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Conserved domains on  [gi|494453306|ref|WP_007243883|]
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MULTISPECIES: blue light-activated sensor histidine kinase [Pseudomonas]

Protein Classification

hybrid sensor histidine kinase/response regulator( domain architecture ID 11486708)

two-component hybrid sensor histidine kinase/response regulator having PAS sensor and/or ligand binding domains; similar to Pseudomonas syringae blue-light-activated protein, which acts as photosensitive kinase and response regulator that is involved in increased bacterial virulence upon exposure to light

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
1-534 0e+00

histidine kinase; Provisional


:

Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 1064.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   1 MSENKTRVDNAATGDIQHQGKDIFFAAVETTRMPMIVTDPNRPDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDP 80
Cdd:PRK13557   9 PHGRAPSVDESAAGDVSDHRSDIFFAAVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  81 AVVQSIRDAIAQRNDISAEIINYRKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRRKDAEEALRQAQKMEALGQLTG 160
Cdd:PRK13557  89 ATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQAQKMEALGQLTG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 161 GIAHDFNNLLQVMGGYIDLIGSAAEKPVIDVQRVQRSVYHAKSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEP 240
Cdd:PRK13557 169 GIAHDFNNLLQVMSGYLDVIQAALSHPDADRGRMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVSGMGE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 241 LIERTFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINARDALIGRENpkVFIETRNLLVDELANMSYDGLLPGRYVS 320
Cdd:PRK13557 249 LAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGR--VTIRTRNVEIEDEDLAMYHGLPPGRYVS 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 321 IAVTDNGIGMPASIRDRVMDPFFTTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEAGLTNTESPQ 400
Cdd:PRK13557 327 IAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEPK 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 401 ASDRRLGSSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMYDLLFTDLIMPGGMNGVMLAREVRRR 480
Cdd:PRK13557 407 ARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPGGMNGVMLAREARRR 486
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494453306 481 YPKVKVLLTTGYAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVLDGPNGIA 534
Cdd:PRK13557 487 QPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLDGPTGVG 540
 
Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
1-534 0e+00

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 1064.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   1 MSENKTRVDNAATGDIQHQGKDIFFAAVETTRMPMIVTDPNRPDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDP 80
Cdd:PRK13557   9 PHGRAPSVDESAAGDVSDHRSDIFFAAVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  81 AVVQSIRDAIAQRNDISAEIINYRKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRRKDAEEALRQAQKMEALGQLTG 160
Cdd:PRK13557  89 ATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQAQKMEALGQLTG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 161 GIAHDFNNLLQVMGGYIDLIGSAAEKPVIDVQRVQRSVYHAKSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEP 240
Cdd:PRK13557 169 GIAHDFNNLLQVMSGYLDVIQAALSHPDADRGRMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVSGMGE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 241 LIERTFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINARDALIGRENpkVFIETRNLLVDELANMSYDGLLPGRYVS 320
Cdd:PRK13557 249 LAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGR--VTIRTRNVEIEDEDLAMYHGLPPGRYVS 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 321 IAVTDNGIGMPASIRDRVMDPFFTTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEAGLTNTESPQ 400
Cdd:PRK13557 327 IAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEPK 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 401 ASDRRLGSSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMYDLLFTDLIMPGGMNGVMLAREVRRR 480
Cdd:PRK13557 407 ARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPGGMNGVMLAREARRR 486
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494453306 481 YPKVKVLLTTGYAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVLDGPNGIA 534
Cdd:PRK13557 487 QPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLDGPTGVG 540
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
21-391 2.52e-84

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 265.56  E-value: 2.52e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  21 KDIFFAAVETTRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDpaVVQSIRDAIAQRNDISA-E 99
Cdd:COG3852    6 EELLRAILDSLPDAVIVLDA---DGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP--LRELLERALAEGQPVTErE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 100 IINYRKDGSSFWNALFISPVYNDAGDlIYFFASQLDISRRKDAEEALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDL 179
Cdd:COG3852   81 VTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 180 IGSAAEKPvidvqRVQRSVYHAKSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIERTFGPEVAIETDLEPA 259
Cdd:COG3852  160 LERELPDD-----ELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 260 LKNCRIDPTQAEVALLNIFINARDALigRENPKVFIETRNLLVDELAnmsydGLLPGRYVSIAVTDNGIGMPASIRDRVM 339
Cdd:COG3852  235 LPEVLGDPDQLIQVLLNLVRNAAEAM--PEGGTITIRTRVERQVTLG-----GLRPRLYVRIEVIDNGPGIPEEILDRIF 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 494453306 340 DPFFTTKEegKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEA 391
Cdd:COG3852  308 EPFFTTKE--KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQA 357
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
270-387 3.11e-59

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: 191.82  E-value: 3.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 270 AEVALLNIFINARDALIgrENPKVFIETRNLLVDELANMSYDGLLPGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEG 349
Cdd:cd16919    1 LELAILNLAVNARDAMP--EGGRLTIETSNQRVDADYALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVG 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494453306 350 KGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16919   79 KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
44-137 3.34e-18

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: 79.43  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   44 DNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGpdtDPAVVQSIRDAIAQ-RNDISAEIINYRKDGSSFWNALFISPVYND 122
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREgKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
                          90
                  ....*....|....*
gi 494453306  123 AGDLIYFFASQLDIS 137
Cdd:pfam13426  78 GGELVGIIAILRDIT 92
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
265-388 3.44e-18

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 80.00  E-value: 3.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   265 IDPTQAEVALLNIFINARDAliGRENPKVFIETRNLlvdelanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPFFT 344
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKY--TPEGGRITVTLERD---------------GDHVEITVEDNGPGIPPEDLEKIFEPFFR 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 494453306   345 TKE---EGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPV 388
Cdd:smart00387  64 TDKrsrKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPL 110
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
26-146 1.60e-17

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: 78.87  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   26 AAVETTRMPMIVTDPNrpdNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQR-NDISAEIINYR 104
Cdd:TIGR00229   7 AIFESSPDAIIVIDLE---GNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEpEPVSEERRVRR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 494453306  105 KDGSSFWNALFISPVYnDAGDLIYFFASQLDISRRKDAEEAL 146
Cdd:TIGR00229  84 KDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
 
Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
1-534 0e+00

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 1064.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   1 MSENKTRVDNAATGDIQHQGKDIFFAAVETTRMPMIVTDPNRPDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDP 80
Cdd:PRK13557   9 PHGRAPSVDESAAGDVSDHRSDIFFAAVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  81 AVVQSIRDAIAQRNDISAEIINYRKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRRKDAEEALRQAQKMEALGQLTG 160
Cdd:PRK13557  89 ATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQAQKMEALGQLTG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 161 GIAHDFNNLLQVMGGYIDLIGSAAEKPVIDVQRVQRSVYHAKSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEP 240
Cdd:PRK13557 169 GIAHDFNNLLQVMSGYLDVIQAALSHPDADRGRMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVSGMGE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 241 LIERTFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINARDALIGRENpkVFIETRNLLVDELANMSYDGLLPGRYVS 320
Cdd:PRK13557 249 LAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGR--VTIRTRNVEIEDEDLAMYHGLPPGRYVS 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 321 IAVTDNGIGMPASIRDRVMDPFFTTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEAGLTNTESPQ 400
Cdd:PRK13557 327 IAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEPK 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 401 ASDRRLGSSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMYDLLFTDLIMPGGMNGVMLAREVRRR 480
Cdd:PRK13557 407 ARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPGGMNGVMLAREARRR 486
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494453306 481 YPKVKVLLTTGYAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVLDGPNGIA 534
Cdd:PRK13557 487 QPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLDGPTGVG 540
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
21-391 2.52e-84

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 265.56  E-value: 2.52e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  21 KDIFFAAVETTRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDpaVVQSIRDAIAQRNDISA-E 99
Cdd:COG3852    6 EELLRAILDSLPDAVIVLDA---DGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP--LRELLERALAEGQPVTErE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 100 IINYRKDGSSFWNALFISPVYNDAGDlIYFFASQLDISRRKDAEEALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDL 179
Cdd:COG3852   81 VTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 180 IGSAAEKPvidvqRVQRSVYHAKSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIERTFGPEVAIETDLEPA 259
Cdd:COG3852  160 LERELPDD-----ELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 260 LKNCRIDPTQAEVALLNIFINARDALigRENPKVFIETRNLLVDELAnmsydGLLPGRYVSIAVTDNGIGMPASIRDRVM 339
Cdd:COG3852  235 LPEVLGDPDQLIQVLLNLVRNAAEAM--PEGGTITIRTRVERQVTLG-----GLRPRLYVRIEVIDNGPGIPEEILDRIF 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 494453306 340 DPFFTTKEegKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEA 391
Cdd:COG3852  308 EPFFTTKE--KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQA 357
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
133-388 5.31e-79

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 252.03  E-value: 5.31e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 133 QLDISRRKDAEEALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSAAEKPvIDVQRVQRSVYHAKSAVERASTLT 212
Cdd:COG4191  120 ERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILGNAELLRRRLEDE-PDPEELREALERILEGAERAAEIV 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 213 KQLLAFARKQKLQGRVLNLNGLVSIVEPLIERTFGP-EVAIETDLEPALKNCRIDPTQAEVALLNIFINARDALIGRENP 291
Cdd:COG4191  199 RSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKArGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEGEGG 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 292 KVFIETRnllvdelanmsydglLPGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEGKGSGLGLSMVYGFAKQSGGAAR 371
Cdd:COG4191  279 RITISTR---------------REGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGKGTGLGLSISYGIVEKHGGRIE 343
                        250
                 ....*....|....*..
gi 494453306 372 IYTEEGVGTTLRLYFPV 388
Cdd:COG4191  344 VESEPGGGTTFTITLPL 360
PRK13559 PRK13559
hypothetical protein; Provisional
23-208 4.93e-60

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 202.36  E-value: 4.93e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  23 IFFAAVETTRMPMIVTDPNRPDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIIN 102
Cdd:PRK13559  44 LFEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLN 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 103 YRKDGSSFWNALFISPVYNDAGDLIYFFASQLDIS--RRKDAEEALRQAQKMEalgqltggIAHDFNNLLQVMGGYIDLI 180
Cdd:PRK13559 124 YRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTdiRAVRALEAHERRLARE--------VDHRSKNVFAVVDSIVRLT 195
                        170       180
                 ....*....|....*....|....*...
gi 494453306 181 GSAAekpviDVQRVQRSVYHAKSAVERA 208
Cdd:PRK13559 196 GRAD-----DPSLYAAAIQERVQALARA 218
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
270-387 3.11e-59

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: 191.82  E-value: 3.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 270 AEVALLNIFINARDALIgrENPKVFIETRNLLVDELANMSYDGLLPGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEG 349
Cdd:cd16919    1 LELAILNLAVNARDAMP--EGGRLTIETSNQRVDADYALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVG 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494453306 350 KGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16919   79 KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
28-392 4.22e-53

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: 185.55  E-value: 4.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  28 VETTRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGtncRFLQGPDTDPAVVQSIRDAIAQRNDisaEIINYRKDG 107
Cdd:COG5000   96 LENLPAGVIVLDA---DGRITLANPAAERLLGIPLEELIG---KPLEELLPELDLAELLREALERGWQ---EEIELTRDG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 108 SSFWNaLFISPVYNDaGDLIYFfasqLDISRrkdaeeaLRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSA-AEK 186
Cdd:COG5000  167 RRTLL-VRASPLRDD-GYVIVF----DDITE-------LLRAERLAAWGELARRIAHEIKNPLTPIQLSAERLRRKlADK 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 187 PVIDVQRVQRSVYHAKSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIERTF-GPEVAIETDLEPALKNCRI 265
Cdd:COG5000  234 LEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVDLNELLREVLALYEPALkEKDIRLELDLDPDLPEVLA 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 266 DPTQAEVALLNIFINARDALigRENPKVFIETRnllvdelanmsydglLPGRYVSIAVTDNGIGMPASIRDRVMDPFFTT 345
Cdd:COG5000  314 DRDQLEQVLINLLKNAIEAI--EEGGEIEVSTR---------------REDGRVRIEVSDNGPGIPEEVLERIFEPFFTT 376
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 494453306 346 KEegKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEAG 392
Cdd:COG5000  377 KP--KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEA 421
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
47-388 1.34e-43

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: 161.44  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  47 IIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINYRKDGSSFWNALFISPVYNDAGDL 126
Cdd:COG5805  179 ILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSV 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 127 IYFFASQLDISRRKDAEEALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSAAE--KPVIDVQRvqrsvyhakSA 204
Cdd:COG5805  259 KGILVILRDITEKKEAEELMARSEKLSIAGQLAAGIAHEIRNPLTSIKGFLQLLQPGIEdkEEYFDIML---------SE 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 205 VERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIErtfgPE-----VAIETDLEPALKNCRIDPTQAEVALLNIFI 279
Cdd:COG5805  330 LDRIESIISEFLALAKPQAVNKEKENINELIQDVVTLLE----TEailhnIQIRLELLDEDPFIYCDENQIKQVFINLIK 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 280 NARDALigrENP-KVFIETRnllvdelanmsydglLPGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEegKGSGLGLSM 358
Cdd:COG5805  406 NAIEAM---PNGgTITIHTE---------------EEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKE--KGTGLGLMV 465
                        330       340       350
                 ....*....|....*....|....*....|
gi 494453306 359 VYGFAKQSGGAARIYTEEGVGTTLRLYFPV 388
Cdd:COG5805  466 SYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
412-514 8.82e-42

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: 145.18  E-value: 8.82e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMYDLLFTDLIMPGGMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPGGMNGSQLAEEARRRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|...
gi 494453306 492 YAESSIErTDIGGSEFDVVSKPC 514
Cdd:cd18161   81 YAENAIE-GGDLAPGVDVLSKPF 102
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
138-424 1.75e-41

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 159.46  E-value: 1.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 138 RRKDAE-----EALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLigsaAEKPVIDVQRVQRSVYHAKSAVERASTLT 212
Cdd:PRK13837 428 RRLETErdaleRRLEHARRLEAVGTLASGIAHNFNNILGAILGYAEM----ALNKLARHSRAARYIDEIISAGARARLII 503
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 213 KQLLAFARKQKLQGRVLNLNGLVSIVEPLIERTFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINARDALIGRENPK 292
Cdd:PRK13837 504 DQILAFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGRVD 583
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 293 VFIETRNLL-VDELANMSydgLLPGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKeeGKGSGLGLSMVYGFAKQSGGAAR 371
Cdd:PRK13837 584 ISLSRAKLRaPKVLSHGV---LPPGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTR--AGGTGLGLATVHGIVSAHAGYID 658
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494453306 372 IYTEEGVGTTLRLYFPVDEAGLTNTESPQASDRR-LGSSERILIVEdrPDVAEL 424
Cdd:PRK13837 659 VQSTVGRGTRFDVYLPPSSKVPVAPQAFFGPGPLpRGRGETVLLVE--PDDATL 710
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
24-389 8.76e-41

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: 153.59  E-value: 8.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  24 FFAAVETTRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINY 103
Cdd:COG5809  143 FRLIFNHSPDGIIVTDL---DGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFW 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 104 RKDGSSFWNALFISPV-YNDAGDLIYFFASqlDISRRKDAEEALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIgs 182
Cdd:COG5809  220 TKDGRWRLLEASGAPIkKNGEVDGIVIIFR--DITERKKLEELLRKSEKLSVVGELAAGIAHEIRNPLTSLKGFIQLL-- 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 183 aaeKPVIDVQrvQRSVYHA-KSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIErtfgPE-----VAIETDL 256
Cdd:COG5809  296 ---KDTIDEE--QKTYLDImLSELDRIESIISEFLVLAKPQAIKYEPKDLNTLIEEVIPLLQ----PQallknVQIELEL 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 257 E---PALKnCriDPTQAEVALLNIFINARDALigRENPKVFIETRnllvdelanmsydgLLPGRYVSIAVTDNGIGMPAS 333
Cdd:COG5809  367 EddiPDIL-G--DENQLKQVFINLLKNAIEAM--PEGGNITIETK--------------AEDDDKVVISVTDEGCGIPEE 427
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494453306 334 IRDRVMDPFFTTKEegKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVD 389
Cdd:COG5809  428 RLKKLGEPFYTTKE--KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIK 481
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
80-388 2.92e-40

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 148.52  E-value: 2.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  80 PAVVQSIRDAIAQRNDISAEIINYRKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRRKDAEEALRQAQkmEALGQLT 159
Cdd:COG0642   37 LLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEAN--EAKSRFL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 160 GGIAHDFNNLLQVMGGYIDLIGSAAEkpvidvQRVQRSVYHAKSAVERASTLTKQLLAFAR----KQKLQGRVLNLNGLV 235
Cdd:COG0642  115 ANVSHELRTPLTAIRGYLELLLEELD------EEQREYLETILRSADRLLRLINDLLDLSRleagKLELEPEPVDLAELL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 236 -SIVEPLIERTFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINARDAliGRENPKVFIETRnllvdelanmsydglL 314
Cdd:COG0642  189 eEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKY--TPEGGTVTVSVR---------------R 251
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494453306 315 PGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKE--EGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPV 388
Cdd:COG0642  252 EGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPsrRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPL 327
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
47-389 4.05e-39

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: 146.08  E-value: 4.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  47 IIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPavvQSIRDAIAQRNDISAeiinYRKDGssfWNALFISPVYNDAGDL 126
Cdd:COG5807   49 ILECNDFAEDLYGLSQNEYIGKTFVEEKCILKDE---QLYNKEAFDRIEISY----LTKNG---EFDEIIYPIYYKDGVI 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 127 IYFFASQLDISRRKDAEEALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSAAEKPVIDVqrvqrsvYHAK--SA 204
Cdd:COG5807  119 LGLITVYRDITKRKEAEDKLLRSEKLSVAGELAAGIAHEIRNPLTSIKGFLQLLQESREDSEREE-------YFNIiiSE 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 205 VERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIERTFG-PEVAIETDLEPALKNCRIDPTQAEVALLNIFINARD 283
Cdd:COG5807  192 IDRINTIITELLVLSKPKKFNFKKLNLNDVLEDVIALLSTEAIlKNISIKYDLADDEPVINGDKNQLKQVFINLIKNAIE 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 284 ALigRENPKVFIETRNLlvdelanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEgkGSGLGLSMVYGFA 363
Cdd:COG5807  272 AM--ETGGNITIKTYVE---------------GDFVVISVKDEGIGIPEEVLEKIGEPFFTTKEE--GTGLGLSICKKII 332
                        330       340
                 ....*....|....*....|....*.
gi 494453306 364 KQSGGAARIYTEEGVGTTLRLYFPVD 389
Cdd:COG5807  333 EEHNGTIEVESKPGKGTTFTIYLPLY 358
PRK13558 PRK13558
bacterio-opsin activator; Provisional
37-155 2.50e-37

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 146.14  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  37 VTDPNRPDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINYRKDGSSFWNALFI 116
Cdd:PRK13558 163 IADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDI 242
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494453306 117 SPVYNDAGDLIYFFASQLDISRRKDAEEAL-RQAQKMEAL 155
Cdd:PRK13558 243 APIRDEDGTVTHYVGFQTDVTERKEAELALqRERRKLQRL 282
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
47-390 1.66e-36

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 143.18  E-value: 1.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  47 IIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVqsIRDAIAQRNDISAEIINYRKDGSSFWNALFISPVYNDAGDL 126
Cdd:PRK11360 284 ITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASP--LLDTLEHGTEHVDLEISFPGRDRTIELSVSTSLLHNTHGEM 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 127 IYFFASQLDISRRKDAEEALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSAAEKPVidvqrVQRSVYHAKSAVE 206
Cdd:PRK11360 362 IGALVIFSDLTERKRLQRRVARQERLAALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPP-----SQEYLSVVLREVD 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 207 RASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIERTFGPE-VAIETDLEPALKNCRIDPTQAEVALLNIFINARDAL 285
Cdd:PRK11360 437 RLNKVIDQLLEFSRPRESQWQPVSLNALVEEVLQLFQTAGVQArVDFETELDNELPPIWADPELLKQVLLNILINAVQAI 516
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 286 igRENPKVFIETRNLLVDELAnmsydgllpgryvsIAVTDNGIGMPASIRDRVMDPFFTTKEegKGSGLGLSMVYGFAKQ 365
Cdd:PRK11360 517 --SARGKIRIRTWQYSDGQVA--------------VSIEDNGCGIDPELLKKIFDPFFTTKA--KGTGLGLALSQRIINA 578
                        330       340
                 ....*....|....*....|....*
gi 494453306 366 SGGAARIYTEEGVGTTLRLYFPVDE 390
Cdd:PRK11360 579 HGGDIEVESEPGVGTTFTLYLPINP 603
PAS COG2202
PAS domain [Signal transduction mechanisms];
24-176 1.73e-31

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 122.44  E-value: 1.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  24 FFAAVETTRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINY 103
Cdd:COG2202   13 LRALVESSPDAIIITDL---DGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 104 RKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRRKDAEEALRQA-QKMEALGQLTG---------GIAHDFNNLLQVM 173
Cdd:COG2202   90 RKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESeERLRLLVENAPdgifvldldGRILYVNPAAEEL 169

                 ...
gi 494453306 174 GGY 176
Cdd:COG2202  170 LGY 172
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
143-391 2.08e-31

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 121.55  E-value: 2.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 143 EEALRQAQKMEAL-GQLTGGIAHDFNNLLQVMGGYIDLIgsaAEKPVIDVQRVQRSVYHAKSAVERASTLTKQLLAFAR- 220
Cdd:COG2205    3 EEALEELEELERLkSEFLANVSHELRTPLTSILGAAELL---LDEEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 221 ---KQKLQGRVLNLNGLV-SIVEPLIERTFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINARDAliGRENPKVFIE 296
Cdd:COG2205   80 esgKLSLELEPVDLAELLeEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKY--SPPGGTITIS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 297 TRNLlvdelanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEGK--GSGLGLSMVYGFAKQSGGAARIYT 374
Cdd:COG2205  158 ARRE---------------GDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGegGTGLGLAIVKRIVEAHGGTIWVES 222
                        250
                 ....*....|....*..
gi 494453306 375 EEGVGTTLRLYFPVDEA 391
Cdd:COG2205  223 EPGGGTTFTVTLPLAES 239
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
23-391 1.85e-26

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 111.18  E-value: 1.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  23 IFFAAVETTRMPMIVTDPNRPDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIIN 102
Cdd:COG5002   42 LLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 103 YRKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRRKDAEEALRQaqkmealgqLTGGIAHDFNNLLQVMGGYIDLIgs 182
Cdd:COG5002  122 SELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRRE---------FVANVSHELRTPLTSIRGYLELL-- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 183 aAEKPVIDVQRVQRSVYHAKSAVERASTLTKQLLAFAR----KQKLQGRVLNLNGLV-SIVEPLIERTFGPEVAIETDLE 257
Cdd:COG5002  191 -LDGAADDPEERREYLEIILEEAERLSRLVNDLLDLSRlesgELKLEKEPVDLAELLeEVVEELRPLAEEKGIELELDLP 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 258 PALKNCRIDPTQAEVALLNIFINARDAliGRENPKVFIETRNLlvdelanmsydgllpGRYVSIAVTDNGIGMPASIRDR 337
Cdd:COG5002  270 EDPLLVLGDPDRLEQVLTNLLDNAIKY--TPEGGTITVSLREE---------------DDQVRISVRDTGIGIPEEDLPR 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494453306 338 VMDPFFTTKE----EGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEA 391
Cdd:COG5002  333 IFERFYRVDKsrsrETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
407-530 3.91e-26

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: 103.01  E-value: 3.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 407 GSSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRR--YPKV 484
Cdd:COG0784    3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP-PDLILLDINMP-GMDGLELLRRIRALprLPDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 494453306 485 KVLLTTGYAESSIERT--DIGGSEFdvVSKPCMPHDLARKVRQVLDGP 530
Cdd:COG0784   81 PIIALTAYADEEDRERalEAGADDY--LTKPVDPEELLEALRRLLARA 126
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
123-389 5.90e-25

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 107.56  E-value: 5.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 123 AGDLIYFFASQLDISRRKdAEEALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSAAEKPVIDVQRVQRSVyhak 202
Cdd:PRK10364 206 ASLLAFFWYRRYLRSRQL-LQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMA---- 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 203 SAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIER-TFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINA 281
Cdd:PRK10364 281 KEADRLNRVVSELLELVKPTHLALQAVDLNDLINHSLQLVSQdANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNA 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 282 RDAlIGRENPKVFIETRNllvdelanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKeeGKGSGLGLSMVYG 361
Cdd:PRK10364 361 IQA-IGQHGVISVTASES----------------GAGVKISVTDSGKGIAADQLEAIFTPYFTTK--AEGTGLGLAVVHN 421
                        250       260
                 ....*....|....*....|....*...
gi 494453306 362 FAKQSGGAARIYTEEGVGTTLRLYFPVD 389
Cdd:PRK10364 422 IVEQHGGTIQVASQEGKGATFTLWLPVN 449
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
146-388 1.51e-22

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: 99.94  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 146 LRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGsaaEKPVIDVQRvQRSVYHAKSAVERASTLTKQLLAFARKQKLQ 225
Cdd:COG5806  192 LQRAEKLEVVSELAASIAHEVRNPLTVVRGFIQLLQ---EPELSDEKR-KQYIRIALEELDRAEAIITDYLTFAKPQPEK 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 226 GRVLNLNGLVSIVEPLIeRTFGP--EVAIETDLEPALKNCrIDPTQAEVALLNIFINArdaligrenpkvfIETrnllvd 303
Cdd:COG5806  268 LEKIDVSEELEHVIDVL-SPYANmnNVEIQTELEPGLYIE-GDRQKLQQCLINIIKNG-------------IEA------ 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 304 elanMSYDGLL------PGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEegKGSGLGLSMVYGFAKQSGGAARIYTEEG 377
Cdd:COG5806  327 ----MPNGGTLtidvsiDKNKVIISIKDTGVGMTKEQLERLGEPYFSTKE--KGTGLGTMVSYRIIEAMNGTIRVESEVG 400
                        250
                 ....*....|.
gi 494453306 378 VGTTLRLYFPV 388
Cdd:COG5806  401 KGTTFTITLPL 411
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
408-528 2.14e-21

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: 96.57  E-value: 2.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 408 SSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVL 487
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP-PDLVLLDLRMP-GMDGLELLRELRALDPDLPVI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494453306 488 LTTGYAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVLD 528
Cdd:COG2204   79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE 119
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
127-391 2.32e-21

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: 96.74  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 127 IYFFASQLDISRRKDAEEALRQA---QKMEALGQLTGGIAHDFNNLLQVMGGYIDLIgSAAEKPVIDvqrvQRSVYHAKS 203
Cdd:COG5808  210 IIFLLLQYNLLKRKTLLERVIQEintQKLELIGTFAASTAHEIRNPLTSIKGFIQLL-QEKYPELED----QKYFDIIQE 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 204 AVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIERT---FGPEVAIETDLEPALKNCRIDptQAEVALLNIFIN 280
Cdd:COG5808  285 EIQRINQIVSEFLVLGKPTAKKLELDDLNELIEEILSIIDSEanlKNIRVEKQSLDEPLHIKCDKD--RIKQVLLNLIKN 362
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 281 ARDALigRENPKVFIETRNLlvdelanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEegKGSGLGLSMVY 360
Cdd:COG5808  363 AIEAM--KEGGKLTISIEND---------------DEKAVIEVIDNGEGIPEDIIDEIFEPFVTTKE--GGTGLGLSVCK 423
                        250       260       270
                 ....*....|....*....|....*....|.
gi 494453306 361 GFAKQSGGAARIYTEEGVGTTLRLYFPVDEA 391
Cdd:COG5808  424 RIVEMHGGEIDIESEEGKGTTFTIRLPLKKE 454
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
267-388 2.39e-20

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: 85.94  E-value: 2.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 267 PTQAEVALLNIFINARDALIGREnpKVFIETrNLLVDELAnmsydgllpgryvsIAVTDNGIGMPASIRDRVMDPFFTTK 346
Cdd:cd16943    1 PSQLNQVLLNLLVNAAQAMEGRG--RITIRT-WAHVDQVL--------------IEVEDTGSGIDPEILGRIFDPFFTTK 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494453306 347 EEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPV 388
Cdd:cd16943   64 PVGEGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
274-384 3.27e-19

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: 82.89  E-value: 3.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 274 LLNIFINARDALIGRENPKVFIETRnllvdelanmsydgLLPGRYVsIAVTDNGIGMPASIRDRVMDPFFTTKEEGKGSG 353
Cdd:cd16976    5 LMNLLQNALDAMGKVENPRIRIAAR--------------RLGGRLV-LVVRDNGPGIAEEHLSRVFDPFFTTKPVGKGTG 69
                         90       100       110
                 ....*....|....*....|....*....|.
gi 494453306 354 LGLSMVYGFAKQSGGAARIYTEEGVGTTLRL 384
Cdd:cd16976   70 LGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
413-513 8.84e-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: 81.50  E-value: 8.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 413 LIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLLTTGY 492
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREER-PDLVLLDLMMPG-MDGLELLRKLRELPPDIPVIVLTAK 78
                         90       100
                 ....*....|....*....|.
gi 494453306 493 AESSIERTDIGGSEFDVVSKP 513
Cdd:cd00156   79 ADEEDAVRALELGADDYLVKP 99
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
411-495 9.47e-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: 81.88  E-value: 9.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESED-PDLVILDIKMP-GMDGLETLRKIREKKPDLPVIICT 79

                 ....*
gi 494453306 491 GYAES 495
Cdd:cd17554   80 AYSEY 84
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
47-391 1.28e-18

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 88.69  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  47 IIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINYRKDGSSFWNALFISPVYNDAGDL 126
Cdd:COG4251  164 LALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLIL 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 127 IYFFASQLDISRR-----KDAEEALRQA-----QKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSAAeKPVIDvQRVQR 196
Cdd:COG4251  244 LLLLLILVLELLElrlelEELEEELEERtaeleRSNEELEQFAYVASHDLREPLRKISGFSQLLEEDY-GDKLD-EEGRE 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 197 SVYHAKSAVERASTLTKQLLAFAR--KQKLQGRVLNLNGLV-SIVEPLIERTFGPEVAIETDLEPALkncRIDPTQAEVA 273
Cdd:COG4251  322 YLERIRDAAERMQALIDDLLAYSRvgRQELEFEPVDLNELLeEVLEDLEPRIEERGAEIEVGPLPTV---RGDPTLLRQV 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 274 LLNIFINARDALIGRENPKVFIETRnllvdelanmsydglLPGRYVSIAVTDNGIGMPASIRDRVMDPFFT--TKEEGKG 351
Cdd:COG4251  399 FQNLISNAIKYSRPGEPPRIEIGAE---------------REGGEWVFSVRDNGIGIDPEYAEKIFEIFQRlhSRDEYEG 463
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 494453306 352 SGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEA 391
Cdd:COG4251  464 TGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAPA 503
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
133-372 1.45e-18

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 88.98  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 133 QLDISRRKDAEEALRQAQ-------KMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSAAEKPviDVQRVQRSVYHAKSAV 205
Cdd:COG4192  404 ETEIEERKRIEKNLRQTQdeliqaaKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQE--NYAQLPTSLDKIEGLI 481
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 206 ERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVEPLIERTFGPEVAIETDLEPALKNcrIDPTQAEVALLNIFINARDAl 285
Cdd:COG4192  482 ERMDKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIPDDLMVQ--GDQVLLEQVLVNLLVNALDA- 558
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 286 igrenpkvfietrnllVDELANMSYDGLLPGRYVSIAVTDNGIGMPasIRDRVMDPFFTTKEegKGSGLGLSMVYGFAKQ 365
Cdd:COG4192  559 ----------------VATQPQISVDLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTTKE--VGLGLGLSICRSIMQQ 618

                 ....*..
gi 494453306 366 SGGAARI 372
Cdd:COG4192  619 FGGDLYL 625
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
44-137 3.34e-18

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: 79.43  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   44 DNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGpdtDPAVVQSIRDAIAQ-RNDISAEIINYRKDGSSFWNALFISPVYND 122
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREgKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
                          90
                  ....*....|....*
gi 494453306  123 AGDLIYFFASQLDIS 137
Cdd:pfam13426  78 GGELVGIIAILRDIT 92
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
265-388 3.44e-18

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 80.00  E-value: 3.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   265 IDPTQAEVALLNIFINARDAliGRENPKVFIETRNLlvdelanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPFFT 344
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKY--TPEGGRITVTLERD---------------GDHVEITVEDNGPGIPPEDLEKIFEPFFR 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 494453306   345 TKE---EGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPV 388
Cdd:smart00387  64 TDKrsrKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPL 110
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
411-513 4.90e-18

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: 79.43  E-value: 4.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDY-GYvsEIVL---NAREALKKFESgNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKV 486
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEaGF--EVVGeaeNGEEALELLEE-HKPDLVITDINMPG-MDGLELLEAIRELDPDTKI 76
                         90       100
                 ....*....|....*....|....*..
gi 494453306 487 LLTTGYAESSIERTDIGGSEFDVVSKP 513
Cdd:COG4753   77 IILSGYSDFEYAQEAIKLGADDYLLKP 103
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
411-527 5.64e-18

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: 82.31  E-value: 5.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:COG0745    3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEE-ERPDLILLDLMLP-GMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494453306 491 GYAESSIERT--DIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:COG0745   81 ARDDEEDRVRglEAGAD--DYLTKPFDPEELLARIRALL 117
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
411-528 1.46e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 79.24  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEI--VLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLL 488
Cdd:COG4565    5 RVLIVEDDPMVAELLRRYLERLPGFEVVgvASSGEEALALLAEHR-PDLILLDIYLP-DGDGLELLRELRARGPDVDVIV 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494453306 489 TTGYAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVLD 528
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
26-146 1.60e-17

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: 78.87  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   26 AAVETTRMPMIVTDPNrpdNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQR-NDISAEIINYR 104
Cdd:TIGR00229   7 AIFESSPDAIIVIDLE---GNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEpEPVSEERRVRR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 494453306  105 KDGSSFWNALFISPVYnDAGDLIYFFASQLDISRRKDAEEAL 146
Cdd:TIGR00229  84 KDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
266-390 2.70e-17

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: 77.41  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  266 DPTQAEVALLNIFINARDALIGRENPKVFIEtrnllvdelanmsydgllPGRYVSIAVTDNGIGMPASIRDRVMDPFFTT 345
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGEITVTLS------------------EGGELTLTVEDNGIGIPPEDLPRIFEPFSTA 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 494453306  346 -KEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDE 390
Cdd:pfam02518  64 dKRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
26-391 3.10e-17

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 83.74  E-value: 3.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  26 AAVETTRMPMIVTDPNRPdnpIIFSNRAFLEMTGYTA--EEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEiiny 103
Cdd:COG3290   88 AVLESIREGVIAVDRDGR---ITLINDAARRLLGLDAigRPIDEVLAEVLETGERDEEILLNGRVLVVNRVPIRDD---- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 104 rkdgssfwnalfispvyndaGDLIYFFASQLDISRRKDAEEALRQAQKM-EALGQLTggiaHDFNNLLQVMGGYIDLIgs 182
Cdd:COG3290  161 --------------------GRVVGAVATFRDRTELERLEEELEGVKELaEALRAQR----HDFRNHLHTISGLLQLG-- 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 183 aaekpvidvqrvqrsvyHAKSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSIVeplIERTFGPEVAIETDLEPALKN 262
Cdd:COG3290  215 -----------------EYDEALEYIDEISEELQELIDSLLSRIGNPVLAALLLGK---AARARERGIDLTIDIDSDLPD 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 263 CRIDPTQAEVALLNIFINARDALIGRENPKVFIEtrnllVDelanMSYDGllpgRYVSIAVTDNGIGMPASIRDRVMDPF 342
Cdd:COG3290  275 LPLSDTDLVTILGNLLDNAIEAVEKLPEEERRVE-----LS----IRDDG----DELVIEVEDSGPGIPEELLEKIFERG 341
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 494453306 343 FTTKeEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEA 391
Cdd:COG3290  342 FSTK-LGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
405-528 3.98e-17

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 80.59  E-value: 3.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 405 RLGSSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRYP-- 482
Cdd:COG3437    2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLE-APPDLILLDVRMP-GMDGFELLRLLRADPStr 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494453306 483 KVKVLLTTGYAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVLD 528
Cdd:COG3437   80 DIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
273-386 1.39e-16

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


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 75.33  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 273 ALLNIFINARDAliGRENPKVFIETRNLlvdelanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPFFTTK--EEGK 350
Cdd:cd00075    4 VLSNLLDNALKY--SPPGGTIEISLRQE---------------GDGVVLEVEDNGPGIPEEDLERIFERFYRGDksREGG 66
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494453306 351 GSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYF 386
Cdd:cd00075   67 GTGLGLAIVRRIVEAHGGRITVESEPGGGTTFTVTL 102
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
412-524 1.73e-16

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: 75.27  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER-PDLILLDINMP-GMDGLELLKRIRRRDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 494453306  492 YAESS--IERTDIGGseFDVVSKPCMPHDLARKVR 524
Cdd:pfam00072  79 HGDEDdaVEALEAGA--DDFLSKPFDPDELLAAIR 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
411-523 2.44e-16

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: 76.87  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRR--RYPKVKVLL 488
Cdd:COG3706    3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQE-HRPDLILLDLEMP-DMDGLELCRRLRAdpRTADIPIIF 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494453306 489 TTGYAESSIERT--DIGGSefDVVSKPCMPHDLARKV 523
Cdd:COG3706   81 LTALDDEEDRARalEAGAD--DYLTKPFDPEELLARV 115
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
412-523 7.28e-15

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 70.56  E-value: 7.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRYP--KVKVLLT 489
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQR-FRPDVILSDIGMP-GMDGYELARRLRELPWlaNTPAIAL 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494453306 490 TGYAESS-IERTDIGGseFDV-VSKPCMPHDLARKV 523
Cdd:cd17580   79 TGYGQPEdRERALEAG--FDAhLVKPVDPDELIELI 112
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
411-513 1.29e-14

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: 69.84  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMP-EMDGIELAREARKIDPDVKILFIS 79
                         90       100
                 ....*....|....*....|...
gi 494453306 491 GYAESSIERTDIGGSEFDVVSKP 513
Cdd:cd18160   80 GGAAAAPELLSDAVGDNATLKKP 102
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
323-513 1.32e-14

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 76.90  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 323 VTDNGIGMPASIRDRVMDPFFTTKE--EGK---GSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDeAGLTNTE 397
Cdd:PRK11091 435 VEDSGIGIPEDELDKIFAMYYQVKDshGGKpatGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAP-AVAEEVE 513
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 398 SPQASDRRLGSSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREV 477
Cdd:PRK11091 514 DAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDE-YDLVLLDIQLP-DMTGLDIAREL 591
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 494453306 478 RRRYPKVK----VLLTTGYAESSIERTDIGGSefDVVSKP 513
Cdd:PRK11091 592 RERYPREDlpplVALTANVLKDKKEYLDAGMD--DVLSKP 629
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
412-513 7.49e-14

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: 67.88  E-value: 7.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVR---RRYPKVKVLL 488
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEP-FDLVLMDLQMP-VMDGLEATRRIReleGGGRRTPIIA 78
                         90       100
                 ....*....|....*....|....*..
gi 494453306 489 TTGYA-ESSIER-TDIGGSefDVVSKP 513
Cdd:cd17546   79 LTANAlEEDREKcLEAGMD--DYLSKP 103
glnL PRK11073
nitrogen regulation protein NR(II);
106-388 7.88e-14

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 72.81  E-value: 7.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 106 DGSSFWNALFISPVYNDagdLIYFFASQLDiSRRKDAEEALRQAQKMEAlGQLTGGIAHDFNNLLQVMGGYIDLIGSAAE 185
Cdd:PRK11073  86 DGRSHILSLTAQRLPEG---MILLEMAPMD-NQRRLSQEQLQHAQQVAA-RDLVRGLAHEIKNPLGGLRGAAQLLSKALP 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 186 KP-------VIDVQrvqrsvyhaksaVERASTLTKQLLAfarKQKLQGRVL-NLNGLVSIVEPLIERTFGPEVAIETDLE 257
Cdd:PRK11073 161 DPalteytkVIIEQ------------ADRLRNLVDRLLG---PQRPGTHVTeSIHKVAERVVQLVSLELPDNVRLIRDYD 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 258 PALKNCRIDPTQAEVALLNIFINARDALiGRENPKVFIETRNLLVDELANMSYDglLPGRyvsIAVTDNGIGMPASIRDR 337
Cdd:PRK11073 226 PSLPELAHDPDQIEQVLLNIVRNALQAL-GPEGGTITLRTRTAFQLTLHGERYR--LAAR---IDIEDNGPGIPPHLQDT 299
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 494453306 338 VMDPFFTTKEegKGSGLGLSMVYGFAKQSGGaaRIYTEEGVG-TTLRLYFPV 388
Cdd:PRK11073 300 LFYPMVSGRE--GGTGLGLSIARNLIDQHSG--KIEFTSWPGhTEFSVYLPI 347
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
412-494 9.61e-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: 67.75  E-value: 9.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAE-LAKMV-LDDYGYvsEIVL---NAREALKKFESgNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKV 486
Cdd:cd17536    1 VLIVDDEPLIREgLKKLIdWEELGF--EVVGeaeNGEEALELIEE-HKPDIVITDIRMPG-MDGLELIEKIRELYPDIKI 76

                 ....*...
gi 494453306 487 LLTTGYAE 494
Cdd:cd17536   77 IILSGYDD 84
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
321-534 1.68e-13

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 73.40  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 321 IAVTDNGIGMPASIRDRVMDPFFTTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEAGLTNTESPQ 400
Cdd:PRK11466 595 VEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVN 674
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 401 ASDRRLGssERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMYDLLFTDLIMPgGMNGVMLAREVRRR 480
Cdd:PRK11466 675 QAVRLDG--LRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPFAAALVDFDLP-DYDGITLARQLAQQ 751
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494453306 481 YPKVKVLLTTGYAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVLDGPNGIA 534
Cdd:PRK11466 752 YPSLVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQVNND 805
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
266-387 2.04e-13

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: 66.41  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 266 DPTQAEVALLNIFINARDALIGRENPKvfIETRnllVDELANMSYDgllpgryVSIAVTDNGIGMPASIRDRVMDPFFTT 345
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEGRPSDV--GEVR---IRVEADQDGR-------IVLIVCDNGKGFPREMRHRATEPYVTT 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494453306 346 KEegKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16944   69 RP--KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
412-513 6.56e-13

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: 6.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKE-RRPDLVLLDIWLP-DMDGLELLKEIKEKYPDLPVIMISG 78
                         90       100
                 ....*....|....*....|....
gi 494453306 492 YA--ESSIERTDIGGseFDVVSKP 513
Cdd:cd17550   79 HGtiETAVKATKLGA--YDFIEKP 100
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
413-490 8.25e-13

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 64.35  E-value: 8.25e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494453306 413 LIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELARE-EQPDLIILDVMLP-GMDGFEVCRRLREKGSDIPIIMLT 76
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
31-136 3.67e-12

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: 62.65  E-value: 3.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  31 TRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINYRKDGSSF 110
Cdd:cd00130    1 LPDGVIVLDL---DGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVI 77
                         90       100
                 ....*....|....*....|....*.
gi 494453306 111 WNALFISPVYNDAGDLIYFFASQLDI 136
Cdd:cd00130   78 WVLVSLTPIRDEGGEVIGLLGVVRDI 103
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
411-499 5.12e-12

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: 62.81  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGY-VSEIVLNAREALKKFESgNMYDLLFTDLIMPGGMNGVMLAREVRRRYPkVKVLLT 489
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYeVVGIADSGEEAIELAEE-NKPDLILMDINLKGDMDGIEAAREIREKFD-IPVIFL 79
                         90
                 ....*....|.
gi 494453306 490 TGYA-ESSIER 499
Cdd:cd17534   80 TAYSdEETLER 90
PAS COG2202
PAS domain [Signal transduction mechanisms];
26-146 5.47e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 66.20  E-value: 5.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  26 AAVETTRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDiSAEIINYRK 105
Cdd:COG2202  141 LLVENAPDGIFVLDL---DGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRE-SYELELRLK 216
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494453306 106 DGSSFWNALFISPVYNDAGD-LIYFFASQLDISRRKDAEEAL 146
Cdd:COG2202  217 DGDGRWVWVEASAVPLRDGGeVIGVLGIVRDITERKRAEEAL 258
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
273-387 1.14e-11

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: 61.65  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 273 ALLNIFINARDALiGRENPKVFIETRnllVDELANMSYDGL-LPGRyvsIAVTDNGIGMPASIRDRVMDPFFTTKEEgkG 351
Cdd:cd16918    4 VFLNLVRNAAQAL-AGSGGEIILRTR---TQRQVTLGHPRHrLALR---VSVIDNGPGIPPDLQDTIFYPMVSGREN--G 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494453306 352 SGLGLSMVYGFAKQSGGaaRIYTEEGVGTTL-RLYFP 387
Cdd:cd16918   75 TGLGLAIAQNIVSQHGG--VIECDSQPGHTVfSVSLP 109
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
411-528 1.90e-11

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: 61.27  E-value: 1.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMyDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPV-DVVISDQRMPG-MDGAELLKRVRERYPDTVRILLT 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494453306 491 GYAE-----SSIERTDIggseFDVVSKPCMPHDLARKVRQVLD 528
Cdd:cd17569   80 GYADldaaiEAINEGEI----YRFLTKPWDDEELKETIRQALE 118
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
412-527 6.81e-11

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: 59.45  E-value: 6.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVL---DDYGYVSEiVLNAREALKKFESGNmYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLL 488
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLesePDIEVVGE-AADGEEALALLRELR-PDVVLMDLSMPG-MDGIEALRRLRRRYPDLKVIV 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494453306 489 TTGYAESSIERT--DIGGSEFdvVSKPCMPHDLARKVRQVL 527
Cdd:cd17535   78 LTAHDDPEYVLRalKAGAAGY--LLKDSSPEELIEAIRAVA 116
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
411-527 7.39e-11

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: 59.31  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVrRRYPKVKVLLTT 490
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRH-TPPDLILLDLMLP-GTDGLTLCREI-RRFSDVPIIMVT 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494453306 491 GYAEsSIER---TDIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:cd19938   78 ARVE-EIDRllgLELGAD--DYICKPYSPREVVARVKAIL 114
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
47-129 1.08e-10

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: 58.12  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   47 IIFSNRAFLEMTGYTAEEILGTNCRFLQG--PDTDPAVVQSIRDAIAQRNDISAEIINYRKDGSSFWNALFISPVYNDAG 124
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLvhPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                  ....*
gi 494453306  125 DLIYF 129
Cdd:pfam08447  81 KPVRV 85
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
24-391 1.88e-10

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 63.00  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  24 FFAAVETTRMPMIVTDPNRPDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINY 103
Cdd:COG3920  166 ELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRR 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 104 RKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRRKDAEEALRQAQKMEALgqLTGGIAHDFNNLLQVMGGYIDLIGSA 183
Cdd:COG3920  246 RARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKEL--LLRELHHRVKNNLQVVSSLLRLQARR 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 184 AEKPVIDVqrvqrsvyHAKSAVERASTLTK--QLLAfarkQKLQGRVLNLNGLV-SIVEPLIERTFGPEVAIETDLEPal 260
Cdd:COG3920  324 ADDPEARE--------ALEESQNRIQALALvhELLY----QSEDWEGVDLRDYLrELLEPLRDSYGGRGIRIELDGPD-- 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 261 knCRIDPTQAeVAL---LN-IFINA-RDALIGRENPKVFIETRnllvdelanmsydglLPGRYVSIAVTDNGIGMPASIr 335
Cdd:COG3920  390 --VELPADAA-VPLgliLNeLVTNAlKHAFLSGEGGRIRVSWR---------------REDGRLRLTVSDNGVGLPEDV- 450
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494453306 336 drvmdpffttkEEGKGSGLGLSMVYGFAKQSGGAARIYTEEgvGTTLRLYFPVDEA 391
Cdd:COG3920  451 -----------DPPARKGLGLRLIRALVRQLGGTLELDRPE--GTRVRITFPLAEL 493
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
274-387 2.62e-10

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: 57.41  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 274 LLNIFINARDALIGrenpkVFIETRNLLVdelANMSYDGllpgRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEGKgsG 353
Cdd:cd16920    5 LINLVRNGIEAMSE-----GGCERRELTI---RTSPADD----RAVTISVKDTGPGIAEEVAGQLFDPFYTTKSEGL--G 70
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494453306 354 LGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16920   71 MGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
411-527 2.62e-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: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVsEIVL---NAREALKKFESgNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVL 487
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKYPDL-EVVGeasNGEEALELLEE-HKPDLVFLDIQMPG-LDGFELARQLRELDPPPPII 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494453306 488 LTTGYAESSIErtdigGSEFDVVS---KPCMPHDLARKVRQVL 527
Cdd:COG3279   80 FTTAYDEYALE-----AFEVNAVDyllKPIDEERLAKALEKAK 117
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
412-498 2.64e-10

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 57.45  E-value: 2.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTg 491
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNE-YDLIILDVMLP-GLDGLEVLRRLRAAGKQTPVLMLT- 77

                 ....*..
gi 494453306 492 yAESSIE 498
Cdd:cd19935   78 -ARDSVE 83
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
24-136 9.39e-10

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: 56.27  E-value: 9.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   24 FFAAVETTRMPMIVTDPNRPdnpIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINY 103
Cdd:pfam00989   3 LRAILESLPDGIFVVDEDGR---ILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSF 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 494453306  104 R-KDGSSFWNALFISPVYNDAGDLIYFFASQLDI 136
Cdd:pfam00989  80 RvPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
411-465 2.24e-09

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: 53.34  E-value: 2.24e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 494453306   411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMP 465
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEK-PDLILLDIMMP 55
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
412-527 2.45e-09

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: 55.02  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRyPKVK----VL 487
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAE-HRPTLVISDIVMP-EMDGYELCRKIKSD-PDLKdipvIL 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494453306 488 LTT-GYAESSIERTDIGGSEFdvVSKPCMPHDLARKVRQVL 527
Cdd:cd17598   78 LTTlSDPRDVIRGLECGADNF--ITKPYDEKYLLSRIKYIL 116
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
316-387 2.72e-09

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


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 54.60  E-value: 2.72e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494453306 316 GRYVSIAVTDNGIGMPASIRDRVMDPFFTTK---EEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16948   35 EQGVVLSIKDFGIGIPEEDLPRVFDKGFTGEngrNFQESTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
413-527 2.78e-09

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: 54.97  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 413 LIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRR--RYPKVKVLLTT 490
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKD-EKPDLIILDLMLP-GIDGLEVCRILRSdpKTSSIPIIMLT 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494453306 491 GYAEssiERTDIGGSEF---DVVSKPCMPHDLARKVRQVL 527
Cdd:cd19937   79 AKGE---EFDKVLGLELgadDYITKPFSPRELLARVKAVL 115
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
411-524 5.24e-09

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: 54.68  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSeIVLNAREALKKFEsGNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17596    2 TILVVDDEVRSLEALRRTLEEDFDVL-TAASAEEALAILE-EEWVQVILCDQRMPG-TTGVEFLKEVRERWPEVVRIIIS 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494453306 491 GYAESSiertDI-----GGSEFDVVSKPCMPHDLARKVR 524
Cdd:cd17596   79 GYTDSE----DIiaginEAGIYQYLTKPWHPDQLLLTVR 113
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
319-496 7.86e-09

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 58.59  E-value: 7.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  319 VSIAVTDNGIGMPASIRDRVMDPFFTTK--EEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVD-----EA 391
Cdd:PRK09959  865 IKMTIMDSGSGLSQEEQQQLFKRYSQTSagRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEisqqvAT 944
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  392 GLTNTESPQASDRRLGsserILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFeSGNMYDLLFTDLIMPgGMNGV 471
Cdd:PRK09959  945 VEAKAEQPITLPEKLS----ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKV-SMQHYDLLITDVNMP-NMDGF 1018
                         170       180
                  ....*....|....*....|....*
gi 494453306  472 MLAREVRRRYPKVKVLLTTGYAESS 496
Cdd:PRK09959 1019 ELTRKLREQNSSLPIWGLTANAQAN 1043
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
412-527 8.50e-09

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: 53.46  E-value: 8.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPGgMNGVMLAREVRRRyPKVKVLLTTG 491
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGS-PDLVVLDVMLPK-MNGLDVLKELRKT-SQVPVLMLTA 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494453306 492 YAESsIERtdIGGSEF---DVVSKPCMPHDLARKVRQVL 527
Cdd:cd17623   78 RGDD-IDR--ILGLELgadDYLPKPFNPRELVARIRAIL 113
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
15-148 8.80e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 58.24  E-value: 8.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  15 DIQHQGKDIFFAAVETTRMPMIVTDPNrpdNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIR----DAI 90
Cdd:PRK11359   5 DADNAADGIFFPALEQNMMGAVLINEN---DEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRhnreGGK 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494453306  91 AQRNDISAEIINYRKDGSSFWNALFISPVynDAGDLIYFFASQLDISRRKDAEEALRQ 148
Cdd:PRK11359  82 ARVEGMSRELQLEKKDGSKIWTRFALSKV--SAEGKVYYLALVRDASVEMAQKEQTRQ 137
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
276-387 1.31e-08

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 52.67  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 276 NIFINARDALIGRENPKVFIETrnLLVDElanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEGkGSGLG 355
Cdd:cd16915    7 NLIDNALDALAATGAPNKQVEV--FLRDE-----------GDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQG-ERGIG 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 494453306 356 LSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16915   73 LALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
406-513 2.38e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 56.40  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 406 LGSSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMyDLLFTDLIMPGgMNGVMLAREVRRRYPKVK 485
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHP-DVVLMDIRMPE-MDGIKALKEMRSHETRTP 78
                         90       100
                 ....*....|....*....|....*...
gi 494453306 486 VLLTTGYAESSIERTDIGGSEFDVVSKP 513
Cdd:PRK11361  79 VILMTAYAEVETAVEALRCGAFDYVIKP 106
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
413-498 2.47e-08

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: 52.22  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 413 LIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTgy 492
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGI-YDLIILDIMLP-GMDGLEVLKSLREEGIETPVLLLT-- 76

                 ....*.
gi 494453306 493 AESSIE 498
Cdd:cd17625   77 ALDAVE 82
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
411-499 2.58e-08

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: 52.30  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRR--RYPKVKVL- 487
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKK-FDLIITDQNMP-NMDGIELIKELRKlpAYKFTPILm 79
                         90
                 ....*....|..
gi 494453306 488 LTTgyaESSIER 499
Cdd:cd17562   80 LTT---ESSDEK 88
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
319-388 4.06e-08

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: 51.34  E-value: 4.06e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494453306 319 VSIAVTDNGIGMPASIRDRVMDPFF-----TTKEEGkGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPV 388
Cdd:cd16922   37 LRFSVEDTGIGIPEEQQARLFEPFSqadssTTRKYG-GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
411-513 5.27e-08

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: 51.29  E-value: 5.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVsEIV--LNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRYPK--VKV 486
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYL-EVVsfTDPREALAWCRE-NPPDLILLDYMMP-GMDGLEFIRRLRALPGLedVPI 78
                         90       100
                 ....*....|....*....|....*....
gi 494453306 487 LLTTGYAESSIERT--DIGGSEFdvVSKP 513
Cdd:cd17551   79 VMITADTDREVRLRalEAGATDF--LTKP 105
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
412-513 5.63e-08

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: 50.61  E-value: 5.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPGGmNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLAS-EPYDLCLTDMRLPDG-SGLELVQHIQQRLPQTPVAVITA 78
                         90       100
                 ....*....|....*....|....
gi 494453306 492 Y--AESSIERTDIGGseFDVVSKP 513
Cdd:cd19926   79 YgsLDTAIEALKAGA--FDFLTKP 100
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
412-528 8.39e-08

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 50.95  E-value: 8.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFeSGNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAAL-SPDFPGVVISDIRMPG-MDGLELLAQIRELDPDLPVILITG 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494453306 492 YAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVLD 528
Cdd:cd17549   79 HGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALE 115
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
411-527 1.17e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 52.66  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVL-LT 489
Cdd:PRK11083   5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQP-PDLVILDVGLP-DISGFELCRQLLAFHPALPVIfLT 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494453306 490 TGYAEssIERT---DIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:PRK11083  83 ARSDE--VDRLvglEIGAD--DYVAKPFSPREVAARVRTIL 119
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
51-162 1.51e-07

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 54.29  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306   51 NRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIAQR-NDISAEIINYRKDGSSFWNALFISPVYNDAGDLIYF 129
Cdd:PRK09776  309 NKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGEiNSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYF 388
                          90       100       110
                  ....*....|....*....|....*....|...
gi 494453306  130 FASQLDISRRKDAEEALRQAQKMEALGQLTGGI 162
Cdd:PRK09776  389 IAQIEDINELKRTEQVNERLMERITLANEAGGI 421
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
412-524 1.51e-07

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 49.97  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTg 491
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEP-YDLVVLDLGLP-GMDGLSVLRRWRSEGRATPVLILT- 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494453306 492 yAESS----IERTDIGGSefDVVSKPCMPHDLARKVR 524
Cdd:cd19934   78 -ARDSwqdkVEGLDAGAD--DYLTKPFHIEELLARLR 111
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
316-387 1.77e-07

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: 49.37  E-value: 1.77e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494453306 316 GRYVSIAVTDNGIGMPASIRDRVMDPFF--TTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16950   28 GNRTRIQVLDNGPGIAPEEVDELFQPFYrgDNARGTSGTGLGLAIVQRISDAHGGSLTLANRAGGGLCARIELP 101
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
411-513 2.02e-07

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 49.55  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVL--NAREALKKFESGNMyDLLFTDLIMPGGmNGVMLAREVRRRYPKVKVLL 488
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEQVPGFTVIGTagTGEEALKLLKERQP-DLILLDIYLPDG-NGLDLLRELRAAGHDVDVIV 79
                         90       100
                 ....*....|....*....|....*
gi 494453306 489 TTGYAESSIERTDIGGSEFDVVSKP 513
Cdd:cd19925   80 VTAANDVETVREALRLGVVDYLIKP 104
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
27-204 2.77e-07

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 53.23  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  27 AVETTRMPMIVTDPNRPdnpIIFSNRAFLEMTGYTAEEILG-TNCRFLQGPDTDPAVVQSIRDAIAQRNDISAEIINYRK 105
Cdd:PRK11359 141 AVDHLDRPVIVLDPERR---IVQCNRAFTEMFGYCISEASGmQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTR 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 106 DGSSFWNALFISPVYNDAGDLIYFFASQLDISrrkdaEEalRQAQKMEA--LGQLTGGIAhdfnnlLQVMGGYI-DLIGS 182
Cdd:PRK11359 218 TGEKIWIKASISPVYDVLAHLQNLVMTFSDIT-----EE--RQIRQLEGniLAAMCSSPP------FHEMGEIIcRNIES 284
                        170       180
                 ....*....|....*....|..
gi 494453306 183 AAEKPVIDVQRVQRSVYHAKSA 204
Cdd:PRK11359 285 VLNESHVSLFALRNGMPIHWAS 306
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
411-526 2.92e-07

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 49.34  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVL--NAREALK------KFESGNMYDLLFTDLIMPgGMNGVMLAREVRRRyP 482
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNELHVvrDGEEALDflrgegEYADAPRPDLILLDLNMP-RMDGFEVLREIKAD-P 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494453306 483 KVK----VLLTTGYAESSIERT-DIGGSEFdvVSKPCMPHDLARKVRQV 526
Cdd:cd17557   79 DLRripvVVLTTSDAEEDIERAyELGANSY--IVKPVDFEEFVEAIRSL 125
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
411-527 2.98e-07

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: 49.27  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMyDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRP-DAVVLDIMLP-DMDGLEVLRRLRADGPDVPVLFLT 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494453306 491 gyAESSIERT----DIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:cd17615   79 --AKDSVEDRiaglTAGGD--DYVTKPFSLEEVVARLRALL 115
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
99-139 3.28e-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: 46.79  E-value: 3.28e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 494453306    99 EIINYRKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRR 139
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
411-527 3.30e-07

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 49.26  E-value: 3.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGY--VSEIVlNAREALKKFESGnMYDLLFTDLIMPgGMNGVMLAREVRR--RYPKVKV 486
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFnnVEEAE-DGVDALEKLKAG-GFDFVITDWNMP-NMDGLELLKTIRAdgALSHLPV 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494453306 487 LLTT--GYAESSIERTDIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:cd19923   79 LMVTaeAKKENVIAAAQAGVN--NYIVKPFTAATLKEKLEKIF 119
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
411-524 4.05e-07

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 48.62  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMyDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRP-DLVLLDLMLP-GIDGIEVCRQIRAESGVPIVMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494453306 491 GYAESSIERTDIGGSEfDVVSKPCMPHDLARKVR 524
Cdd:cd17626   80 KSDTVDVVLGLESGAD-DYVAKPFKPKELVARIR 112
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
408-527 4.35e-07

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 51.22  E-value: 4.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 408 SSERILIVEDRPDVAELakmvLDDY----GYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVrRRYPK 483
Cdd:PRK10710   9 NTPRILIVEDEPKLGQL----LIDYlqaaSYATTLLSHGDEVLPYVRQTP-PDLILLDLMLP-GTDGLTLCREI-RRFSD 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494453306 484 VKVLLTTGYAEsSIER---TDIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:PRK10710  82 IPIVMVTAKIE-EIDRllgLEIGAD--DYICKPYSPREVVARVKTIL 125
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
24-91 4.39e-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: 47.01  E-value: 4.39e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494453306    24 FFAAVETTRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTDPAVVQSIRDAIA 91
Cdd:smart00091   3 LRAILESLPDGIFVLDL---DGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
412-527 4.40e-07

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: 48.57  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMyDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTg 491
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQP-DLILLDLMLP-EKDGLEVCREVRKTSNVPIIMLTA- 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494453306 492 yAESSIERT---DIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:cd17614   78 -KDSEVDKVlglELGAD--DYVTKPFSNRELLARVKANL 113
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
411-524 5.60e-07

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: 48.15  E-value: 5.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMyDLLFTDLIMPgGMNGVMLAREVRRRyPKVKVLLTT 490
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDI-DLVLLDINLP-GKDGLSLTRELREQ-SEVGIILVT 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494453306 491 GYAEsSIERtdIGGSEF---DVVSKPCMPHDLARKVR 524
Cdd:cd17619   79 GRDD-EVDR--IVGLEIgadDYVTKPFNPRELLVRAK 112
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
411-527 7.17e-07

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: 48.14  E-value: 7.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17622    2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAR-EKPDAVLLDIMLP-GIDGLTLCRDLRPKYQGPILLLTA 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494453306 491 gyAESSIERtdIGGSEF---DVVSKPCMPHDLARKVRQVL 527
Cdd:cd17622   80 --LDSDIDH--ILGLELgadDYVVKPVEPAVLLARLRALL 115
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
321-387 7.60e-07

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: 47.71  E-value: 7.60e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494453306 321 IAVTDNGIGMPASIRDRVMDPF--FTTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16921   37 FYVRDNGIGIDPEYAEKVFGIFqrLHSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
152-220 8.89e-07

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: 8.89e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494453306 152 MEALGQLTGGIAHDFNNLLQVMGGYIDLIgsaaEKPVIDVQRVQRSVYHAKSAVERASTLTKQLLAFAR 220
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELL----EEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
21-157 1.02e-06

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 51.31  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  21 KDIFFAAVETTRMPMIVTDPnrpDNPIIFSNRAFLEMTGYTAEEILGTNCRFLQGPDTdpavvqsIRDAIAQRNDISAEI 100
Cdd:COG3829   10 EEELEAILDSLDDGIIVVDA---DGRITYVNRAAERILGLPREEVIGKNVTELIPNSP-------LLEVLKTGKPVTGVI 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494453306 101 INYRKDGSSFWNAlfISPVYNDaGDLIYFFASQLDISRRKDAEEALRQAQKMEALGQ 157
Cdd:COG3829   80 QKTGGKGKTVIVT--AIPIFED-GEVIGAVETFRDITELKRLERKLREEELERGLSA 133
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
411-525 1.16e-06

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: 47.53  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRR--RYPKVKVLL 488
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARK-EKPDLILMDIQLP-GMDGLEATRLLKEdpATRDIPVIA 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494453306 489 TTGYAESSiERTDIGGSEFD-VVSKPCMPHDLARKVRQ 525
Cdd:cd17548   79 LTAYAMKG-DREKILEAGCDgYISKPIDTREFLETVAK 115
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
412-490 1.32e-06

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 47.09  E-value: 1.32e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGP-YDLVILDLGLP-DGDGLDLLRRWRRQGQSLPVLILT 77
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
411-491 1.73e-06

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: 46.81  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRS-EQPDLVLCDLRMP-EMDGLEVLKQITKESPDTPVIVVS 79

                 .
gi 494453306 491 G 491
Cdd:cd17555   80 G 80
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
408-526 1.94e-06

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: 48.37  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 408 SSERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPGGmNGVMLAREVRRRYPKVKVL 487
Cdd:COG4567    3 EDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAP-PDYAVLDLRLGDG-SGLDLIEALRERDPDARIV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494453306 488 LTTGYA--ESSIERTDIGGseFDVVSKPCMPHDLARKVRQV 526
Cdd:COG4567   81 VLTGYAsiATAVEAIKLGA--DDYLAKPADADDLLAALERA 119
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
412-515 2.87e-06

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 46.42  E-value: 2.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALkKFESGNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEAL-AFLSDQPPDVVLLDLKLP-DMSGMEILKWIQERSLPTSVIVITA 78
                         90       100
                 ....*....|....*....|....
gi 494453306 492 YAESSIERTDIGGSEFDVVSKPCM 515
Cdd:cd17572   79 HGSVDIAVEAMRLGAYDFLEKPFD 102
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
411-483 3.98e-06

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: 45.97  E-value: 3.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGY-VSEIVlNAREALKKFESGNMYDLLFTDLIMPGgMNGVMLAREVRRRYPK 483
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFqVLEAA-NGQEALEVLEQHPDIKLVITDYNMPE-MDGFELVREIRKKYSR 73
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
276-389 4.65e-06

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 49.14  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 276 NIFINARDALIGRENPKVFIetrnllvdelaNMSY-DGLLpgryvSIAVTDNGIGMPASIRDRVMDPFFTTKeeGKGSGL 354
Cdd:PRK11086 440 NLIENALEAVGGEEGGEISV-----------SLHYrNGWL-----HCEVSDDGPGIAPDEIDAIFDKGYSTK--GSNRGV 501
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494453306 355 GLSMVygfaKQS----GGAARIYTEEGVGTTLRLYFPVD 389
Cdd:PRK11086 502 GLYLV----KQSvenlGGSIAVESEPGVGTQFFVQIPWD 536
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
412-526 4.83e-06

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 45.61  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVED-RPDVAELAKMV--LDDYGYVSEiVLNAREALKKFESgNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLL 488
Cdd:cd17532    1 ALIVDDePLAREELRYLLeeHPDIEIVGE-AENGEEALEAIEE-LKPDVVFLDIQMPG-LDGLELAKKLSKLAKPPLIVF 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494453306 489 TTGYAESSIERTDIGGseFDVVSKPCMPHDLARKVRQV 526
Cdd:cd17532   78 VTAYDEYAVEAFELNA--VDYLLKPFSEERLAEALAKL 113
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
410-497 5.49e-06

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: 45.51  E-value: 5.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 410 ERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPGGmNGVMLAREVRRRYPKVKVLLT 489
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALARE-EKPDYAVLDLRLGGD-SGLDLIPPLRALQPDARIVVL 78

                 ....*...
gi 494453306 490 TGYAesSI 497
Cdd:cd17563   79 TGYA--SI 84
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
411-527 1.20e-05

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: 44.67  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFeSGNMYDLLFTDLIMPgGMNGVMLAREVRRRYpKVKVLLTT 490
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRI-IDEQPSLVVLDIMLP-GMDGLTVCREVREHS-HVPILMLT 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494453306 491 GYAEsSIERT---DIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:cd19939   78 ARTE-EMDRVlglEMGAD--DYLCKPFSPRELLARVRALL 114
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
409-528 1.22e-05

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: 44.46  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 409 SERILIVEDRPDVAELAKMVLDDY-GYvseIVLNA---REALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRyPKV 484
Cdd:cd17552    1 SKRILVIDDEEDIREVVQACLEKLaGW---EVLTAssgQEGLEKAAT-EQPDAILLDVMMP-DMDGLATLKKLQAN-PET 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494453306 485 K---VLLTTGYAESSIER--TDIGGSefDVVSKPCMPHDLARKVRQVLD 528
Cdd:cd17552   75 QsipVILLTAKAQPSDRQrfASLGVA--GVIAKPFDPLTLAEQIAKLLG 121
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
411-527 1.43e-05

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 44.55  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRR--RYPKVKVLL 488
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVE-PRPDLILLDWMLP-GGSGIQFIRRLKRdeMTRDIPIIM 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494453306 489 TTGYAESS--IERTDIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:cd17618   80 LTARGEEEdkVRGLEAGAD--DYITKPFSPRELVARIKAVL 118
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
411-514 2.65e-05

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: 43.26  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYvsEIVL--NAREALKKFESGNMyDLLFTDLIMPgGMNGVMLAREVR--RRYPKVKV 486
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGY--EVLTadSGQEALALAEEELP-DLILLDVMMP-GMDGFEVCRRLKedPETRHIPV 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 494453306 487 LLTTGY--AESSIERTDIGGSEFdvVSKPC 514
Cdd:cd17538   77 IMITALddREDRIRGLEAGADDF--LSKPI 104
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
313-388 2.84e-05

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: 43.19  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 313 LLPGRYVSIAVTDNGIGMPASIRDRVMDPFF-----TTKEEGkGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16939   25 LVSGGRLTLIVEDDGPGIPAAARERVFEPFVrldpsRDRATG-GFGLGLAIVHRVALWHGGHVECDDSELGGACFRLTWP 103

                 .
gi 494453306 388 V 388
Cdd:cd16939  104 R 104
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
319-384 3.53e-05

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 43.68  E-value: 3.53e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494453306 319 VSIAVTDNGIGMPASirDRVMDPFFTTKEEGKGSGLGLSMVYGFAKQsggaARIYTEEGVGTTLRL 384
Cdd:cd16942   74 VHLTVRDEGVGIPDI--EEARQPLFTTKPELERSGMGFTIMENFMDE----VIVESEVNKGTTVYL 133
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
412-513 3.89e-05

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 46.18  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFeSGNMYDLLFTDLIMpGGMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQV-REQVFDLVLCDVRM-AEMDGIATLKEIKALNPAIPVLIMTA 85
                         90       100
                 ....*....|....*....|....
gi 494453306 492 YA--ESSIERTDIGGseFDVVSKP 513
Cdd:PRK10365  86 YSsvETAVEALKTGA--LDYLIKP 107
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
412-513 4.08e-05

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: 42.75  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALkKFESGNMYDLLFTDLIMPgGMNGVMLAREVRR--RYPKVKVLLT 489
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEAL-DLLNQYIPDLIISDIIMP-GVDGYSLLGKLRKnaDFDTIPVIFL 78
                         90       100
                 ....*....|....*....|....*.
gi 494453306 490 T--GYAESSIERTDIGGSEFdvVSKP 513
Cdd:cd19927   79 TakGMTSDRIKGYNAGCDGY--LSKP 102
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
411-524 4.43e-05

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: 43.15  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVsEIVL---NAREALKKFESGNMyDLLFTDLIMPgGMNGVMLAREVRRRYPkVKVL 487
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDPDI-EVVGtarDGEEALEKIKELKP-DVITLDIEMP-VMDGLEALRRIMAERP-TPVV 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 494453306 488 ----LTTGYAESSIERTDIGGseFDVVSKPCMP---------HDLARKVR 524
Cdd:cd17541   78 mvssLTEEGAEITLEALELGA--VDFIAKPSGGisldleeiaEELIEKIK 125
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
412-528 6.00e-05

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 42.64  E-value: 6.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDV--AELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLLT 489
Cdd:cd19930    1 VLIAEDQEMVrgALAALLELEDDLEVVAQASNGQEALRLVLKHS-PDVAILDIEMPG-RTGLEVAAELREELPDTKVLIV 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494453306 490 T-----GYAESSIErTDIGGsefdVVSKPCMPHDLARKVRQVLD 528
Cdd:cd19930   79 TtfgrpGYFRRALA-AGVDG----YVLKDRPIEELADAIRTVHA 117
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
412-490 6.84e-05

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 42.37  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESG--------NMYDLLFTDLIMPgGMNGVMLAREVRR--RY 481
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlsKELDLIITDIEMP-KMDGYELTFELRDdpRL 79

                 ....*....
gi 494453306 482 PKVKVLLTT 490
Cdd:cd19924   80 ANIPVILNS 88
PRK15347 PRK15347
two component system sensor kinase;
321-390 8.96e-05

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 45.40  E-value: 8.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 321 IAVTDNGIGMPASIRDRVMDPFFTTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDE 390
Cdd:PRK15347 547 FTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNE 616
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
412-513 9.02e-05

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 41.80  E-value: 9.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREVRRRyPKVKVLLTTG 491
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDR-AGADIVLLDLMLP-GLSGTEVCRQLRAR-SNVPVIMVTA 77
                         90       100
                 ....*....|....*....|....*
gi 494453306 492 yAESSIERT---DIGGSefDVVSKP 513
Cdd:cd17621   78 -KDSEIDKVvglELGAD--DYVTKP 99
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
409-527 1.39e-04

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 43.55  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 409 SERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPGGmNGVM----LAREVRRRYPKV 484
Cdd:PRK10161   2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNE-PWPDLILLDWMLPGG-SGIQfikhLKRESMTRDIPV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494453306 485 KVLLTTGYAESSIERTDIGGSefDVVSKPCMPHDLARKVRQVL 527
Cdd:PRK10161  80 VMLTARGEEEDRVRGLETGAD--DYITKPFSPKELVARIKAVM 120
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
316-390 1.69e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 44.24  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 316 GRYVSIAVTDNGIGMPASIRDRVMDPFfttKEEGKGSGLGLSMV-----------YGFakqsggaaRIYTEEGVGTTLRL 384
Cdd:COG2972  370 GDRLVITVEDNGVGMPEEKLEKLLEEL---SSKGEGRGIGLRNVrerlklyygeeYGL--------EIESEPGEGTTVTI 438

                 ....*.
gi 494453306 385 YFPVDE 390
Cdd:COG2972  439 RIPLEE 444
PRK15369 PRK15369
two component system response regulator;
411-494 1.98e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 42.76  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVsEIVLNAREALKKFESGNMY--DLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLL 488
Cdd:PRK15369   5 KILLVDDHELIINGIKNMLAPYPRY-KIVGQVDNGLEVYNACRQLepDIVILDLGLPG-MNGLDVIPQLHQRWPAMNILV 82

                 ....*.
gi 494453306 489 TTGYAE 494
Cdd:PRK15369  83 LTARQE 88
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
316-387 2.04e-04

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: 40.94  E-value: 2.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494453306 316 GRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEG----KGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:cd16925   35 LNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSStrahGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
PRK10604 PRK10604
sensor protein RstB; Provisional
211-388 2.12e-04

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 43.82  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 211 LTKQLLAFAR----KQKLQGRVLNLNG-LVSIVEPLieRTFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINARDAL 285
Cdd:PRK10604 258 LIEELLTYARldrpQNELHLSEPDLPAwLSTHLADI--QAVTPEKTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRYA 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 286 IGREnpkvfieTRNLLVDelanmsydgllpGRYVSIAVTDNGIGMPASIRDRVMDPfFTTKEEGK-----GSGLGLSMVY 360
Cdd:PRK10604 336 HSRV-------RVSLLLD------------GNQACLIVEDDGPGIPPEERERVFEP-FVRLDPSRdratgGCGLGLAIVH 395
                        170       180
                 ....*....|....*....|....*...
gi 494453306 361 GFAKQSGGAARIYTEEGVGTTLRLYFPV 388
Cdd:PRK10604 396 SIALAMGGSVNCDESELGGARFSFSWPV 423
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
411-527 2.78e-04

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 42.48  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGnmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS--IDLLLLDVMMP-KKNGIDTLKELRQTHQTPVIMLTA 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494453306 491 gyAESSIERtdIGGSEF---DVVSKPCMPHDLARKVRQVL 527
Cdd:PRK10955  80 --RGSELDR--VLGLELgadDYLPKPFNDRELVARIRAIL 115
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
410-503 3.91e-04

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 40.23  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 410 ERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKkFESGNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLLT 489
Cdd:cd17553    1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALD-IVTKERPDLVLLDMKIPG-MDGIEILKRMKVIDENIRVIIM 78
                         90
                 ....*....|....*.
gi 494453306 490 TGYAESSI--ERTDIG 503
Cdd:cd17553   79 TAYGELDMiqESKELG 94
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
410-513 3.92e-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: 40.33  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 410 ERILIVEDrpD-----VAELAkmvLDDYGYVSEIVLNAREALKKFESgNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKV 484
Cdd:cd19919    1 KTVWIVDD--DssirwVLERA---LAGAGLTVTSFENAQEALAALAS-SQPDVLISDIRMPG-MDGLALLAQIKQRHPDL 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 494453306 485 KVLLTTGYA--ESSIERTDIGGseFDVVSKP 513
Cdd:cd19919   74 PVIIMTAHSdlDSAVSAYQGGA--FEYLPKP 102
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
316-387 3.95e-04

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 43.28  E-value: 3.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494453306 316 GRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEGKGS-GLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFP 387
Cdd:PRK15053 466 GDDVVIEVADQGCGVPESLRDKIFEQGVSTRADEPGEhGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
113-391 4.79e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 41.91  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 113 ALFISPVyndAGDLIYFFASQLDISRRKDAEEALRQAQKMEALGQLTGGIA---HDfnNLLQVMGGYIDLIGSAAEKPVI 189
Cdd:COG4585   11 ALLVGAL---LGLLLALVLLRARRAERAAELERELAARAEEAREEERRRIArelHD--GVGQSLSAIKLQLEAARRLLDA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 190 DVQRVQRSVYHAKSAVERASTLTKQLLAfarkqKLQGRVLNLNGLVSIVEPLIERtFGPEVAIETDLEPALKNCRIDPTQ 269
Cdd:COG4585   86 DPEAAREELEEIRELAREALAELRRLVR-----GLRPPALDDLGLAAALEELAER-LLRAAGIRVELDVDGDPDRLPPEV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 270 AEV-------ALLNIfinARDAligrenpkvfiETRNLLVDelanMSYDGllpgRYVSIAVTDNGIGMPAsirdrvmdpf 342
Cdd:COG4585  160 ELAlyrivqeALTNA---LKHA-----------GATRVTVT----LEVDD----GELTLTVRDDGVGFDP---------- 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 494453306 343 fttkEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEA 391
Cdd:COG4585  208 ----EAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLAAA 252
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
412-470 5.83e-04

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 39.42  E-value: 5.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNG 470
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEP-PDLILLDVMMP-GMDG 57
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
319-387 6.93e-04

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 40.40  E-value: 6.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 319 VSIAVTDNGIGMPASIRDRVMDPFFTTKEE-------------------GKGSGLGLSMVYgfAKQSGGAARIYTEEGVG 379
Cdd:cd16929   84 LTIKISDRGGGIPREDLARLFSYMYSTAPQpslddfsdlisgtqpsplaGFGYGLPMSRLY--AEYFGGDLDLQSMEGYG 161

                 ....*...
gi 494453306 380 TTLRLYFP 387
Cdd:cd16929  162 TDVYIYLK 169
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
321-386 7.44e-04

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: 39.31  E-value: 7.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494453306 321 IAVTDNGIGMPASIRDRVMDPFF-TTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYF 386
Cdd:cd16940   47 IRVEDNGPGIDEEELEALFERFYrSDGQNYGGSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
PRK10643 PRK10643
two-component system response regulator PmrA;
411-490 7.76e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 41.17  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPGGmNGVMLAREVRRRYPKVKVLLTT 490
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGH-YSLVVLDLGLPDE-DGLHLLRRWRQKKYTLPVLILT 79
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
411-520 7.81e-04

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: 40.71  E-value: 7.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGY-VSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLT 489
Cdd:COG3707    5 RVLVVDDEPLRRADLREGLREAGYeVVAEAADGEDAVELVRELK-PDLVIVDIDMP-DRDGLEAARQISEERPAPVILLT 82
                         90       100       110
                 ....*....|....*....|....*....|..
gi 494453306 490 TGYAESSIER-TDIGGSEFdvVSKPCMPHDLA 520
Cdd:COG3707   83 AYSDPELIERaLEAGVSAY--LVKPLDPEDLL 112
PRK10766 PRK10766
two-component system response regulator TorR;
409-527 9.49e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 40.79  E-value: 9.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 409 SERILIVEDRPdvaeLAKMVLDDY----GY-VSEiVLNAREALKKFESGNMyDLLFTDLIMPGgMNGVMLAREVRRRyPK 483
Cdd:PRK10766   2 SYHILVVEDEP----VTRARLQGYfeqeGYtVSE-AASGAGMREIMQNQHV-DLILLDINLPG-EDGLMLTRELRSR-ST 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494453306 484 VKVLLTTGYAEsSIERtdIGGSEF---DVVSKPCMPHDLARKVRQVL 527
Cdd:PRK10766  74 VGIILVTGRTD-SIDR--IVGLEMgadDYVTKPLELRELLVRVKNLL 117
ompR PRK09468
osmolarity response regulator; Provisional
410-527 9.51e-04

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 41.11  E-value: 9.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 410 ERILIVEDRPDVAELAKMVLDDYGYVSEIVLNArEALKKFESGNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLT 489
Cdd:PRK09468   6 YKILVVDDDMRLRALLERYLTEQGFQVRSAANA-EQMDRLLTRESFHLMVLDLMLP-GEDGLSICRRLRSQNNPTPIIML 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494453306 490 TGYAEsSIERtdIGGSEF---DVVSKPCMPHDLARKVRQVL 527
Cdd:PRK09468  84 TAKGE-EVDR--IVGLEIgadDYLPKPFNPRELLARIRAVL 121
PRK15115 PRK15115
response regulator GlrR; Provisional
409-497 1.01e-03

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 41.75  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 409 SERILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNMyDLLFTDLIMpGGMNGVMLAREVRRRYPKVKVLL 488
Cdd:PRK15115   5 PAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKV-DLVISDLRM-DEMDGMQLFAEIQKVQPGMPVII 82

                 ....*....
gi 494453306 489 TTgyAESSI 497
Cdd:PRK15115  83 LT--AHGSI 89
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
411-477 1.18e-03

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: 39.11  E-value: 1.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEI--VLNAREALKKFESgNMYDLLFTDLIMPgGMNGVMLAREV 477
Cdd:COG2197    3 RVLIVDDHPLVREGLRALLEAEPDIEVVgeAADGEEALELLEE-LRPDVVLLDIRMP-GMDGLEALRRL 69
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
316-389 1.18e-03

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 41.37  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494453306 316 GRYVSIAVTDNGIGMPASIRDRVMDPFFTTKEEG---KGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVD 389
Cdd:PRK11100 398 GEQVALSVEDQGPGIPDYALPRIFERFYSLPRPAngrKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRH 474
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
412-527 1.21e-03

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: 38.90  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFeSGNMYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVI-SGNRPDAVVLDVMMP-RLDGLEVCRRLRAAGNDLPILVLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494453306 492 YAESS--IERTDIGGSEFDVvsKPCMPHDLARKVRQVL 527
Cdd:cd17627   79 RDSVSdrVAGLDAGADDYLV--KPFALEELLARVRALL 114
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
316-384 1.31e-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: 38.60  E-value: 1.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494453306 316 GRYVSIAVTDNGIGMPASIRDRVMDPFFT---TKEEGKGSGLGLSMVYGFAKQSGGAARIYT-EEGVGTTLRL 384
Cdd:cd16945   34 TEGIELLVFDEGSGIPDYALNRVFERFYSlprPHSGQKSTGLGLAFVQEVAQLHGGRITLRNrPDGVLAFLTL 106
envZ PRK09467
osmolarity sensor protein; Provisional
214-390 2.17e-03

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 40.66  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 214 QLLAFARK-QKLQGRVLNLNGLVSIVeplIERTFGPEVAIETDLEPALKNCRIDPTQAEVALLNIFINArdALIGRENPK 292
Cdd:PRK09467 278 QFIDYLRTgQEMPMEMADLNALLGEV---IAAESGYEREIETALQPGPIEVPMNPIAIKRALANLVVNA--ARYGNGWIK 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 293 VfietrnllvdelaNMSYDGllpgRYVSIAVTDNGIGMPASIRDRVMDPFFT--TKEEGKGSGLGLSMVYGFAKQSGGAA 370
Cdd:PRK09467 353 V-------------SSGTEG----KRAWFQVEDDGPGIPPEQLKHLFQPFTRgdSARGSSGTGLGLAIVKRIVDQHNGKV 415
                        170       180
                 ....*....|....*....|
gi 494453306 371 RIYTEEGVGTTLRLYFPVDE 390
Cdd:PRK09467 416 ELGNSEEGGLSARAWLPLTT 435
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
412-528 2.70e-03

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: 39.31  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFEsGNMYDLLFTDLIMPGgMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALD-PDRPGCLLLDVRMPG-MSGLELQEELAARGSPLPVIFLTG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494453306 492 YAessiertDI--------GGSeFDVVSKPCMPHDLARKVRQVLD 528
Cdd:COG4566   80 HG-------DVpmavramkAGA-VDFLEKPFDDQALLDAVRRALA 116
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
412-527 3.46e-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: 37.39  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTTG 491
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYD-YDIILLDLNLP-DMSGYEVLRTLRLAKVKTPILILSG 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494453306 492 YAESSIERTDIGGSEFDVVSKPCMPHDLARKVRQVL 527
Cdd:cd17616   79 LADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
PRK15479 PRK15479
transcriptional regulator TctD;
411-490 3.55e-03

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 38.93  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLLTT 490
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEM-YALAVLDINMP-GMDGLEVLQRLRKRGQTLPVLLLT 79
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
316-388 3.88e-03

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 37.59  E-value: 3.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494453306 316 GRYVSIAVTDNGIGMPasiRDRVMDPFfttkEEGKGSGLGLSMVYGFAKQSGgaariYTEEGVGTTLRLYFPV 388
Cdd:COG2172   67 PDGLEIEVRDEGPGFD---PEDLPDPY----STLAEGGRGLFLIRRLMDEVE-----YESDPGGTTVRLVKRL 127
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
411-490 3.89e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 39.23  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 411 RILIVEDRPDVAELAKMVLDDYGYvsEIVLNAR--EALKKFESGNMyDLLFTDLIMPgGMNGVMLAREVRRRYPKVKVLL 488
Cdd:PRK10701   3 KIVFVEDDAEVGSLIAAYLAKHDI--DVTVEPRgdRAEATILREQP-DLVLLDIMLP-GKDGMTICRDLRPKWQGPIVLL 78

                 ..
gi 494453306 489 TT 490
Cdd:PRK10701  79 TS 80
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
412-478 4.61e-03

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 36.76  E-value: 4.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494453306 412 ILIVEDRPDVAELAKMVLDDYGYVSEIVLNAREALKKFESGNmYDLLFTDLIMPgGMNGVMLAREVR 478
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRK-PDLIILDLGLP-DMDGLEVIRRLR 65
PRK13435 PRK13435
response regulator; Provisional
410-521 5.82e-03

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 37.34  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306 410 ERILIVEDRPDVAELAKMVLDDYGY-VSEIVLNAREAL---KKFESgnmyDLLFTDLIMPGGMNGVMLAREVRRRYpKVK 485
Cdd:PRK13435   6 LKVLIVEDEALIALELEKLVEEAGHeVVGIAMSSEQAIalgRRRQP----DVALVDVHLADGPTGVEVARRLSADG-GVE 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494453306 486 VLLTTGyaesSIER--TDIGGSEfDVVSKPCMPHDLAR 521
Cdd:PRK13435  81 VVFMTG----NPERvpHDFAGAL-GVIAKPYSPRGVAR 113
PRK13560 PRK13560
hypothetical protein; Provisional
12-149 6.71e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 39.27  E-value: 6.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494453306  12 ATGDIQHQGKDIFFAAVETTRMPMIVTDPnrpDNPIIFSNRAFLE-MTGYTAEEILGTN-------------CRFLQ--G 75
Cdd:PRK13560 322 AAERELLEKEDMLRAIIEAAPIAAIGLDA---DGNICFVNNNAAErMLGWSAAEVMGKPlpgmdpelneefwCGDFQewY 398
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494453306  76 PDTDPAVVQSIRDAIAQRNDI---SAEIINYRKDGSSFWNALFISPVYNDAGDLIYFFASQLDISRRKDAEEALRQA 149
Cdd:PRK13560 399 PDGRPMAFDACPMAKTIKGGKifdGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLA 475
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
318-371 7.03e-03

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 39.15  E-value: 7.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494453306 318 YVSIAVTDNGIGMPASIRDRVMDPFFTTKE----EGKGSGLGLSMVYGFAKQSGGAAR 371
Cdd:PRK09470 383 GLTITVDDDGPGVPEEEREQIFRPFYRVDEardrESGGTGLGLAIVENAIQQHRGWVK 440
 
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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