEEDRERALEAGADDYLTKPVdPEELLEALRRLLARAS 127
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
765-879 6.26e-17

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: 77.34  E-value: 6.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTfAQNvGRIDLVITDLMMPYMGGVALIHALRKIrP---GIPIVGS 841
Cdd:cd17562    4 LAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSK-AQS-KKFDLIITDQNMPNMDGIELIKELRKL-PaykFTPILML 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494040517 842 TGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:cd17562   81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
765-882 1.08e-16

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: 77.14  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGL 844
Cdd:cd17549    2 LLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPD--FPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGH 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494040517 845 AEKrqlaeleQMNIQAL-------LNKPYGSDTLLQTVREALATR 882
Cdd:cd17549   80 GDV-------PMAVEAMragaydfLEKPFDPERLLDVVRRALEKR 117
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
493-871 4.16e-16

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 83.25  E-value: 4.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  493 DMTEQRELeARFLRAQRMESI-GTLA-----SGVAHDLNNILSPIMMSVPLLR-RNLEKETFENVISTIELSATRGAEIV 565
Cdd:PRK09959  687 DITETRDL-IHALEVERNKAInATVAksqflATMSHEIRTPISSIMGFLELLSgSGLSKEQRVEAISLAYATGQSLLGLI 765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  566 KQVLTFGRGLDG--VRRP--TSLASIIQEIIKILGQ-TFPKDIRIE-TELAPDLWRVVGDSTQLHQVMLNLCVNARDaMP 639
Cdd:PRK09959  766 GEILDVDKIESGnyQLQPqwVDIPTLVQNTCHSFGAiAASKSIALScSSTFPDHYLVKIDPQAFKQVLSNLLSNALK-FT 844
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  640 TGGKLRIRGKNAMVDSSYAgmlpgatagpNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLGLSTVL--GIIKSH 717
Cdd:PRK09959  845 TEGAVKITTSLGHIDDNHA----------VIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMIckELIKNM 914
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  718 HGHVGVSSQTGFGTTFRIHLPA---MGQESEDARASQPLNgLPRGNGecLLVVDDEEHVRRLVQLSLEASGYTVLVATDG 794
Cdd:PRK09959  915 QGDLSLESHPGIGTTFTITIPVeisQQVATVEAKAEQPIT-LPEKLS--ILIADDHPTNRLLLKRQLNLLGYDVDEATDG 991
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517  795 TEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGLAEKRQLAELEQMNIQALLNKPYGSDTL 871
Cdd:PRK09959  992 VQALHKVSMQ--HYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVL 1066
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
763-839 7.70e-16

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: 74.16  E-value: 7.70e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517 763 CLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSE--QPDLVLCDLRMPEMDGLEVLKQITKESPDTPVI 76
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
765-839 3.60e-15

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: 72.31  E-value: 3.60e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRP--GIPIV 839
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDE--KPDLIILDLMLPGIDGLEVCRILRSDPKtsSIPII 75
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
4-106 4.96e-15

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: 74.17  E-value: 4.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   4 PLNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWL---SPslDLIISDYEMPGFGGMRALE-LKQLAEI-DV 78
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEV--VEAADGEEALELLqehRP--DLILLDLEMPDMDGLELCRrLRADPRTaDI 76
                         90       100
                 ....*....|....*....|....*...
gi 494040517  79 PFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:COG3706   77 PIIFLTALDDEEDRARALEAGADDYLTK 104
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
764-866 5.32e-15

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: 71.38  E-value: 5.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvGRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQG-KDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                         90       100
                 ....*....|....*....|...
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPY 866
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKPF 103
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
6-106 7.54e-15

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 70.96  E-value: 7.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   6 NLLIAEDNPDDADLLIWALRG-AGFEFEYHVVSKEE--DFLRWLSPslDLIISDYEMPGFGGMRALE-LKQLaEIDVPFI 81
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWeAGFEVVGEAENGEEalELLEEHKP--DLVITDINMPGMDGLELLEaIREL-DPDTKII 77
                         90       100
                 ....*....|....*....|....*
gi 494040517  82 IISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:COG4753   78 ILSGYSDFEYAQEAIKLGADDYLLK 102
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
764-839 2.73e-14

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: 70.06  E-value: 2.73e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494040517 764 LLVVDDEEHVRRLVQLSL--EASGYT-VLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIdwEELGFEvVGEAENGEEALELIEEH--KPDIVITDIRMPGMDGLELIEKIRELYPDIKII 77
PRK15115 PRK15115
response regulator GlrR; Provisional
764-882 2.98e-14

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 76.03  E-value: 2.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:PRK15115   8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNRE--KVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTA 85
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:PRK15115  86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQS 124
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
3-137 3.01e-14

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: 72.89  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   3 SPLNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWL-SPSLDLIISDYEMPGFGGMRALE-LKQLAE-IDVP 79
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLRTLGYDV--VTAESGEEALELLlEAPPDLILLDVRMPGMDGFELLRlLRADPStRDIP 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494040517  80 FIIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVAQLR 137
Cdd:COG3437   83 VIFLTALADPEDRERALEAGADDYLTKPFdPEELLARVRNALELRRLQRELDDLVLYLK 141
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-738 3.81e-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: 68.96  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAM----PTGGKLRIRgkNAMVDSSYagmlpgatagpnVILEVQDEGTGIPPEIVERIFDPFFTTKG 698
Cdd:cd16920    1 IQQVLINLVRNGIEAMseggCERRELTIR--TSPADDRA------------VTISVKDTGPGIAEEVAGQLFDPFYTTKS 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040517 699 LGKGTGLGLStvLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16920   67 EGLGMGLSIC--RSIIEAHGGRLSVESPAGGGATFQFTLP 104
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
139-261 3.88e-14

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 69.63  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  139 SEERFREVVQNIEQVFWMTNvEKTEMLFVSDAYEKIWGHTCESLYAspKQWLEAIHPEDRERVLA---AALTRQVDGsYQ 215
Cdd:TIGR00229   1 SEERYRAIFESSPDAIIVID-LEGNILYVNPAFEEIFGYSAEELIG--RNVLELIPEEDREEVRErieRRLEGEPEP-VS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 494040517  216 EEYRIVRPDGAVRWISDRAFPVRdADGNVYRVAGISEDVTERRQAQ 261
Cdd:TIGR00229  77 EERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAE 121
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
765-875 5.69e-14

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: 69.02  E-value: 5.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPG--IPIVGST 842
Cdd:cd17580    2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRF--RPDVILSDIGMPGMDGYELARRLRELPWLanTPAIALT 79
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494040517 843 GLA--EKRQLAELEQMNiqALLNKPYGSDTLLQTV 875
Cdd:cd17580   80 GYGqpEDRERALEAGFD--AHLVKPVDPDELIELI 112
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
15-139 7.90e-14

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: 69.06  E-value: 7.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  15 DDADLL---IWALRGAGFEFEYHvvSKEEDFLRWLSPSL-DLIISDYEMPGFGGMrALeLKQLAEID--VPFIIISGSIG 88
Cdd:cd17549    6 DDADVRealQQTLELAGFRVRAF--ADAEEALAALSPDFpGVVISDIRMPGMDGL-EL-LAQIRELDpdLPVILITGHGD 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 494040517  89 EEMAVEAMRRGATDYLLKGCLS-RLESAVTQAISQRRLRHEQLktvaQLRES 139
Cdd:cd17549   82 VPMAVEAMRAGAYDFLEKPFDPeRLLDVVRRALEKRRLVLENR----RLRQQ 129
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
115-259 8.42e-14

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: 75.01  E-value: 8.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 115 AVTQAISQRRlRHEQlktvaQLRESEERFREVVQNIEQVFWMTNVEKTeMLFVSDAYEKIWGHTCESLYAspKQWLEAIH 194
Cdd:COG5809  121 AISRDITERK-RMEE-----ALRESEEKFRLIFNHSPDGIIVTDLDGR-IIYANPAACKLLGISIEELIG--KSILELIH 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 195 PEDRERVLAAALTRQVDGSY-QEEYRIVRPDGAVRWISDRAFPVrDADGNVYRVAGISEDVTERRQ 259
Cdd:COG5809  192 SDDQENVAAFISQLLKDGGIaQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKK 256
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
185-259 1.22e-13

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 75.48  E-value: 1.22e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517  185 SPKQWLEAIHPEDRERVLA---AALTRqvDGSYQEEYRIVRPDGaVRWISDRAFPVRDADGNVYRVAGISEDVTERRQ 259
Cdd:PRK09776  452 TWQVWYACLHPEDRQRVEKeirDALQG--RSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRQ 526
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
765-840 1.49e-13

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 67.93  E-value: 1.49e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVGrIDLVITDLMMPYMGGVALIHALRKIRPG--IPIVG 840
Cdd:cd17544    4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPD-IKLVITDYNMPEMDGFELVREIRKKYSRdqLAIIG 80
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
765-839 1.80e-13

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: 67.19  E-value: 1.80e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRpGIPIV 839
Cdd:cd17620    2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATR--KPDLIILDLGLPDMDGLEVIRRLREWS-AVPVI 73
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
764-879 2.00e-13

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 67.75  E-value: 2.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYT-VLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALihaLRKIRP-----GIP 837
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKA--GGFDFVITDWNMPNMDGLEL---LKTIRAdgalsHLP 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494040517 838 IVGSTGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:cd19923   78 VLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
764-848 2.58e-13

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 66.63  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVgrIDLVITDLMMPYMGGVALIHALRKIRP--GIPIVGS 841
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYI--PDLIISDIIMPGVDGYSLLGKLRKNADfdTIPVIFL 78

                 ....*....
gi 494040517 842 T--GLAEKR 848
Cdd:cd19927   79 TakGMTSDR 87
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
764-874 4.82e-13

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 73.47  E-value: 4.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:PRK10841 804 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKN--HIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTA 881
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494040517 844 LAekrqLAELEQMNIQA----LLNKPYGSDTLLQT 874
Cdd:PRK10841 882 NA----LAEEKQRCLEAgmdsCLSKPVTLDVLKQT 912
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
764-818 5.06e-13

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: 64.13  E-value: 5.06e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 494040517   764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMP 818
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE--KPDLILLDIMMP 55
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
8-116 5.20e-13

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: 66.02  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517    8 LIAEDNPDDADLLIWALRGAGFEFEyhVVSKEEDFLRWLSP-SLDLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGS 86
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVA--EADDGKEALELLKEeRPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAH 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 494040517   87 IGEEMAVEAMRRGATDYLLKGC-LSRLESAV 116
Cdd:pfam00072  80 GDEDDAVEALEAGADDFLSKPFdPDELLAAI 110
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
15-146 6.09e-13

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 68.20  E-value: 6.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  15 DDADL---LIWALRGAGFEFEYHvvSKEEDFLRWLSPSL-DLIISDYEMPGFGGMRALElkQLAE--IDVPFIIISGSIG 88
Cdd:COG4566    7 DDEAVrdsLAFLLESAGLRVETF--ASAEAFLAALDPDRpGCLLLDVRMPGMSGLELQE--ELAArgSPLPVIFLTGHGD 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040517  89 EEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVAQLRESEERF----REV 146
Cdd:COG4566   83 VPMAVRAMKAGAVDFLEKPFdDQALLDAVRRALARDRARRAERARRAELRARLASLtpreREV 145
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
765-839 6.62e-13

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


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 65.93  E-value: 6.62e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVA-TDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPG--IPIV 839
Cdd:cd17551    4 LIVDDNPTNLLLLEALLRSAGYLEVVSfTDPREALAWCREN--PPDLILLDYMMPGMDGLEFIRRLRALPGLedVPIV 79
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
764-880 7.37e-13

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 67.63  E-value: 7.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:COG4567    7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQA--PPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTG 84
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALA 880
Cdd:COG4567   85 YASIATAVEAIKLGADDYLAKPADADDLLAALERAEG 121
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
764-883 7.74e-13

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 71.80  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADI--HPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALATRG 883
Cdd:PRK11361  85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQS 124
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
764-839 1.08e-12

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: 65.21  E-value: 1.08e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKER--RPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVI 74
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
764-838 1.11e-12

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: 65.48  E-value: 1.11e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPI 838
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGN--RPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPI 73
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
3-129 1.45e-12

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 65.76  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   3 SPLNLLIAEDNPDDADLLIWAL-RGAGFEFEYHVVSKEE--DFLRWLSPslDLIISDYEMPGFGGMRAL-ELKQlAEIDV 78
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLeRLPGFEVVGVASSGEEalALLAEHRP--DLILLDIYLPDGDGLELLrELRA-RGPDV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494040517  79 PFIIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRR-LRHEQ 129
Cdd:COG4565   79 DVIVITAARDPETVREALRAGVVDYLIKPFtFERLREALERYLEYRRlLREDQ 131
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
764-839 1.66e-12

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


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 65.07  E-value: 1.66e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREF--RPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVL 75
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
7-127 1.94e-12

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: 64.91  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEyHVVSKEE--DFLRWLSPslDLIISDYEMPGFGGMRALELKQLAEIDVPFIIIS 84
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVT-HVETGKEalAFLSDQPP--DVVLLDLKLPDMSGMEILKWIQERSLPTSVIVIT 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494040517  85 --GSIgeEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRH 127
Cdd:cd17572   78 ahGSV--DIAVEAMRLGAYDFLEKPFdADRLRVTVRNALKHRKLTK 121
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
765-880 2.01e-12

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


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 64.46  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEA-SGYTVL-VATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGST 842
Cdd:cd17535    2 LIVDDHPLVREGLRRLLESePDIEVVgEAADGEEALALLREL--RPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494040517 843 GLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALA 880
Cdd:cd17535   80 AHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
498-693 4.70e-12

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 69.72  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 498 RELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKE---TFENVISTIELSATRGAEIVKQVLTFGRG 574
Cdd:COG4192  418 RQTQDELIQAAKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQEnyaQLPTSLDKIEGLIERMDKIIKSLRQFSRK 497
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 575 LDGVRRPTSLASIIQEIIKILG-QTFPKDIRIETelaPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIrgknAMV 653
Cdd:COG4192  498 SDTPLQPVDLRQVIEQAWELVEsRAKPQQITLHI---PDDLMVQGDQVLLEQVLVNLLVNALDAVATQPQISV----DLL 570
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 494040517 654 DSSyagmlpgatagPNVILEVQDEGTGIPpeIVERIFDPF 693
Cdd:COG4192  571 SNA-----------ENLRVAISDNGNGWP--LVDKLFTPF 597
PRK13560 PRK13560
hypothetical protein; Provisional
175-261 4.75e-12

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 70.09  E-value: 4.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 175 WGHTCESLYASPKQWLEAIHPEDRERVLA--AALTRQVDGSYQEEYRIVRPDGAVRWISDRAFPVRDADGNVYRVAGISE 252
Cdd:PRK13560 507 FGYEPDEFISGKRMFAAIIHPADLEQVAAevAEFAAQGVDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVI 586

                 ....*....
gi 494040517 253 DVTERRQAQ 261
Cdd:PRK13560 587 DISERKHAE 595
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
4-106 6.67e-12

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: 65.75  E-value: 6.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   4 PLNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWL-SPSLDLIISDYEMPGFGGMRAL-ELKQLaEIDVPFI 81
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEV--DTAADGEEALELLeEERPDLILLDLMLPGMDGLEVCrRLRAR-PSDIPII 77
                         90       100
                 ....*....|....*....|....*
gi 494040517  82 IISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:COG0745   78 MLTARDDEEDRVRGLEAGADDYLTK 102
orf27 CHL00148
Ycf27; Reviewed
762-846 1.38e-11

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 65.51  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 762 ECLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKiRPGIPIVGS 841
Cdd:CHL00148   7 EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKE--QPDLVILDVMMPKLDGYGVCQEIRK-ESDVPIIML 83

                 ....*
gi 494040517 842 TGLAE 846
Cdd:CHL00148  84 TALGD 88
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
764-845 1.45e-11

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 62.07  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:cd17563    3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREE--KPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTG 80

                 ..
gi 494040517 844 LA 845
Cdd:cd17563   81 YA 82
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
404-496 1.70e-11

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 61.32  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  404 DGLITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEQRNAELLIKDEWHGEIIQTDRQGKKVIVNSRATLVRDERGK 483
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGGE 80
                          90
                  ....*....|...
gi 494040517  484 PKSVFLIHADMTE 496
Cdd:pfam13426  81 LVGIIAILRDITE 93
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
4-142 1.88e-11

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 64.21  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   4 PLNLLIAEDNPDDADLLIWALRGAGFEFEYHVVSKEE--DFLRWLSPslDLIISDYEMPGFGGMRALELKQlAEIDVPFI 81
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEVVAEAADGEDavELVRELKP--DLVIVDIDMPDRDGLEAARQIS-EERPAPVI 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040517  82 IISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVAQLRES-EER 142
Cdd:COG3707   80 LLTAYSDPELIERALEAGVSAYLVKPLdPEDLLPALELALARFRELRALRRELAKLREAlEER 142
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
764-847 1.96e-11

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: 61.37  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALrKIRP---GIPIVG 840
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAE--PPDLILLDVMMPGMDGFEVCRRL-KADPatrHIPVIF 77

                 ....*..
gi 494040517 841 STGLAEK 847
Cdd:cd19920   78 LTALTDT 84
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
764-879 2.13e-11

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 61.57  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALrKIRPG---IPIVG 840
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEH--RPTLVISDIVMPEMDGYELCRKI-KSDPDlkdIPVIL 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494040517 841 STGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:cd17598   78 LTTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
764-852 2.32e-11

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: 60.97  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRKiRPG---IPIVG 840
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEE--ELPDLILLDVMMPGMDGFEVCRRLKE-DPEtrhIPVIM 78
                         90
                 ....*....|..
gi 494040517 841 STGLAEKRQLAE 852
Cdd:cd17538   79 ITALDDREDRIR 90
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
765-838 2.73e-11

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: 61.47  E-value: 2.73e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALttFAQNVGRIDLVITDLMMPYMGGVALIHALRKIRPGIPI 838
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGL--EYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPV 72
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
379-504 4.78e-11

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 60.77  E-value: 4.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  379 SEERMReqaAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEQRNAELLIKDEWHGEI 458
Cdd:TIGR00229   1 SEERYR---AIFESSPDAIIVIDL-EGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 494040517  459 IQT---DRQGKKVIVNSRATLVRDErGKPKSVFLIHADMTEQRELEARF 504
Cdd:TIGR00229  77 EERrvrRKDGSEIWVEVSVSPIRTN-GGELGVVGIVRDITERKEAEEAL 124
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
765-877 5.49e-11

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: 60.63  E-value: 5.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIrPG---IPIVGS 841
Cdd:cd17548    3 LIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKE--KPDLILMDIQLPGMDGLEATRLLKED-PAtrdIPVIAL 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494040517 842 TGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVRE 877
Cdd:cd17548   80 TAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
766-880 1.01e-10

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 62.04  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 766 VVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGLA 845
Cdd:COG4566    4 IVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPD--RPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494040517 846 EkrqlaelEQMNIQAL-------LNKPYGSDTLLQTVREALA 880
Cdd:COG4566   82 D-------VPMAVRAMkagavdfLEKPFDDQALLDAVRRALA 116
glnL PRK11073
nitrogen regulation protein NR(II);
407-738 1.65e-10

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 63.56  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 407 ITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEQRNAELlikdewhgeiiqTDRQGkkvIVNSRATLVRDER----- 481
Cdd:PRK11073  29 IHYANPAAQQLLAQSSRKLFGTPLPELLSYFSLNIELMRESL------------QAGQG---FTDNEVTLVIDGRshils 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 482 --GKPKSVFLI---HADMTEQRELEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFENVISTIEL 556
Cdd:PRK11073  94 ltAQRLPEGMIlleMAPMDNQRRLSQEQLQHAQQVAARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 557 SATRGAEIVKQVLtfGRGLDGVRRPTSLASIIQEIIKILGQTFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARD 636
Cdd:PRK11073 174 QADRLRNLVDRLL--GPQRPGTHVTESIHKVAERVVQLVSLELPDNVRLIRDYDPSLPELAHDPDQIEQVLLNIVRNALQ 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 637 AM-PTGGKLRIRGKNAmvdssYAGMLPGATAGPNVILEVQDEGTGIPPEIVERIFDPFfttkglgkGTGLGLSTVLG--- 712
Cdd:PRK11073 252 ALgPEGGTITLRTRTA-----FQLTLHGERYRLAARIDIEDNGPGIPPHLQDTLFYPM--------VSGREGGTGLGlsi 318
                        330       340
                 ....*....|....*....|....*....
gi 494040517 713 ---IIKSHHGHVGVSSQTGFgTTFRIHLP 738
Cdd:PRK11073 319 arnLIDQHSGKIEFTSWPGH-TEFSVYLP 346
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
264-382 1.82e-10

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 59.23  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  264 LQLFRKLVDASNDTFEVIDpESGRFLDVSAKGPAESGFTREEYLKMRVFDI--NPDIPPSVwsRYMEQMQAGE--AVTGE 339
Cdd:TIGR00229   2 EERYRAIFESSPDAIIVID-LEGNILYVNPAFEEIFGYSAEELIGRNVLELipEEDREEVR--ERIERRLEGEpePVSEE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 494040517  340 ARHYCKDGTAYPIEFNGKLVQL--EKPYVVAVIRDISTRKLSEER 382
Cdd:TIGR00229  79 RRVRRKDGSEIWVEVSVSPIRTngGELGVVGIVRDITERKEAEEA 123
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
764-838 2.04e-10

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 58.22  E-value: 2.04e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALttFAQNVGRIDLVITDLMMPYMGGVALIHALRKIRPGIPI 838
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGL--HLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPV 73
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
765-879 2.09e-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: 58.96  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVL-VATDGTEALTTFAQNvgRIDLVITDLMMP-YMGGVALIHALRKIRPgIPIVGST 842
Cdd:cd17534    4 LIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEEN--KPDLILMDINLKgDMDGIEAAREIREKFD-IPVIFLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494040517 843 GLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:cd17534   81 AYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
PRK15347 PRK15347
two component system sensor kinase;
589-865 4.19e-10

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 63.89  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 589 QEIIKILGQTFPKDIRIETELAPDL-WRVVGDSTQLHQVMLNLCVNARDAMPTGG-KLRIRGKNAMVdssyagmlpgata 666
Cdd:PRK15347 479 QAMLTIQGPAQSKSLTLRTFVGAHVpLYLHLDSLRLRQILVNLLGNAVKFTETGGiRLRVKRHEQQL------------- 545
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 667 gpnvILEVQDEGTGIPPEIVERIFDPFFttkglgKGTGLGLSTVLGI-IKSH-----HGHVGVSSQTGFGTTFRIHLP-- 738
Cdd:PRK15347 546 ----CFTVEDTGCGIDIQQQQQIFTPFY------QADTHSQGTGLGLtIASSlakmmGGELTLFSTPGVGSCFSLVLPln 615
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 739 --------------------------AMGQESED-----------------ARASQPLNGLPRGNGECL---------LV 766
Cdd:PRK15347 616 eyappeplkgelsaplalhrqlsawgITCQPGHQnpalldpelaylpgrlyDLLQQIIQGAPNEPVINLplqpwqlqiLL 695
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 767 VDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRK----IRPGIPIVGST 842
Cdd:PRK15347 696 VDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQH--RFDLVLMDIRMPGLDGLETTQLWRDdpnnLDPDCMIVALT 773
                        330       340
                 ....*....|....*....|...
gi 494040517 843 GLAEKRQLAELEQMNIQALLNKP 865
Cdd:PRK15347 774 ANAAPEEIHRCKKAGMNHYLTKP 796
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
4-137 4.66e-10

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 60.60  E-value: 4.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   4 PLNLLIAEDNPDDADLLIWALRgagfEFEYHVVSKE----EDFLRWL-SPSLDLIISDYEMPGFGGMRALelKQLAEIDV 78
Cdd:COG3279    1 MMKILIVDDEPLARERLERLLE----KYPDLEVVGEasngEEALELLeEHKPDLVFLDIQMPGLDGFELA--RQLRELDP 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494040517  79 PFIII--SGSigEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVAQLR 137
Cdd:COG3279   75 PPPIIftTAY--DEYALEAFEVNAVDYLLKPIdEERLAKALEKAKERLEAKAAAEASPEEKD 134
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
764-898 6.08e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 62.36  E-value: 6.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVgrIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV--FDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTA 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALAtrggNGHVAANDLSAALA 898
Cdd:PRK10365  86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA----HTHSIDAETPAVTA 136
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-738 6.58e-10

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: 57.03  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAMP-TGGKLRIRgknamvdSSYAGMLPGATAGPNVIL--EVQDEGTGIPPEIVERIFDPFftTKGL 699
Cdd:cd16918    1 LIQVFLNLVRNAAQALAgSGGEIILR-------TRTQRQVTLGHPRHRLALrvSVIDNGPGIPPDLQDTIFYPM--VSGR 71
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494040517 700 GKGTGLGLSTVLGIIKSHHGHVGVSSQTGFgTTFRIHLP 738
Cdd:cd16918   72 ENGTGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
380-535 7.15e-10

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 62.10  E-value: 7.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 380 EERMREQAAMLNLAHDAIFVhgyYD--GLITFWNKGAENLYGWSADETLGNHFREFIDIDSAQ--LEQRNAELlikdewh 455
Cdd:COG3829    7 KELEEELEAILDSLDDGIIV---VDadGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLevLKTGKPVT------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 456 GEIIQTDRQGKKVIVNsrATLVRDErGKPKSVFLIHADMTEQRELEARFLRAQRMESIGTLASgvahdLNNIL--SPIMM 533
Cdd:COG3829   77 GVIQKTGGKGKTVIVT--AIPIFED-GEVIGAVETFRDITELKRLERKLREEELERGLSAKYT-----FDDIIgkSPAMK 148

                 ..
gi 494040517 534 SV 535
Cdd:COG3829  149 EL 150
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
51-119 8.18e-10

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 57.21  E-value: 8.18e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494040517  51 DLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGSIGEEMAVEAMRRGATDYLLKGC--LSRLESAVTQA 119
Cdd:cd17555   46 DLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAGVMSDAVEALRLGAWDYLTKPIedLAVLEHAVRRA 116
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
9-106 1.17e-09

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 56.83  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   9 IAEDNPDDADLLIWALRGAGFEFEYHvvSKEEDFLRWLSPSL-DLIISDYEMPGFGGMRAL-ELKQLaEIDVPFIIISGS 86
Cdd:cd17537    5 VVDDDEAVRDSLAFLLRSVGLAVKTF--TSASAFLAAAPPDQpGCLVLDVRMPGMSGLELQdELLAR-GSNIPIIFITGH 81
                         90       100
                 ....*....|....*....|
gi 494040517  87 IGEEMAVEAMRRGATDYLLK 106
Cdd:cd17537   82 GDVPMAVEAMKAGAVDFLEK 101
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
490-840 1.63e-09

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 61.84  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 490 IHADMTEQRELEARFLRAQRMESigTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFENVISTIELSATRGAEIVKQVL 569
Cdd:PRK11466 423 LQELVIEHRQARAEAEKASQAKS--AFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDIL 500
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 570 TF------GRGLDGVRRPTSLASIIQEIIKIL-GQTFPKDIRIETELAPDL--WrVVGDSTQLHQVMLNLCVNArdampt 640
Cdd:PRK11466 501 DYsaieagGKNVSVSDEPFEPRPLLESTLQLMsGRVKGRPIRLATDIADDLptA-LMGDPRRIRQVITNLLSNA------ 573
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 641 ggkLRIRGKNAMVDSSYagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLGLSTVLGIIKSHHGH 720
Cdd:PRK11466 574 ---LRFTDEGSIVLRSR-------TDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGE 643
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 721 VGVSSQTGFGTTFRIHLP---AMGQESEDARASQPLNGLPrgngecLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEA 797
Cdd:PRK11466 644 LSATSTPEVGSCFCLRLPlrvATAPVPKTVNQAVRLDGLR------LLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQA 717
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 494040517 798 LTTFAQNVGrIDLVITDLMMPYMGGVALIHALRKIRPGIPIVG 840
Cdd:PRK11466 718 LETLQNSEP-FAAALVDFDLPDYDGITLARQLAQQYPSLVLIG 759
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
154-254 1.70e-09

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 55.72  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 154 FWMTNvEKTEMLFVSDAYEKIWGHTCESLYAspKQWLEAIHPEDRERVLAAALTRQVDGS-YQEEYRIVRPDGAVRWISD 232
Cdd:cd00130    5 VIVLD-LDGRILYANPAAEQLLGYSPEELIG--KSLLDLIHPEDREELRERLENLLSGGEpVTLEVRLRRKDGSVIWVLV 81
                         90       100
                 ....*....|....*....|..
gi 494040517 233 RAFPVRDADGNVYRVAGISEDV 254
Cdd:cd00130   82 SLTPIRDEGGEVIGLLGVVRDI 103
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
765-839 1.79e-09

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 56.10  E-value: 1.79e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVGRIDLVITDLMMPYMGGVALIHALRKIrPGIPIV 839
Cdd:cd17584    2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRLE-MDLPVI 75
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1-137 2.11e-09

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: 57.62  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   1 MASPLNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWLSPSL-DLIISDYEMPGFGGMRALELKQLAEIDVP 79
Cdd:COG4567    1 SAEDRSLLLVDDDEAFARVLARALERRGFEV--TTAASVEEALALLEQAPpDYAVLDLRLGDGSGLDLIEALRERDPDAR 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494040517  80 FIIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVAQLR 137
Cdd:COG4567   79 IVVLTGYASIATAVEAIKLGADDYLAKPAdADDLLAALERAEGDAPAPPENPMSLDRLE 137
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-737 2.44e-09

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 55.54  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAMPTGGKLRIRgknamvdssyagmLPGATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKG 702
Cdd:cd16976    1 IQQVLMNLLQNALDAMGKVENPRIR-------------IAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGKG 67
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494040517 703 TGLGLSTVLGIIKSHHGHVGVSSQTGFGTTFRIHL 737
Cdd:cd16976   68 TGLGLSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
6-106 2.66e-09

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: 55.89  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   6 NLLIAEDNPDDADLLIWALRGAGFEFEYHVVSK-EE--DFLR-----WLSPSLDLIISDYEMPGFGGMRAL-ELKQ---L 73
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDgEEalDFLRgegeyADAPRPDLILLDLNMPRMDGFEVLrEIKAdpdL 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494040517  74 AEIdvPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17557   81 RRI--PVVVLTTSDAEEDIERAYELGANSYIVK 111
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
765-879 2.95e-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: 55.75  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLV-ATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:cd17542    4 LIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKEL--KPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSA 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494040517 844 LAEkrqlaelEQMNIQALLN-------KPYGSDTLLQTVREAL 879
Cdd:cd17542   82 MGQ-------EEMVKEAIKAgakdfivKPFQPERVLEAVEKVL 117
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
393-494 3.60e-09

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 54.95  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 393 AHDAIFVHgYYDGLITFWNKGAENLYGWSADETLGNHFREFIDI-DSAQLEQRNAELLIKDE-WHGEIIQTDRQGKKVIV 470
Cdd:cd00130    1 LPDGVIVL-DLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPeDREELRERLENLLSGGEpVTLEVRLRRKDGSVIWV 79
                         90       100
                 ....*....|....*....|....
gi 494040517 471 NSRATLVRDERGKPKSVFLIHADM 494
Cdd:cd00130   80 LVSLTPIRDEGGEVIGLLGVVRDI 103
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
33-106 3.77e-09

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 55.33  E-value: 3.77e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494040517  33 YHVVSKEE-----DFLRWLSPSLDLIISDYEMPGFGGMRALELKQLaEIDVPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17584   23 YQVTTCTDaeealSMLRENKDEFDLVITDVHMPDMDGFEFLELIRL-EMDLPVIMMSADGSTSTVMKGLAHGACDYLLK 100
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
764-843 4.75e-09

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: 54.70  E-value: 4.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRKiRPGIPIVGSTG 843
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILAR--QDIDLVLLDINLPGKDGLSLTRELRE-QSEVGIILVTG 79
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
766-839 6.64e-09

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 53.99  E-value: 6.64e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517 766 VVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFaqNVGRIDLVITDLMMPYMGGVALIHALRKiRPGIPIV 839
Cdd:cd19936    3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDGL--NARPPDLAILDIKMPRMDGMELLQRLRQ-KSTLPVI 73
PRK09303 PRK09303
histidine kinase;
520-738 7.61e-09

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 58.81  E-value: 7.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 520 VAHDLNNILSPIMMSVPLLRRNLEKETFENVISTIEL---SATRGAEIV----KQVLTFGRG----LDGVRRPTSLASII 588
Cdd:PRK09303 158 LAHDLRTPLTAASLALETLELGQIDEDTELKPALIEQlqdQARRQLEEIerliTDLLEVGRTrweaLRFNPQKLDLGSLC 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 589 QEIIKILGQTF-PKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIrgknamvdssyaGMLPGATAg 667
Cdd:PRK09303 238 QEVILELEKRWlAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGGTITL------------SMLHRTTQ- 304
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517 668 pNVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLGlstvLG------IIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:PRK09303 305 -KVQVSICDTGPGIPEEEQERIFEDRVRLPRDEGTEGYG----IGlsvcrrIVRVHYGQIWVDSEPGQGSCFHFTLP 376
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
765-880 9.43e-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: 56.12  E-value: 9.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVL-VATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPgIPIVGSTG 843
Cdd:COG3707    7 LVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVREL--KPDLVIVDIDMPDRDGLEAARQISEERP-APVILLTA 83
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494040517 844 LAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALA 880
Cdd:COG3707   84 YSDPELIERALEAGVSAYLVKPLDPEDLLPALELALA 120
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
764-879 1.04e-08

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 53.97  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRpGIPIVGSTg 843
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEE--QPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLT- 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494040517 844 lAEKRQLAELEQMNIQA--LLNKPYGSDTLLQTVREAL 879
Cdd:cd17614   77 -AKDSEVDKVLGLELGAddYVTKPFSNRELLARVKANL 113
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
764-839 1.25e-08

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: 53.63  E-value: 1.25e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGvalIHALRKIR--PGIPIV 839
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREV--RPDLVLLDLMLPGIDG---IEVCRQIRaeSGVPIV 75
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
765-880 1.46e-08

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 56.36  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEA-SGYTVL-VATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGST 842
Cdd:COG3279    5 LIVDDEPLARERLERLLEKyPDLEVVgEASNGEEALELLEEH--KPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040517 843 GLAEKrqlaELEQMNIQAL--LNKPYGSDTLLQTVREALA 880
Cdd:COG3279   83 AYDEY----ALEAFEVNAVdyLLKPIDEERLAKALEKAKE 118
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
619-738 1.69e-08

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: 53.27  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 619 DSTQLHQVMLNLCVNARDAMPTGGKLRIRGKnamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFFTTKG 698
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILE--------------KFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDG 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494040517 699 LGKGTGLGL----STVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16925   67 SSTRAHGGTglglSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
fixJ PRK09390
response regulator FixJ; Provisional
766-898 1.83e-08

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 55.39  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 766 VVDDEEHVRRLVQLSLEASGYTVLV---ATDGTEALTTFAQNVgridlVITDLMMPYMGGVALIHALRKIRPGIPIVGST 842
Cdd:PRK09390   8 VVDDDEAMRDSLAFLLDSAGFEVRLfesAQAFLDALPGLRFGC-----VVTDVRMPGIDGIELLRRLKARGSPLPVIVMT 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 843 GLAEKrQLAeLEQMNIQAL--LNKPYGSDTLLQTVREALAT--RGGNGHVAANDLSAALA 898
Cdd:PRK09390  83 GHGDV-PLA-VEAMKLGAVdfIEKPFEDERLIGAIERALAQapEAAKSEAVAADIRARIA 140
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
8-121 2.03e-08

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: 53.28  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPddadLLIWALR---GAGFEFEyhVVSKEED------FLRWLSPslDLIISDYEMPGFGGMRALELKQLAEIDV 78
Cdd:cd17535    2 LIVDDHP----LVREGLRrllESEPDIE--VVGEAADgeealaLLRELRP--DVVLMDLSMPGMDGIEALRRLRRRYPDL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494040517  79 PFIIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAIS 121
Cdd:cd17535   74 KVIVLTAHDDPEYVLRALKAGAAGYLLKDSsPEELIEAIRAVAA 117
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
764-882 2.23e-08

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: 53.36  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV---- 839
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQ--PPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIvita 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494040517 840 -GSTGLAekrqlAELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:cd17572   79 hGSVDIA-----VEAMRLGAYDFLEKPFDADRLRVTVRNALKHR 117
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
765-831 2.30e-08

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: 53.02  E-value: 2.30e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRK 831
Cdd:cd17618    4 LIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEP--RPDLILLDWMLPGGSGIQFIRRLKR 68
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
388-494 2.35e-08

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 52.80  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  388 AMLNLAHDAIFV--HgyyDGLITFWNKGAENLYGWSADETLGNHFREFIDIDSAQLEQRNAELLIKDEWHGEIIQTDR-- 463
Cdd:pfam00989   5 AILESLPDGIFVvdE---DGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFrv 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 494040517  464 -QGKKVIVNSRATLVRDERGKPKSVFLIHADM 494
Cdd:pfam00989  82 pDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
664-738 3.01e-08

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: 52.29  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 664 ATAGPNVILEVQDEGTGIPPEIVERIFDPFFttkGLGKGTGLGLSTVLGI-----IKSHHGH-VGVSSQTGFGTTFRIHL 737
Cdd:cd16948   32 ETNEQGVVLSIKDFGIGIPEEDLPRVFDKGF---TGENGRNFQESTGMGLylvkkLCDKLGHkIDVESEVGEGTTFTITF 108

                 .
gi 494040517 738 P 738
Cdd:cd16948  109 P 109
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
764-831 4.00e-08

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: 52.00  E-value: 4.00e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEAL------TTFAQNVGR-IDLVITDLMMPYMGGVALIHALRK 831
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALnklenlAKEGNDLSKeLDLIITDIEMPKMDGYELTFELRD 75
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
764-839 4.90e-08

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 51.43  E-value: 4.90e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVGriDLVITDLMMPYMGGVALIHALRKiRPGIPIV 839
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGA--DIVLLDLMLPGLSGTEVCRQLRA-RSNVPVI 73
PRK13560 PRK13560
hypothetical protein; Provisional
112-394 4.93e-08

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 56.99  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 112 LESAVTQaISQRRlrheqlKTVAQLRESEERFREVVQNIEQVFWMTNVEKTEMLFVSDAYEKIWGHTCESLYASP----- 186
Cdd:PRK13560 310 LVGAITD-ISGRR------AAERELLEKEDMLRAIIEAAPIAAIGLDADGNICFVNNNAAERMLGWSAAEVMGKPlpgmd 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 187 ------------KQWLEAIHPEDRERVLAAALTRQVDGSYQEEYRIVRPDGAVRWISDRAFPVRDADGNVYRVAGISEDV 254
Cdd:PRK13560 383 pelneefwcgdfQEWYPDGRPMAFDACPMAKTIKGGKIFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDI 462
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 255 TERRQAQFDLQLFRKLVDASNDTFEVIDPESGRFLDVSAKGPAESGFTREEYLK-MRVFD--INPDIPPSVWSRYME--- 328
Cdd:PRK13560 463 TERKQVEEQLLLANLIVENSPLVLFRWKAEEGWPVELVSKNITQFGYEPDEFISgKRMFAaiIHPADLEQVAAEVAEfaa 542
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 329 ------QMQAGEAVTGEARHYCKDGTAYPIEFNGKLVQLEkpyvvAVIRDISTRKLSEERMR----EQAAMLNLAH 394
Cdd:PRK13560 543 qgvdrfEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFE-----GIVIDISERKHAEEKIKaaltEKEVLLKEIH 613
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
764-876 4.99e-08

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: 52.42  E-value: 4.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRrLVQLSLEASGYT--VLVATDGTEALT------TFAQNvGRIDLVITDLMMPYMGGvalIHALRKIR-- 833
Cdd:cd17557    3 LLVEDNPGDAE-LIQEAFKEAGVPneLHVVRDGEEALDflrgegEYADA-PRPDLILLDLNMPRMDG---FEVLREIKad 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494040517 834 PG---IPIVGSTGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVR 876
Cdd:cd17557   78 PDlrrIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIR 123
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
8-106 5.56e-08

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: 51.25  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPDDADLLIWALRGAGFEFeYHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRAL-ELKQLaEIDVPFIIISGS 86
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEV-DTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCrRLREK-GSDIPIIMLTAK 78
                         90       100
                 ....*....|....*....|
gi 494040517  87 IGEEMAVEAMRRGATDYLLK 106
Cdd:cd17574   79 DEEEDKVLGLELGADDYITK 98
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
7-122 6.64e-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: 51.95  E-value: 6.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEyhVVSKEED------FLRWLSPslDLIISDYEMPGFGGmraLEL-KQLAEI--D 77
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGFE--VVGEAENgeealeLIEEHKP--DIVITDIRMPGMDG---LELiEKIRELypD 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494040517  78 VPFIIISGsIGE-EMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQ 122
Cdd:cd17536   74 IKIIILSG-YDDfEYAQKAIRLGVVDYLLKPVdEEELEEALEKAKEE 119
PRK10610 PRK10610
chemotaxis protein CheY;
764-871 6.82e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 51.90  E-value: 6.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGY-TVLVATDGTEALTTFaqNVGRIDLVITDLMMPYMGGVALIHALRK--IRPGIPIVG 840
Cdd:PRK10610   8 FLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKL--QAGGFGFVISDWNMPNMDGLELLKTIRAdgAMSALPVLM 85
                         90       100       110
                 ....*....|....*....|....*....|.
gi 494040517 841 STGLAEKRQLAELEQMNIQALLNKPYGSDTL 871
Cdd:PRK10610  86 VTAEAKKENIIAAAQAGASGYVVKPFTAATL 116
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
766-879 7.79e-08

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 51.44  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 766 VVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVGriDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGLA 845
Cdd:cd17537    5 VVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQP--GCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494040517 846 EKrqlaeleQMNIQAL-------LNKPYGSDTLLQTVREAL 879
Cdd:cd17537   83 DV-------PMAVEAMkagavdfLEKPFRDQVLLDAIEQAL 116
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
764-839 9.58e-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: 51.33  E-value: 9.58e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALAS--GPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVL 74
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
764-882 1.65e-07

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 51.21  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASgYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLEED-FDVLTAASAEEALAILEEE--WVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040517 844 LAEKRQL-AELEQMNIQALLNKPYGSDTLLQTVREALATR 882
Cdd:cd17596   80 YTDSEDIiAGINEAGIYQYLTKPWHPDQLLLTVRNAARLF 119
pleD PRK09581
response regulator PleD; Reviewed
765-844 1.82e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 54.52  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALrKIRPG---IPIVGS 841
Cdd:PRK09581   6 LVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICER--EQPDIILLDVMMPGMDGFEVCRRL-KSDPAtthIPVVMV 82

                 ...
gi 494040517 842 TGL 844
Cdd:PRK09581  83 TAL 85
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
764-839 1.82e-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: 50.38  E-value: 1.82e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRKiRPGIPIV 839
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLE--GSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVL 73
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
764-846 1.87e-07

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: 50.45  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVGriDLVITDLMMPYMGGVALIHALRKIrPGIPIVGSTG 843
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPP--DLILLDLMLPGTDGLTLCREIRRF-SDVPIIMVTA 78

                 ...
gi 494040517 844 LAE 846
Cdd:cd19938   79 RVE 81
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
765-876 1.95e-07

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 50.14  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKiRPGIPIVGSTG- 843
Cdd:cd17594    3 LVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHR--RVDLVLLDLRLGQESGLDLLRTIRA-RSDVPIIIISGd 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494040517 844 -LAEKRQLAELEqMNIQALLNKPYGSDTLLQTVR 876
Cdd:cd17594   80 rRDEIDRVVGLE-LGADDYLAKPFGLRELLARVR 112
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
7-106 2.07e-07

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: 50.16  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEyHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGM------RALElkqLAEIDVPF 80
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVD-VAENGQEALELLKEEPFDLVLMDLQMPVMDGLeatrriRELE---GGGRRTPI 76
                         90       100
                 ....*....|....*....|....*.
gi 494040517  81 IIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17546   77 IALTANALEEDREKCLEAGMDDYLSK 102
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
764-880 2.33e-07

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 50.10  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLV-ATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGiPIVGST 842
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKH--KPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494040517 843 GLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALA 880
Cdd:cd19932   80 AYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIA 117
PRK13558 PRK13558
bacterio-opsin activator; Provisional
48-265 2.38e-07

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 54.46  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  48 PSLDLIISDYEMPGFGGMRALE-LKQlaEIDVPFIIISGSIGEE-MAVEAMRRGATDYLL---KGCLSRLESAVTQAISQ 122
Cdd:PRK13558  50 GEIDCVVADHEPDGFDGLALLEaVRQ--TTAVPPVVVVPTAGDEaVARRAVDADAAAYVPavsDDATAAIAERIESAVPE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 123 RRLRHEQLKTVAQLR-ESEERFREVVQNiEQVFWMTNVEKTE----MLFVSDAYEKIWGHTCESLYASPKQWLEAihpED 197
Cdd:PRK13558 128 HSRDTEARMPISDLTvESDRRLKERALD-EAPVGITIADATLpdepLIYINDAFERITGYSPDEVLGRNCRFLQG---ED 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 198 RERVLAAALTRQVDG--SYQEEYRIVRPDGAVRWISDRAFPVRDADGNVYRVAGISEDVTERRQAQFDLQ 265
Cdd:PRK13558 204 TNEERVAELREAIDEerPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALQ 273
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
764-839 2.67e-07

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 49.42  E-value: 2.67e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLvATDGTEALTTFAQNvGRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVR-TTGNAATLWRWVEE-GEGDLVITDVVMPDENGLDLIPRIKKARPDLPII 74
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
365-742 2.80e-07

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 53.70  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 365 YVVAVIRDISTRKLSEERMR---EQAAMLNLAHDAIFVHGYyDGLITFWNKGAENLYGWSAdetLGNHFREFIDiDSAQL 441
Cdd:COG3290   62 LLLLLLLAALLLKLLEEIARlveEREAVLESIREGVIAVDR-DGRITLINDAARRLLGLDA---IGRPIDEVLA-EVLET 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 442 EQRNAELLIKdewhgeiiqtdrqGKKVIVNSRATLVRDERGKPKSVFlihADMTEQRELEARF---------LRAQRmes 512
Cdd:COG3290  137 GERDEEILLN-------------GRVLVVNRVPIRDDGRVVGAVATF---RDRTELERLEEELegvkelaeaLRAQR--- 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 513 igtlasgvaHDLNNILSPIMMsvpllrrNLEKETFENVISTI-ELSATRGAEIVKQVLTFGrgldgvrrPTSLASIIQEI 591
Cdd:COG3290  198 ---------HDFRNHLHTISG-------LLQLGEYDEALEYIdEISEELQELIDSLLSRIG--------NPVLAALLLGK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 592 IKILGQtfpKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGG------KLRIRGKNAMVdssyagmlpgat 665
Cdd:COG3290  254 AARARE---RGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIEAVEKLPeeerrvELSIRDDGDEL------------ 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 666 agpnvILEVQDEGTGIPPEIVERIFDP-----------FfttkglgkgtglGLSTVLGIIKSHHGHVGVSSQTGFGTTFR 734
Cdd:COG3290  319 -----VIEVEDSGPGIPEELLEKIFERgfstklgegrgL------------GLALVKQIVEKYGGTIEVESEEGEGTVFT 381

                 ....*...
gi 494040517 735 IHLPAMGQ 742
Cdd:COG3290  382 VRLPKEGE 389
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
764-831 2.88e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 52.50  E-value: 2.88e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgrIDLVITDLMMPYMGGVALIHALRK 831
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS---IDLLLLDVMMPKKNGIDTLKELRQ 68
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
521-739 2.89e-07

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 54.08  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 521 AHDLNNILSPIMMSVPLLRRNLEKETFENVISTIELSATRGAEIVKQVLTFGR-----GLDgVRRPTSLASIIQEI---- 591
Cdd:PRK11100 264 THELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARleqrqELE-VLEPVALAALLEELvear 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 592 -IKILGQtfpkdiRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGknamvdssyagmlpgATAGPNV 670
Cdd:PRK11100 343 eAQAAAK------GITLRLRPDDARVLGDPFLLRQALGNLLDNAIDFSPEGGTITLSA---------------EVDGEQV 401
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494040517 671 ILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLG---LSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLPA 739
Cdd:PRK11100 402 ALSVEDQGPGIPDYALPRIFERFYSLPRPANGRKSTglgLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
764-829 3.17e-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: 50.28  E-value: 3.17e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 764 LLVVDDEEHVRRLVQLSLEAS-GYTVL-VATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHAL 829
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEpDIEVVgEAADGEEALELLEEL--RPDVVLLDIRMPGMDGLEALRRL 69
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
387-449 3.50e-07

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 48.16  E-value: 3.50e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517   387 AAMLNLAHDAIFVHgYYDGLITFWNKGAENLYGWSADETLGNHFREFIDI-DSAQLEQRNAELL 449
Cdd:smart00091   4 RAILESLPDGIFVL-DLDGRILYANPAAEELLGYSPEELIGKSLLELIHPeDRERVQEALQRLL 66
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
764-879 3.63e-07

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 52.11  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTG 843
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATR--KPDLIILDLGLPDGDGIEFIRDLRQWSAIPVIVLSAR 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494040517 844 LAEKRQLAELEqMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:PRK10529  82 SEESDKIAALD-AGADDYLSKPFGIGELQARLRVAL 116
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
764-879 3.87e-07

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 49.68  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIhalRKIRP--GIPIVGS 841
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDE--QPSLVVLDIMLPGMDGLTVC---REVREhsHVPILML 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494040517 842 TGLAEK-RQLAELEqMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:cd19939   77 TARTEEmDRVLGLE-MGADDYLCKPFSPRELLARVRALL 114
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
762-879 4.41e-07

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: 49.47  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 762 ECLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGS 841
Cdd:cd17553    1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKE--RPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIM 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494040517 842 TGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:cd17553   79 TAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
fixJ PRK09390
response regulator FixJ; Provisional
9-146 4.75e-07

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 51.16  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   9 IAEDNPDDADLLIWALRGAGFEFEYHvvSKEEDFLRWLsPSLDL--IISDYEMPGFGGMRAL-ELKQLAeIDVPFIIISG 85
Cdd:PRK09390   8 VVDDDEAMRDSLAFLLDSAGFEVRLF--ESAQAFLDAL-PGLRFgcVVTDVRMPGIDGIELLrRLKARG-SPLPVIVMTG 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517  86 SIGEEMAVEAMRRGATDYLLKG-----CLSRLESAVTQAISQRRLRHEQLKTVAQLRESEERFREV 146
Cdd:PRK09390  84 HGDVPLAVEAMKLGAVDFIEKPfederLIGAIERALAQAPEAAKSEAVAADIRARIASLSERERQV 149
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
764-865 5.20e-07

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 49.32  E-value: 5.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVGRIDLVITDLMMPYMGG--VAL-IHALRKIRPGIPIVG 840
Cdd:cd19933    3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGfeVALrIRKLFGRRERPLIVA 82
                         90       100
                 ....*....|....*....|....*
gi 494040517 841 STGLAEKRQLAELEQMNIQALLNKP 865
Cdd:cd19933   83 LTANTDDSTREKCLSLGMNGVITKP 107
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
512-573 5.36e-07

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 47.59  E-value: 5.36e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494040517  512 SIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKETFENVISTIELSATRGAEIVKQVLTFGR 573
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSR 62
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
764-838 5.81e-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: 49.20  E-value: 5.81e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALttFAQNVGRIDLVITDLMMPYMGGVALIHALRKIRPGIPI 838
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEAL--FQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPV 73
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
164-259 6.20e-07

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


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 48.95  E-value: 6.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  164 MLFVSDAYEKIWGHTCESLYASPkqWLEAIHPEDRERVlAAALTRQVDG-SYQEEYRIVRPDGAVRWISDRAFPVRDADG 242
Cdd:pfam08448  17 VRYANAAAAELFGLPPEELLGKT--LAELLPPEDAARL-ERALRRALEGeEPIDFLEELLLNGEERHYELRLTPLRDPDG 93
                          90
                  ....*....|....*..
gi 494040517  243 NVYRVAGISEDVTERRQ 259
Cdd:pfam08448  94 EVIGVLVISRDITERRR 110
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
217-257 7.07e-07

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 46.41  E-value: 7.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 494040517   217 EYRIVRPDGAVRWISDRAFPVRDADGNVYRVAGISEDVTER 257
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
766-839 7.35e-07

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 48.81  E-value: 7.35e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517 766 VVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd19919    5 IVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASS--QPDVLISDIRMPGMDGLALLAQIKQRHPDLPVI 76
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
51-106 1.05e-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: 48.26  E-value: 1.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517  51 DLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17550   44 DLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHGTIETAVKATKLGAYDFIEK 99
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
765-879 1.06e-06

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 48.54  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLV--ATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPgIPIVGST 842
Cdd:cd17541    4 LIVDDSAVMRKLLSRILESDPDIEVVgtARDGEEALEKIKEL--KPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040517 843 GLAEKRQLAELEQMNIQAL--LNKPYGSDTL-LQTVREAL 879
Cdd:cd17541   81 SLTEEGAEITLEALELGAVdfIAKPSGGISLdLEEIAEEL 120
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
6-106 1.13e-06

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: 48.21  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   6 NLLIAEDNPDDADLLIWALRGAGFEfeyHVVSKEE--DFLRWLS---PslDLIISDYEMP---GFGGMRALElKQLAEID 77
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYL---EVVSFTDprEALAWCRenpP--DLILLDYMMPgmdGLEFIRRLR-ALPGLED 75
                         90       100
                 ....*....|....*....|....*....
gi 494040517  78 VPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17551   76 VPIVMITADTDREVRLRALEAGATDFLTK 104
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
265-694 1.41e-06

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 51.83  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  265 QLFRKLVDASNDTFEVIDPESGrFLDVSAKGPAESGFTREEYL-KMRVFDINPDIPPSV----WSRYMEQMQ-AGEAVTg 338
Cdd:TIGR02938   4 EAYRQTVDQAPLAISITDLKAN-ILYANDAFTRITGYTKEEIIgKNESVLSNHTTPPEVyqalWGSLAEQKPwAGKLLN- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  339 eaRHycKDGTAYPIEFNGKLV---QLEKPYVVAVIRDISTRKLSEERMREQAAMLNLAHDAI---FVHGYYDGLITFWN- 411
Cdd:TIGR02938  82 --RR--KDGELYLAELTVAPVlneAGETTHFLGMHRDITELHRLEQVVANQKLLIESVVDAApvaFVLLDPTGRVILDNq 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  412 ---KGAENLYGWSADETLGNHFRE-----FIDIDSAQLEQRNAELLIkDEWHGeiiqtdRQGKKVIVNSRAtlVRDERGK 483
Cdd:TIGR02938 158 eykKLATDLRVKEPAHTVLDLLREawreaLAENWPQQLAFSNREARF-DRGGG------RPARWLSCTGSV--IGMESDC 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  484 PKSVF---------LIHADMTEQRE---------LEARFLRAQRMESIGTLASGVAHDLNNILSPIMMSVPLLRRNLEKE 545
Cdd:TIGR02938 229 ADSFFcaaeqpyllLTIADISNLREeqerarlsaLQALMAEEERLEAIRETLSAAIHRLQGPMNLISAAISVLQRRGDDA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  546 TFENVISTIE--LSATRGA-EIVKQVLTfgRGLDGVRRPTSLASIIQEIIKILG-QTFPKDIRIETELAPDLWRVVGDST 621
Cdd:TIGR02938 309 GNPASAAMLQqaLSAGREHmEALRQVIP--QSPQEIVVPVNLNQILRDVITLSTpRLLAAGIVVDWQPAATLPAILGREL 386
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040517  622 QLHQVMLNLCVNARDAMPTGGKLRIRGKnamvdssyagmLPGATAGPNVILEVQDEGTGIPPEIVERIFDPFF 694
Cdd:TIGR02938 387 QLRSLFKALVDNAIEAMNIKGWKRRELS-----------ITTALNGDLIVVSILDSGPGIPQDLRYKVFEPFF 448
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
767-843 1.70e-06

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 47.36  E-value: 1.70e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494040517 767 VDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRK--IRPGIPIVGSTG 843
Cdd:cd17602    4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNS--KPDLILIDIDMPDLDGYELCSLLRKssALKDTPIIMLTG 80
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
163-256 1.88e-06

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 47.07  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  163 EMLFVSDAYEKIWGHTCESLYASPKQWLeaIHPEDRERVLAAALtRQVDGSYQEEYRIVRPDGAVRWISDRAFPVRDADG 242
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDL--FAEPEDSERLREAL-REGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
                          90
                  ....*....|....
gi 494040517  243 NVYRVAGISEDVTE 256
Cdd:pfam13426  80 ELVGIIAILRDITE 93
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
518-738 2.00e-06

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


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 51.23  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  518 SGVAHDLNNILSPIMMSVP-LLRRNLEKETFENVI--STIELSatRGAEIVKQVLTFGRGLDGV----RRPTSLASIIQE 590
Cdd:TIGR01386 246 ADLAHELRTPLTNLLGQTQvALSQPRTGEEYREVLesNLEELE--RLSRMVSDMLFLARADNGQlaleRVRLDLAAELAK 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  591 IIKILGQTFP-KDIRIETELAPdlwRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGknamvdssyagmlpgATAGPN 669
Cdd:TIGR01386 324 VAEYFEPLAEeRGVRIRVEGEG---LVRGDPQMFRRAISNLLSNALRHTPDGGTITVRI---------------ERRSDE 385
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040517  670 VILEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGL----GLSTVLGIIKSHHGHVGVSSQTGFgTTFRIHLP 738
Cdd:TIGR01386 386 VRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEgtglGLAIVRSIMEAHGGRASAESPDGK-TRFILRFP 457
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
510-573 2.02e-06

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: 46.05  E-value: 2.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 510 MESIGTLASGVAHDLNNILSPIMMSVPLLRRNL-EKETFENVISTIELSATRGAEIVKQVLTFGR 573
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELlDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
8-106 2.18e-06

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: 47.22  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPDDADLLIWALRGAGFEFEYhVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGSI 87
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDV-CFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALD 79
                         90
                 ....*....|....*....
gi 494040517  88 GEEMAVEAMRRGATDYLLK 106
Cdd:cd17625   80 AVEDRVKGLDLGADDYLPK 98
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
7-107 2.66e-06

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 46.99  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFE--------YHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMR-ALELKQ---LA 74
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAeavdgeeaLNKLENLAKEGNDLSKELDLIITDIEMPKMDGYElTFELRDdprLA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494040517  75 eiDVPFIIISGSIGEEMAVEAMRRGATDYLLKG 107
Cdd:cd19924   81 --NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
493-739 2.85e-06

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 50.78  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 493 DMTEQRELEArflrAQRmesigTLASGVAHDLNNILSPI-----MMSVPllrrNLEKETFENVISTIELSATRGAEIVKQ 567
Cdd:PRK11006 193 DVTQMHQLEG----ARR-----NFFANVSHELRTPLTVLqgyleMMQDQ----PLEGALREKALHTMREQTQRMEGLVKQ 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 568 VLTFGR-------GLDGVRRPTSLASIIQEIIKILGQ-----TFPKDirietelapDLWRVVGDSTQLHQVMLNLCVNAR 635
Cdd:PRK11006 260 LLTLSKieaaptiDLNEKVDVPMMLRVLEREAQTLSQgkhtiTFEVD---------NSLKVFGNEDQLRSAISNLVYNAV 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 636 DAMPTGGKLRIRGKNamvdsSYAGMLpgatagpnviLEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLGLSTVLGIIK 715
Cdd:PRK11006 331 NHTPEGTHITVRWQR-----VPQGAE----------FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVK 395
                        250       260
                 ....*....|....*....|....*...
gi 494040517 716 ---SHH-GHVGVSSQTGFGTTFRIHLPA 739
Cdd:PRK11006 396 halSHHdSRLEIESEVGKGTRFSFVLPE 423
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
141-254 3.29e-06

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 46.64  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  141 ERFREVVQNIEQVFWMTNvEKTEMLFVSDAYEKIWGHTCESLyaSPKQWLEAIHPEDRERVLAAALTRQVDG--SYQEEY 218
Cdd:pfam00989   1 EDLRAILESLPDGIFVVD-EDGRILYVNAAAEELLGLSREEV--IGKSLLDLIPEEDDAEVAELLRQALLQGeeSRGFEV 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 494040517  219 RIVRPDGAVRWISDRAFPVRDADGNVYRVAGISEDV 254
Cdd:pfam00989  78 SFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-738 3.67e-06

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: 46.55  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARdamptggKLRIRGKNAMVDSSYagmlpGATAGPNVIlEVQDEGTGIPPEIVERIFDPF--FTTKGLG 700
Cdd:cd16921    1 LGQVLTNLLGNAI-------KFRRPRRPPRIEVGA-----EDVGEEWTF-YVRDNGIGIDPEYAEKVFGIFqrLHSREEY 67
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494040517 701 KGTGLGLSTVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16921   68 EGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
764-896 4.44e-06

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 48.77  E-value: 4.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGteaLTTF-AQNVGRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGST 842
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNG---LNGYhLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLT 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494040517 843 GLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREALatRGGNGHVAANDLSAA 896
Cdd:PRK09836  80 ALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL--RRGAAVIIESQFQVA 131
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
51-106 4.62e-06

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 46.62  E-value: 4.62e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517  51 DLIISDYEMPGFGGMRALElKQLAEIDVPFIIISGSIGE--EMAVEAMRRGATDYLLK 106
Cdd:cd17541   48 DVITLDIEMPVMDGLEALR-RIMAERPTPVVMVSSLTEEgaEITLEALELGAVDFIAK 104
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
623-738 4.67e-06

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: 46.33  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAMPTGG-KLRIRGKNAMVDSSYagmlpgatagpnVILEVQDEGTGIPPEIVERIFDPFFTTKGLGK 701
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEvTLRVSLEEEEEDGVQ------------LRFSVEDTGIGIPEEQQARLFEPFSQADSSTT 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494040517 702 GTGLglSTVLG------IIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16922   69 RKYG--GTGLGlaiskkLVELMGGDISVESEPGQGSTFTFTLP 109
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
8-106 4.91e-06

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: 46.00  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPDDADLLIWALRGAGFEFeYHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRALelKQLAEI-DVPFIIISGS 86
Cdd:cd17620    2 LVIEDEPQIRRFLRTALEAHGYRV-FEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVI--RRLREWsAVPVIVLSAR 78
                         90       100
                 ....*....|....*....|
gi 494040517  87 IGEEMAVEAMRRGATDYLLK 106
Cdd:cd17620   79 DEESDKIAALDAGADDYLTK 98
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
764-876 6.74e-06

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 45.86  E-value: 6.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALttfaqNVGRI---DLVITDLMMPYMGGVALIHALRKIRPGIPIVG 840
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGL-----DLGKLydyDIILLDLNLPDMSGYEVLRTLRLAKVKTPILI 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494040517 841 STGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVR 876
Cdd:cd17616   76 LSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
764-877 6.90e-06

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: 45.99  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEAS-GYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRK--IRPGIpIVG 840
Cdd:cd17593    3 VLICDDSSMARKQLARALPADwDVEITFAENGEEALEILRE--GRIDVLFLDLTMPVMDGYEVLEALPVeqLETKV-IVV 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494040517 841 StglAEKRQLAELEQMNIQAL--LNKPYGSDTLLQTVRE 877
Cdd:cd17593   80 S---GDVQPEAKERVLELGALafLKKPFDPEKLAQLLEE 115
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
124-261 7.21e-06

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 50.06  E-value: 7.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  124 RLRHEQlktvAQLRESEERFREVVQ---------NIEQVFWMTNVEKTEMLfvsdayekiwGHTCESLYASPKQWLeaIH 194
Cdd:PRK09776  270 AFRAER----KHISESETRFRNAMEysaigmalvGTEGQWLQVNKALCQFL----------GYSQEELRGLTFQQL--TW 333
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517  195 PEDRERVLaaaltRQVD-------GSYQEEYRIVRPDGAVRWISDRAFPVRDADGN-VYRVAGIsEDVTERRQAQ 261
Cdd:PRK09776  334 PEDLNKDL-----QQVEkllsgeiNSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTpLYFIAQI-EDINELKRTE 402
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
764-872 1.02e-05

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: 45.51  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGY-TVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGST 842
Cdd:cd17530    3 VLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCN--APDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494040517 843 GL-----AEKRQLAELEQMNIQALLNKPYGSDTLL 872
Cdd:cd17530   81 GLdggilESAETLAGANGLNLLGTLSKPFSPEELT 115
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
404-499 1.10e-05

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


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 45.10  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  404 DGLITFWNKGAENLYGWSADETLGNHFREFI-DIDSAQLEQRNAELLIKDEWHGEIIQTDRQGKKVIVNSRATLVRDERG 482
Cdd:pfam08448  14 DGRVRYANAAAAELFGLPPEELLGKTLAELLpPEDAARLERALRRALEGEEPIDFLEELLLNGEERHYELRLTPLRDPDG 93
                          90
                  ....*....|....*..
gi 494040517  483 KPKSVFLIHADMTEQRE 499
Cdd:pfam08448  94 EVIGVLVISRDITERRR 110
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
619-738 1.11e-05

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: 45.22  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 619 DSTQLHQVMLNLCVNARDAM---PTG-GKLRIRGKnamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFf 694
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIegrPSDvGEVRIRVE--------------ADQDGRIVLIVCDNGKGFPREMRHRATEPY- 65
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 494040517 695 ttkglgkGTGLGLSTVLG------IIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16944   66 -------VTTRPKGTGLGlaivkkIMEEHGGRISLSNREAGGACIRIILP 108
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
8-106 1.49e-05

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 44.98  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPDDADLLIWALRGAGFEFEyHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRAL-ELKQLAEI-DVPFIIISG 85
Cdd:cd17562    4 LAVDDSASIRQMVSFTLRGAGYEVV-EAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIkELRKLPAYkFTPILMLTT 82
                         90       100
                 ....*....|....*....|.
gi 494040517  86 SIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17562   83 ESSDEKKQEGKAAGATGWLVK 103
PRK11173 PRK11173
two-component response regulator; Provisional
764-830 2.01e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 46.93  E-value: 2.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 764 LLVVDDEeHVRRLVQLSL-EASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALR 830
Cdd:PRK11173   6 ILIVEDE-LVTRNTLKSIfEAEGYDVFEATDGAEMHQILSEN--DINLVIMDINLPGKNGLLLARELR 70
PRK10693 PRK10693
two-component system response regulator RssB;
51-128 2.17e-05

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 47.29  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  51 DLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGSigEEMA--VEAMRRGATDYLLKGC--LSRLESAV---------- 116
Cdd:PRK10693  19 DLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISAT--ENMAdiAKALRLGVQDVLLKPVkdLNRLREMVfaclypsmfn 96
                         90
                 ....*....|..
gi 494040517 117 TQAISQRRLRHE 128
Cdd:PRK10693  97 SRVEEEERLFRD 108
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
765-839 2.75e-05

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 44.28  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEAL---------TTFAQNVGRIDLVITDLMMPYMGGVALihaLRKIRPG 835
Cdd:cd17581    2 LAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALeflgledeeDSSNFNEPKVNMIITDYCMPGMTGYDL---LKKVKES 78

                 ....*....
gi 494040517 836 -----IPIV 839
Cdd:cd17581   79 salkeIPVV 87
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
766-880 3.06e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 47.56  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 766 VVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVGriDLVITDLMMPYMGGVALIHALRKIRPGIPIVGSTGLA 845
Cdd:PRK10923   8 VVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTP--DVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494040517 846 EKRQLAELEQMNIQALLNKPYGSDTLLQTVREALA 880
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIS 120
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
765-883 3.25e-05

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 44.07  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLV--ATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGST 842
Cdd:cd17532    2 LIVDDEPLAREELRYLLEEHPDIEIVgeAENGEEALEAIEEL--KPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVT 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494040517 843 GLaekRQLAeLEQMNIQAL--LNKPYGSDTLLQTVREALATRG 883
Cdd:cd17532   80 AY---DEYA-VEAFELNAVdyLLKPFSEERLAEALAKLRKRLS 118
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
7-106 3.29e-05

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 43.65  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWLSPSL-DLIISDYEMPGFGGMRALELKQLAEIDVPFIIISG 85
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEV--RTTGNAATLWRWVEEGEgDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSA 78
                         90       100
                 ....*....|....*....|.
gi 494040517  86 SIGEEMAVEAMRRGATDYLLK 106
Cdd:cd19928   79 QNTLMTAVKAAERGAFEYLPK 99
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
8-106 3.58e-05

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 43.97  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPDDADLLIWALRGAGFeFEYHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRALELKQlAEIDVPFIIISGSI 87
Cdd:cd17594    3 LVVDDDAAMRHLLILYLRERGF-DVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR-ARSDVPIIIISGDR 80
                         90       100
                 ....*....|....*....|
gi 494040517  88 GEEMA-VEAMRRGATDYLLK 106
Cdd:cd17594   81 RDEIDrVVGLELGADDYLAK 100
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
764-854 4.49e-05

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 43.52  E-value: 4.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGiPIVGSTG 843
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIARE--KPDAVLLDIMLPGIDGLTLCRDLRPKYQG-PILLLTA 79
                         90
                 ....*....|..
gi 494040517 844 L-AEKRQLAELE 854
Cdd:cd17622   80 LdSDIDHILGLE 91
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-738 4.76e-05

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: 43.34  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAMPTGGKLRIRgknamvdssYAGMLPGATagpnviLEVQDEGTGIPPEIVERIFDPFFTTKGLGKG 702
Cdd:cd16952    1 LRSAFSNLVSNAVKYTPPSDTITVR---------WSQEESGAR------LSVEDTGPGIPPEHIPRLTERFYRVDIERCR 65
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040517 703 TGLGLSTVLGIIK----SHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16952   66 NTGGTGLGLAIVKhvmsRHDARLLIASELGKGSRFTCLFP 105
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
7-106 6.31e-05

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 43.04  E-value: 6.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEyHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGS 86
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVD-VAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTAR 79
                         90       100
                 ....*....|....*....|
gi 494040517  87 IGEEMAVEAMRRGATDYLLK 106
Cdd:cd19934   80 DSWQDKVEGLDAGADDYLTK 99
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
765-898 6.42e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.03  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEAS-GYTVL-VATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVAlihALRKI---RPgIPIV 839
Cdd:PRK12555   4 GIVNDSPLAVEALRRALARDpDHEVVwVATDGAQAVERCAAQ--PPDVILMDLEMPRMDGVE---ATRRImaeRP-CPIL 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 840 GSTGLAEKRQLAELEQMNIQAL--LNKP---------YGSDTLLQTVREALATRGGNGHVAANDLSAALA 898
Cdd:PRK12555  78 IVTSLTERNASRVFEAMGAGALdaVDTPtlgigagleEYAAELLAKIDQIGRLLGRRLAPAAAPAAASAA 147
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
7-106 6.73e-05

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: 42.86  E-value: 6.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEYhvVSKEEDFLRWLSP-SLDLIISDYEMPGFGGMRALELKQLAEIDVPFIIISG 85
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDW--VRTGAEAEAALASgPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTA 78
                         90       100
                 ....*....|....*....|.
gi 494040517  86 SIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17624   79 RDGVDDRVAGLDAGADDYLVK 99
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
7-106 8.32e-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: 42.75  E-value: 8.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGfeFEYHVVSKEEDFLRWLSPSL-DLIISDYEMPGFGGMRAL-ELKQLAeiDVPFIIIS 84
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAG--YAPTLLAHGDQVLPYVRHTPpDLILLDLMLPGTDGLTLCrEIRRFS--DVPIIMVT 77
                         90       100
                 ....*....|....*....|..
gi 494040517  85 GSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd19938   78 ARVEEIDRLLGLELGADDYICK 99
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
300-507 8.34e-05

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 46.30  E-value: 8.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 300 GFTREEylkMRVFDINPDIPPSVWSRYMEQMQ----AGEA-VTGEARHYC---KDGTAYPIEFNGKLVQLE-KPYVVAVI 370
Cdd:PRK11359  46 GYKREE---VIGNNIDMLIPRDLRPAHPEYIRhnreGGKArVEGMSRELQlekKDGSKIWTRFALSKVSAEgKVYYLALV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 371 RDISTrklsEERMREQAAMLNLAHD----AIFVHGYYDGLITFwNKGAENLYGWSADETLGNHFREFIDI--DSAQLEQR 444
Cdd:PRK11359 123 RDASV----EMAQKEQTRQLIIAVDhldrPVIVLDPERRIVQC-NRAFTEMFGYCISEASGMQPDTLLNIpeFPADNRIR 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517 445 NAELLIKDEW-HGEIIQTDRQGKKVIVNSRATLVRDERGKPKSVFLIHADMTEQ---RELEARFLRA 507
Cdd:PRK11359 198 LQQLLWKTARdQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEErqiRQLEGNILAA 264
PRK10604 PRK10604
sensor protein RstB; Provisional
515-693 8.37e-05

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 46.13  E-value: 8.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 515 TLASGVAHDLNNilspimmsvPLLR--------RNL---EKETFENVISTIElsatrgaEIVKQVLTFGRgLDGVRRPTS 583
Cdd:PRK10604 214 QLIDGIAHELRT---------PLVRlryrlemsDNLsaaESQALNRDIGQLE-------ALIEELLTYAR-LDRPQNELH 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 584 LASI-----IQEIIKILgQTFPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNARDAmpTGGKLRIrgknamvdssya 658
Cdd:PRK10604 277 LSEPdlpawLSTHLADI-QAVTPEKTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRY--AHSRVRV------------ 341
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 494040517 659 GMLpgaTAGPNVILEVQDEGTGIPPEIVERIFDPF 693
Cdd:PRK10604 342 SLL---LDGNQACLIVEDDGPGIPPEERERVFEPF 373
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
764-839 8.45e-05

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 42.65  E-value: 8.45e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPgIPIV 839
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQF--KPDLVLLDINLPYFDGFYWCREIRQISN-VPII 73
ompR PRK09468
osmolarity response regulator; Provisional
760-883 8.64e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 44.96  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 760 NGECLLVVDDEEHVRRLVQLSLEASGYTVLVATDGtEALTTFAQNvGRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:PRK09468   4 ENYKILVVDDDMRLRALLERYLTEQGFQVRSAANA-EQMDRLLTR-ESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPII 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494040517 840 GSTGLAEK-RQLAELEqMNIQALLNKPYGSDTLLQTVREALATRG 883
Cdd:PRK09468  82 MLTAKGEEvDRIVGLE-IGADDYLPKPFNPRELLARIRAVLRRQA 125
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
51-142 1.07e-04

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 44.63  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  51 DLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGSIGEEMAVEAMRRGATDYLLKG-----CLSRLESAVTQ------- 118
Cdd:PRK10651  54 DLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDmepedLLKALQQAAAGemvlsea 133
                         90       100
                 ....*....|....*....|....*....
gi 494040517 119 -----AISQRRLRHEQLKTVAQLRESEER 142
Cdd:PRK10651 134 ltpvlAASLRANRATTERDVNQLTPRERD 162
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
51-106 1.18e-04

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 42.27  E-value: 1.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494040517  51 DLIISDYEMPGFGGMRALelKQLAEID--VPFIIISgSIG-EEMAVEAMRRGATDYLLK 106
Cdd:cd17542   47 DLVTMDITMPEMDGIEAL--KEIKKIDpnAKVIMCS-AMGqEEMVKEAIKAGAKDFIVK 102
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
6-106 1.23e-04

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 42.04  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   6 NLLIAEDNPDDADLLIWALRGAGFEFEyHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRALE-LKQLAEiDVPFIIIS 84
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVE-TAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPpLRALQP-DARIVVLT 79
                         90       100
                 ....*....|....*....|....
gi 494040517  85 G--SIGeeMAVEAMRRGATDYLLK 106
Cdd:cd17563   80 GyaSIA--TAVEAIKLGADDYLAK 101
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
141-204 1.36e-04

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 40.85  E-value: 1.36e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517   141 ERFREVVQNIEQVFWMTNvEKTEMLFVSDAYEKIWGHTCESLYASPkqWLEAIHPEDRERVLAA 204
Cdd:smart00091   1 ERLRAILESLPDGIFVLD-LDGRILYANPAAEELLGYSPEELIGKS--LLELIHPEDRERVQEA 61
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
15-106 1.58e-04

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 41.87  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  15 DDADLLIW----ALRGAGFEFEyhVVSKEEDFLRWLSPSL-DLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGSIGE 89
Cdd:cd19919    7 DDDSSIRWvlerALAGAGLTVT--SFENAQEALAALASSQpDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHSDL 84
                         90
                 ....*....|....*..
gi 494040517  90 EMAVEAMRRGATDYLLK 106
Cdd:cd19919   85 DSAVSAYQGGAFEYLPK 101
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
766-865 1.59e-04

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 41.49  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 766 VVDDEEHVRRLVQLSLEAS--GYTVLVATDGTEAL--TTFAQnvgrIDLVITDLMMPYMGGVALIHALRKIRPGIPIVGS 841
Cdd:cd17565    3 IVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYdeILFLQ----PDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMI 78
                         90       100
                 ....*....|....*....|....
gi 494040517 842 TGLAEKRQLAELEQMNIQALLNKP 865
Cdd:cd17565   79 SQVSDKEMIGKAYQAGIEFFINKP 102
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-128 1.86e-04

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 44.84  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   1 MASPLNLLIAEDNPDDADLLIWALRGAGFEfEYHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRALELKQLAEIDVPF 80
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQGFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494040517  81 IIISGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHE 128
Cdd:PRK11361  80 ILMTAYAEVETAVEALRCGAFDYVIKPFdLDELNLIVQRALQLQSMKKE 128
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-738 1.89e-04

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: 41.28  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAmpTGGKLRIrgknamvdSSYagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPFFttkgLGKG 702
Cdd:cd16950    1 LKRVLSNLVDNALRY--GGGWVEV--------SSD-------GEGNRTRIQVLDNGPGIAPEEVDELFQPFY----RGDN 59
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494040517 703 TGLGLSTVLG------IIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:cd16950   60 ARGTSGTGLGlaivqrISDAHGGSLTLANRAGGGLCARIELP 101
PRK10766 PRK10766
two-component system response regulator TorR;
763-843 1.99e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 43.87  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 763 CLLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKiRPGIPIVGST 842
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQ--HVDLILLDINLPGEDGLMLTRELRS-RSTVGIILVT 80

                 .
gi 494040517 843 G 843
Cdd:PRK10766  81 G 81
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
47-106 2.02e-04

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: 41.94  E-value: 2.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517  47 SPSLDLIISDYEMPgfgGMRALELKQLAEID-----VPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd19923   43 AGGFDFVITDWNMP---NMDGLELLKTIRADgalshLPVLMVTAEAKKENVIAAAQAGVNNYIVK 104
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
764-839 2.07e-04

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 41.23  E-value: 2.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNVGRIDLVITDLMMPYMGGVALIHAL--RKIRPGIPIV 839
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIDLILTEVDLPVSSGFKLLSYImrHKICKNIPVI 78
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
764-839 2.69e-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: 2.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517 764 LLVVDDEEHVRR-LVQL-SLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:cd19930    1 VLIAEDQEMVRGaLAALlELEDDLEVVAQASNGQEALRLVLKH--SPDVAILDIEMPGRTGLEVAAELREELPDTKVL 76
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
5-134 3.55e-04

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 43.87  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   5 LNLLIAEDNPDDADLLIWALRGAGFEFEYhVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRAL-ELKQLAEIdVPFIII 83
Cdd:PRK10365   6 IDILVVDDDISHCTILQALLRGWGYNVAL-ANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLkEIKALNPA-IPVLIM 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 494040517  84 SGSIGEEMAVEAMRRGATDYLLKGC-LSRLESAVTQAISQRRLRHEQLKTVA 134
Cdd:PRK10365  84 TAYSSVETAVEALKTGALDYLIKPLdFDNLQATLEKALAHTHSIDAETPAVT 135
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
46-106 4.26e-04

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 40.79  E-value: 4.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494040517  46 LSPslDLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd19931   43 LDP--DLILLDLNMKGMSGLDTLKALREEGVSARIVILTVSDAEDDVVTALRAGADGYLLK 101
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
7-124 4.42e-04

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: 40.75  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEyHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRAleLKQL-AEIDVPFIIISG 85
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVR-AAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDV--LKELrKTSQVPVLMLTA 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040517  86 SiGEEM-AVEAMRRGATDYLLKGCLSRLESAVTQAIsQRR 124
Cdd:cd17623   78 R-GDDIdRILGLELGADDYLPKPFNPRELVARIRAI-LRR 115
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
6-106 4.43e-04

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: 40.70  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   6 NLLIAEDNPDDADLLIWALRGAGFE-FEYHVVSKEEDFLRWLSPslDLIISDYEMPGFGGMRALE-LKQLAEI-DVPFII 82
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDvVEAEDAESAVNLIVEPRP--DLILLDWMLPGGSGIQFIRrLKRDEMTrDIPIIM 79
                         90       100
                 ....*....|....*....|....
gi 494040517  83 ISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17618   80 LTARGEEEDKVRGLEAGADDYITK 103
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
765-838 4.55e-04

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 40.21  E-value: 4.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517 765 LVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRPGIPI 838
Cdd:cd19926    2 LVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASE--PYDLCLTDMRLPDGSGLELVQHIQQRLPQTPV 73
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-739 4.83e-04

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: 40.39  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNArdamptggkLRIRGKNAMVDSSYAGMLpgatagpnVILEVQDEGTGIPPEIVERIFDPFFTTKGLGKG 702
Cdd:cd16949    1 LARALENVLRNA---------LRYSPSKILLDISQDGDQ--------WTITITDDGPGVPEDQLEQIFLPFYRVDSARDR 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494040517 703 TGLGLSTVLGI----IKSHHGHVGVSSQTGFGTTFRIHLPA 739
Cdd:cd16949   64 ESGGTGLGLAIaeraIEQHGGKIKASNRKPGGLRVRIWLPA 104
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
764-839 6.29e-04

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 42.26  E-value: 6.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQnvGRIDLVITDLMMPYMGGVALIHALRKIRPGIPIV 839
Cdd:PRK11083   6 ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQ--QPPDLVILDVGLPDISGFELCRQLLAFHPALPVI 79
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
39-106 7.68e-04

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 40.04  E-value: 7.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  39 EEDFLRWLSPSLDLIISDYEMPGFGGMRAL-ELKQLAEI-DVPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17581   43 EEDSSNFNEPKVNMIITDYCMPGMTGYDLLkKVKESSALkEIPVVIMSSENIPTRISRCLEEGAEDFLLK 112
envZ PRK09467
osmolarity sensor protein; Provisional
516-738 8.31e-04

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 42.98  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 516 LASGVAHDLNNILSPI-----MMSvpllrrnlEKETF--ENVISTIELSAtrgaEIVKQVLTFGR-GLDGVRRPTSLASI 587
Cdd:PRK09467 232 LMAGVSHDLRTPLTRIrlateMMS--------EEDGYlaESINKDIEECN----AIIEQFIDYLRtGQEMPMEMADLNAL 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 588 IQEIIKILGqtfPKDIRIETELAPDLWRVVGDSTQLHQVMLNLCVNArdAMPTGGKLRIRGKnamVDSSYAGmlpgatag 667
Cdd:PRK09467 300 LGEVIAAES---GYEREIETALQPGPIEVPMNPIAIKRALANLVVNA--ARYGNGWIKVSSG---TEGKRAW-------- 363
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040517 668 pnviLEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLGL--STVLGIIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:PRK09467 364 ----FQVEDDGPGIPPEQLKHLFQPFTRGDSARGSSGTGLglAIVKRIVDQHNGKVELGNSEEGGLSARAWLP 432
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
7-106 1.03e-03

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 39.70  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEYHVVSKEEDFLRWLSpSLDLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGS 86
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLY-DYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGL 79
                         90       100
                 ....*....|....*....|
gi 494040517  87 IGEEMAVEAMRRGATDYLLK 106
Cdd:cd17616   80 ADIEDKVKGLGFGADDYMTK 99
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
764-879 1.04e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 41.63  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFaqNVGRIDLVITDLMMPYMGGVALIHALRK--IRPGIPIVGS 841
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQL--NEPWPDLILLDWMLPGGSGIQFIKHLKResMTRDIPVVML 82
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494040517 842 TGLAEKRQLAELEQMNIQALLNKPYGSDTLLQTVREAL 879
Cdd:PRK10161  83 TARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
7-106 1.11e-03

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: 39.35  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEyhVVSKEEDFLRW-LSPSLDLIISDYEMPGFGGMRAL-ELKQlAEIDVPFIIIS 84
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVD--VAYDGEDGLHLaLTNEYDLIILDVMLPGLDGLEVLrRLRA-AGKQTPVLMLT 77
                         90       100
                 ....*....|....*....|..
gi 494040517  85 GSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd19935   78 ARDSVEDRVKGLDLGADDYLVK 99
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
672-739 1.17e-03

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: 39.34  E-value: 1.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494040517 672 LEVQDEGTGIPPEIVERIFDPFFTTKGLGKGTGLGLSTVLGIIKS----HHGHVGVSSQTGFGTTFRIHLPA 739
Cdd:cd16939   33 LIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRvalwHGGHVECDDSELGGACFRLTWPR 104
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-721 1.29e-03

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: 39.37  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 623 LHQVMLNLCVNARDAMPTGGKLRIRgknAMVDssyagmlpgataGPNVILEVQDEGTGIPPEIVERIFDPFFttkGLGKG 702
Cdd:cd16945    5 LRQAINNLLDNAIDFSPEGGLIALQ---LEAD------------TEGIELLVFDEGSGIPDYALNRVFERFY---SLPRP 66
                         90       100
                 ....*....|....*....|....*
gi 494040517 703 TGLGLSTVLG------IIKSHHGHV 721
Cdd:cd16945   67 HSGQKSTGLGlafvqeVAQLHGGRI 91
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
41-106 1.32e-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: 38.92  E-value: 1.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040517  41 DFLRWLSPSLDLIISDYEMPGFGGMRALELKQLAEI--DVPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17582   36 DVLEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKIckNIPVIMMSSQDSVGVVFKCLSKGAADYLVK 103
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
407-484 1.47e-03

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 38.47  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  407 ITFWNKGAENLYGWSADETLG--NHFREFIDIDSAQLEQRNAELLIKD--EWHGEIIQTDRQGKKVIVNSRATLVRDERG 482
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGgePYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                  ..
gi 494040517  483 KP 484
Cdd:pfam08447  81 KP 82
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
8-106 1.73e-03

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: 39.18  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   8 LIAEDNPDDADLLIWALRGAGFEFEyhVVSKEEDFLRWL-SPSLDLIISDYEMPGFGGMRAL-ELKQLAEI-DVPFIIIS 84
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVV--TAYDGEEALKRAkDEKPDLIILDLMLPGIDGLEVCrILRSDPKTsSIPIIMLT 78
                         90       100
                 ....*....|....*....|..
gi 494040517  85 GSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd19937   79 AKGEEFDKVLGLELGADDYITK 100
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
48-106 1.77e-03

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: 39.04  E-value: 1.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040517  48 PSLDLIISDYEMPgfgGMRALEL-----KQLAEIDVPFIIISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17544   44 PDIKLVITDYNMP---EMDGFELvreirKKYSRDQLAIIGISASGDNALSARFIKAGANDFLTK 104
PRK10490 PRK10490
sensor protein KdpD; Provisional
605-738 1.91e-03

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 41.95  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 605 IETELAPDLWRVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRgknamvdssyagmlpgATAGPNVI-LEVQDEGTGIPP 683
Cdd:PRK10490 761 INLSLPEPLTLIHVDGPLFERVLINLLENAVKYAGAQAEIGID----------------AHVEGERLqLDVWDNGPGIPP 824
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040517 684 EIVERIFDPFfttkglgkGTGLGLSTVLG----------IIKSHHGHVGVSSQTGFGTTFRIHLP 738
Cdd:PRK10490 825 GQEQLIFDKF--------ARGNKESAIPGvglglaicraIVEVHGGTIWAENRPEGGACFRVTLP 881
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
15-129 2.12e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 41.78  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517  15 DDADLLIW----ALRGAGFE---FEyhvvsKEEDFLRWLSPSL-DLIISDYEMPGFGGMRALELKQLAEIDVPFIIISGS 86
Cdd:PRK10923  10 DDDSSIRWvlerALAGAGLTcttFE-----NGNEVLEALASKTpDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 494040517  87 IGEEMAVEAMRRGATDYLLK-----GCLSRLESAVTQAISQRRLRHEQ 129
Cdd:PRK10923  85 SDLDAAVSAYQQGAFDYLPKpfdidEAVALVERAISHYQEQQQPRNIQ 132
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
764-846 2.13e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 40.82  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 764 LLVVDDEEHVRRLVQLSLEASGYTVLVATDGTEALTTFAQNvgRIDLVITDLMMPYMGGVALIHALRKIRpGIPIVGSTG 843
Cdd:PRK10710  13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQT--PPDLILLDLMLPGTDGLTLCREIRRFS-DIPIVMVTA 89

                 ...
gi 494040517 844 LAE 846
Cdd:PRK10710  90 KIE 92
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
7-123 2.38e-03

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 38.51  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEyHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRAL-ELKQlaEIDVPFIIISG 85
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVS-VFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCrEVRE--HSHVPILMLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494040517  86 SIGEEMAVEAMRRGATDYLLKGCLSRLESAVTQAISQR 123
Cdd:cd19939   79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR 116
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
764-834 2.41e-03

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 39.24  E-value: 2.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517 764 LLVVDDEEHVRRLVQLSLEA---SGYTVLVATDGTEALTTFAQNVGR---IDLVITDLMMPYMGGVALIHALRKIRP 834
Cdd:cd17595    3 ILTVDDDPQVLRAVARDLRRqygKDYRVLRADSGAEALDALKELKLRgeaVALFLVDQRMPEMDGVEFLEKAMELFP 79
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
7-106 2.58e-03

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: 38.25  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFeYHVVSKEEDFLRWLSPSLDLIISDYEMPGFGGMRAL-ELKQLAEI-DVPFIIIS 84
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEV-LTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCrRLKEDPETrHIPVIMIT 80
                         90       100
                 ....*....|....*....|..
gi 494040517  85 GSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSK 102
PRK15115 PRK15115
response regulator GlrR; Provisional
4-123 2.58e-03

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 41.36  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   4 PLNLLIAEDNPDDADLLIWALRGAGFefeyHVVSKE--EDFLRWLS-PSLDLIISDYEMPGFGGMRALELKQLAEIDVPF 80
Cdd:PRK15115   5 PAHLLLVDDDPGLLKLLGMRLTSEGY----SVVTAEsgQEALRVLNrEKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494040517  81 IIIS--GSIGEemAVEAMRRGATDYLLKGC-LSRLESAVTQAISQR 123
Cdd:PRK15115  81 IILTahGSIPD--AVAATQQGVFSFLTKPVdRDALYKAIDDALEQS 124
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
616-731 2.90e-03

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: 38.54  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 616 VVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKnamvdssyagmlpgATAGPNVIleVQDEGTGIPPEIVERIFDPFFT 695
Cdd:cd16940    7 VQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLS--------------ADDGAVIR--VEDNGPGIDEEELEALFERFYR 70
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494040517 696 TKGLGKGTG-LGLSTVLGIIKSHHGHVGVSSQTGFGT 731
Cdd:cd16940   71 SDGQNYGGSgLGLSIVKRIVELHGGQIFLGNAQGGGL 107
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
615-741 2.93e-03

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 41.30  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 615 RVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIRGKnamvdssyagmlpgaTAGPNVILEVQDEGTGIPPEIVERIFDPFF 694
Cdd:PRK09835 368 QVAGDPLMLRRAISNLLSNALRYTPAGEAITVRCQ---------------EVDHQVQLVVENPGTPIAPEHLPRLFDRFY 432
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494040517 695 TTKGLGKGTGLGLSTVLGIIKS----HHGHVGVSSQTGfGTTFRIHLPAMG 741
Cdd:PRK09835 433 RVDPSRQRKGEGSGIGLAIVKSivvaHKGTVAVTSDAR-GTRFVISLPRLE 482
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
5-60 3.80e-03

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: 36.39  E-value: 3.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 494040517     5 LNLLIAEDNPDDADLLIWALRGAGFEFeyHVVSKEEDFLRWL-SPSLDLIISDYEMP 60
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEV--DEATDGEEALELLkEEKPDLILLDIMMP 55
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-694 4.07e-03

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: 37.94  E-value: 4.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040517 623 LHQVMLNLCVNARD-AMPTGGKLRIRGknamvdssyagmlpgATAGPNVILEVQDEGTGIPPEIVERIFDPFF 694
Cdd:cd16953    1 LGQVLRNLIGNAISfSPPDTGRITVSA---------------MPTGKMVTISVEDEGPGIPQEKLESIFDRFY 58
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
7-112 4.27e-03

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 38.08  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFEYHVVSKEEdfLRWLSPSL-DLIISDYEMP---GFGGMRALEL-KQLAeiDVPFI 81
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREA--LAMLAEHRpTLVISDIVMPemdGYELCRKIKSdPDLK--DIPVI 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494040517  82 IISGSIGEEMAVEAMRRGATDYLLKGC-----LSRL 112
Cdd:cd17598   77 LLTTLSDPRDVIRGLECGADNFITKPYdekylLSRI 112
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
765-839 4.38e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 40.52  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 765 LVVDDEEHVRRLVQLSLEA-SGYTVL-VATDGTEALTTFAQNvgRIDLVITDLMMPYMGGvalIHALRKI---RPgIPIV 839
Cdd:PRK00742   7 LVVDDSAFMRRLISEILNSdPDIEVVgTAPDGLEAREKIKKL--NPDVITLDVEMPVMDG---LDALEKImrlRP-TPVV 80
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
619-694 6.10e-03

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: 37.44  E-value: 6.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040517 619 DSTQLHQVMLNLCVNARDAMPTGGKLRIRgknamvdssyAGMLPGAtagpnVILEVQDEGTGIPPEIVERIFDPFF 694
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGGKLRIR----------AAQTPQE-----VRLDVEDSAPGVSDDQLARLFERFY 61
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
7-106 6.67e-03

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: 37.11  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEfeyhvVSKEED------FLRWLSPslDLIISDYEMPGFGGMRALE-LK---QLAEI 76
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYR-----VLVATDgqqalqRAQAEPP--DLILLDVMMPGMDGFEVCRrLKadpATRHI 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 494040517  77 DVPFIIISGSIGEEmaVEAMRRGATDYLLK 106
Cdd:cd19920   74 PVIFLTALTDTEDK--VKGFELGAVDYITK 101
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
7-106 6.85e-03

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: 37.33  E-value: 6.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517   7 LLIAEDNPDDADLLIWALRGAGFEFE-----YHVVSKEEDFlrwlSPslDLIISDYEMPGFGGMRALELKQLAEIDVPFI 81
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVEtaadgAEALAAAREF----RP--DAVVLDIMLPDMDGLEVLRRLRADGPDVPVL 75
                         90       100
                 ....*....|....*....|....*
gi 494040517  82 IISGSIGEEMAVEAMRRGATDYLLK 106
Cdd:cd17615   76 FLTAKDSVEDRIAGLTAGGDDYVTK 100
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
611-737 7.00e-03

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: 37.82  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040517 611 PDLwrVVGDSTQLHQVMLNLCVNARDAMPTGGKLRIR----GKNAMVDSSYAGMLPGATAGPNVI--LEVQDEGTGIPPe 684
Cdd:cd16938    2 PDV--VVGDERRVFQVLLHMLGNLLKMRNGGGNITFRvfleGGSEDRSDRDWGPWRPSMSDESVEirFEVEINDSGSPS- 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494040517 685 iverIFDPFFTTKGLGKGTGLGLSTVLG------IIKSHHGHVGVSSQTGFGTTFRIHL 737
Cdd:cd16938   79 ----IESASMRNSLNRRYNLSELGEHLSfsickqLVQLMGGNIWIVPGSGLGTTMSLLL 133
 
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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