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Conserved domains on  [gi|489342835|ref|WP_003249998|]
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MULTISPECIES: sigma-54 dependent transcriptional regulator [Pseudomonas]

Protein Classification

sigma-54-dependent transcriptional regulator( domain architecture ID 11454220)

sigma-54 factor interaction domain-containing protein with a domain similar to that found in the response regulator FleR from Pseudomonas aeruginosa

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-469 0e+00

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: 513.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMT 76
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRelraLDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQNAPAAAPPAeprasngkatapdkgsaatangeiGIIGSC 156
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS------------------------GLIGRS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 157 QPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGR 236
Cdd:COG2204  138 PAMQEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 237 AGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVI 316
Cdd:COG2204  218 IGKFELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVF 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 317 ALKLPALRERGSDVNEIANVFLARQSARIGRDdLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLGID 396
Cdd:COG2204  298 PIELPPLRERREDIPLLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA 376
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489342835 397 IElsDLEEDDILDnALVvanagnasheptedlsledyfqhfvlEHQDHMTETelARKLGVSRKCLWERRQRLG 469
Cdd:COG2204  377 LE--EVERELIER-ALE--------------------------ETGGNVSRA--AELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-469 0e+00

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: 513.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMT 76
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRelraLDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQNAPAAAPPAeprasngkatapdkgsaatangeiGIIGSC 156
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS------------------------GLIGRS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 157 QPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGR 236
Cdd:COG2204  138 PAMQEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 237 AGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVI 316
Cdd:COG2204  218 IGKFELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVF 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 317 ALKLPALRERGSDVNEIANVFLARQSARIGRDdLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLGID 396
Cdd:COG2204  298 PIELPPLRERREDIPLLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA 376
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489342835 397 IElsDLEEDDILDnALVvanagnasheptedlsledyfqhfvlEHQDHMTETelARKLGVSRKCLWERRQRLG 469
Cdd:COG2204  377 LE--EVERELIER-ALE--------------------------ETGGNVSRA--AELLGISRRTLYRKLKKYG 418
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-401 3.24e-123

nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response regulator that is phosphorylated by NtrB and interacts with sigma-54. NtrC usually controls the expression of glutamine synthase, GlnA, and may be called GlnL, GlnG, etc. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 367.53  E-value: 3.24e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTSYA 79
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLpqikKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQNApaaappaeprasnGKATAPdkgsAATANGEIGIIGSCQPM 159
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQ-------------VALPAD----AGEAEDSAELIGEAPAM 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  160 QDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 239
Cdd:TIGR01818 144 QEVFRAIGRLSRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGR 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  240 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALK 319
Cdd:TIGR01818 224 FEQADGGTLFLDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIH 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  320 LPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLgiDIEL 399
Cdd:TIGR01818 304 LPPLRERREDIPRLARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDL--PAEL 381

                  ..
gi 489342835  400 SD 401
Cdd:TIGR01818 382 AL 383
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-470 1.31e-122

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 365.71  E-value: 1.31e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKemrsHETRTPVILMTAYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRqnapaaappaepraSNGKATAPDKGSAATANGEIGIIGSCQPM 159
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQ--------------SMKKEIRHLHQALSTSWQWGHILTNSPAM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 160 QDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 239
Cdd:PRK11361 153 MDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 240 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALK 319
Cdd:PRK11361 233 FERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLI 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 320 LPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLGIDIEL 399
Cdd:PRK11361 313 LPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQ 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489342835 400 SdleeddildnalvVANAGNASHEPTEDLSLEDYFQHF-------VLEHQDHmTETELARKLGVSRKCLWERRQRLGI 470
Cdd:PRK11361 393 P-------------VCNAGEVKTAPVGERNLKEEIKRVekriimeVLEQQEG-NRTRTALMLGISRRALMYKLQEYGI 456
Sigma54_activat pfam00158
Sigma-54 interaction domain;
152-318 3.15e-112

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 328.21  E-value: 3.15e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  152 IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTG 231
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  232 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYY 311
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 489342835  312 RLHVIAL 318
Cdd:pfam00158 161 RLNVIPI 167
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
152-410 8.44e-105

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 323.77  E-value: 8.44e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 152 IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRaKAPMISVNCAAIPETLIESELFGHEKGAFTG 231
Cdd:NF041552 269 IIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGR-KGPFVPVNCSAIPEELFESEFFGYEEGAFTG 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 232 AS-AGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLY 310
Cdd:NF041552 348 ALkKGKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFREDLY 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 311 YRLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISA 390
Cdd:NF041552 428 YRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNGTITK 507
                        250       260
                 ....*....|....*....|
gi 489342835 391 ELLGIDIeLSDLEEDDILDN 410
Cdd:NF041552 508 DSIPEYI-LESVKKKEDEEG 526
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
151-474 4.65e-102

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 315.27  E-value: 4.65e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 151 GIIGSCQPMQDMYSKIRKVAPTD-SNVLIQGESGTGKELVARALHNLSRRA---KAPMISVNCAAIPETLIESELFGHEK 226
Cdd:NF038308 180 GIATRNAAFNRLIEQIERVALRSrAPILLTGPTGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMSELFGHVK 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 227 GAFTGASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFR 306
Cdd:NF038308 260 GAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFR 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 307 EDLYYRLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDDLhFSAEAEQ------AIRHYSWPGNVRELENAVERAV 380
Cdd:NF038308 340 EDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRQVR-FNKEARFrylafaTSPEALWPGNFRELSASVTRMA 418
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 381 ILSESAEISAELLgiDIELSDLEEDDildnalvvanagNASHEPTEDLSLEDYFQHFVLEHQDHMTETELARKLGVSRKC 460
Cdd:NF038308 419 TLADGGRITEELV--EEEIARLRAAW------------QSAPAAADDDALADLLGGEQLAELDLFDRVQLAAVLRVCRQS 484
                        330
                 ....*....|....*..
gi 489342835 461 LWER---RQRLGIPRRK 474
Cdd:NF038308 485 RSLSaagRRLFGVSRQQ 501
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
5-99 9.87e-28

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 106.16  E-value: 9.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTSYAS 80
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLrklrELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 489342835  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
175-295 3.96e-12

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 63.93  E-value: 3.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   175 NVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIES---ELFGHEKGAFTGASAGRAG--LVEAADGGTLF 249
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 489342835   250 LDEIGELPLEAQARLLRVLQEgeiRRVGSVQSQKVDVRLIAATHRD 295
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTNDE 126
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-469 0e+00

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: 513.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMT 76
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRelraLDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQNAPAAAPPAeprasngkatapdkgsaatangeiGIIGSC 156
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS------------------------GLIGRS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 157 QPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGR 236
Cdd:COG2204  138 PAMQEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 237 AGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVI 316
Cdd:COG2204  218 IGKFELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVF 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 317 ALKLPALRERGSDVNEIANVFLARQSARIGRDdLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLGID 396
Cdd:COG2204  298 PIELPPLRERREDIPLLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA 376
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489342835 397 IElsDLEEDDILDnALVvanagnasheptedlsledyfqhfvlEHQDHMTETelARKLGVSRKCLWERRQRLG 469
Cdd:COG2204  377 LE--EVERELIER-ALE--------------------------ETGGNVSRA--AELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
151-470 2.52e-153

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: 443.44  E-value: 2.52e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 151 GIIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFT 230
Cdd:COG3829  139 DIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAFT 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 231 GASA-GRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDL 309
Cdd:COG3829  219 GAKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFREDL 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 310 YYRLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEIS 389
Cdd:COG3829  299 YYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSEGDVIT 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 390 AELLGIDIELSDLEEDDILDNALvvanagNASHEPTEDLSLEDYFQHFvlehqdHMTETELARKLGVSRKCLWERRQRLG 469
Cdd:COG3829  379 PEHLPEYLLEEAEAASAAEEGSL------KEALEEVEKELIEEALEKT------GGNKSKAAKALGISRSTLYRKLKKYG 446

                 .
gi 489342835 470 I 470
Cdd:COG3829  447 I 447
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-401 3.24e-123

nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response regulator that is phosphorylated by NtrB and interacts with sigma-54. NtrC usually controls the expression of glutamine synthase, GlnA, and may be called GlnL, GlnG, etc. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 367.53  E-value: 3.24e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTSYA 79
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLpqikKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQNApaaappaeprasnGKATAPdkgsAATANGEIGIIGSCQPM 159
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQ-------------VALPAD----AGEAEDSAELIGEAPAM 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  160 QDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 239
Cdd:TIGR01818 144 QEVFRAIGRLSRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGR 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  240 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALK 319
Cdd:TIGR01818 224 FEQADGGTLFLDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIH 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  320 LPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLgiDIEL 399
Cdd:TIGR01818 304 LPPLRERREDIPRLARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDL--PAEL 381

                  ..
gi 489342835  400 SD 401
Cdd:TIGR01818 382 AL 383
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-470 1.31e-122

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 365.71  E-value: 1.31e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKemrsHETRTPVILMTAYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRqnapaaappaepraSNGKATAPDKGSAATANGEIGIIGSCQPM 159
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQ--------------SMKKEIRHLHQALSTSWQWGHILTNSPAM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 160 QDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 239
Cdd:PRK11361 153 MDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 240 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALK 319
Cdd:PRK11361 233 FERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLI 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 320 LPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLGIDIEL 399
Cdd:PRK11361 313 LPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQ 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489342835 400 SdleeddildnalvVANAGNASHEPTEDLSLEDYFQHF-------VLEHQDHmTETELARKLGVSRKCLWERRQRLGI 470
Cdd:PRK11361 393 P-------------VCNAGEVKTAPVGERNLKEEIKRVekriimeVLEQQEG-NRTRTALMLGISRRALMYKLQEYGI 456
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
86-470 5.72e-122

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 365.65  E-value: 5.72e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  86 DSMKMGAVDYIAkpfdhDEMLQAVARILRDRQNAPAAAPPAEPRASNGKATAPDKGSAATANGEIgiIGSCQPMQDMYSK 165
Cdd:PRK05022 130 DALDPGQFDAFS-----DEELRALAALAAATLRNALLIEQLESQAELPQDVAEFLRQEALKEGEM--IGQSPAMQQLKKE 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 166 IRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEAADG 245
Cdd:PRK05022 203 IEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADG 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 246 GTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALKLPALRE 325
Cdd:PRK05022 283 GTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRE 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 326 RGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLgidIELSDLeed 405
Cdd:PRK05022 363 RGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVISRAALLARARGAGRIVT---LEAQHL--- 436
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489342835 406 DILDNALVVANAGNASHEPTEDLSLE---DYFQHFVLE-----HQDHMTETelARKLGVSRKCLWERRQRLGI 470
Cdd:PRK05022 437 DLPAEVALPPPEAAAAPAAVVSQNLReatEAFQRQLIRqalaqHQGNWAAA--ARALELDRANLHRLAKRLGL 507
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-467 3.68e-118

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 353.95  E-value: 3.68e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKeikaLNPAIPVLIMTAYS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQNAPAAAppaeprasngkatapdkgSAATANgEIGIIGSCQPM 159
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAET------------------PAVTAS-QFGMVGKSPAM 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 160 QDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 239
Cdd:PRK10365 149 QHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 240 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALK 319
Cdd:PRK10365 229 FVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIE 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 320 LPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLGIDIEl 399
Cdd:PRK10365 309 VPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIA- 387
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489342835 400 sdleeddildnALVVANAGNASHEPTEDLSLEDYFQhfVLEhQDHMTETELARKLGVSRKCLWERRQR 467
Cdd:PRK10365 388 -----------STPIPLGQSQDIQPLVEVEKEVILA--ALE-KTGGNKTEAARQLGITRKTLLAKLSR 441
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
151-469 6.21e-116

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 354.21  E-value: 6.21e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 151 GIIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFT 230
Cdd:COG3284  322 ALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFT 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 231 GASA-GRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDL 309
Cdd:COG3284  402 GARRkGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDL 481
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 310 YYRLHVIALKLPALRERgSDVNEIANVFLARQSARigRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEis 389
Cdd:COG3284  482 YYRLNGLTLTLPPLRER-EDLPALIEHLLRELAAG--RGPLRLSPEALALLAAYPWPGNVRELRNVLRTALALADGGV-- 556
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 390 aellgidIELSDLEED--DILDNALVVANAGNASHEPTEDLSLEDYFQhfvlEHQDHMTETelARKLGVSRKCLWERRQR 467
Cdd:COG3284  557 -------ITVEDLPDElrAELAAAAPAAAAPLTSLEEAERDAILRALR----ACGGNVSAA--ARALGISRSTLYRKLKR 623

                 ..
gi 489342835 468 LG 469
Cdd:COG3284  624 YG 625
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
4-396 1.72e-113

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 341.73  E-value: 1.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835    4 ILIVEDETIIRSALRRLLErnQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGT---------ELIKLGQGTPVLI 74
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPPDADGaseglaalqQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRdrqnapaaapPAEPRASNGKATAPDKGSAATangeiGIIG 154
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFH----------LYTLETENRRLQSALGGTALR-----GLIT 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  155 SCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASA 234
Cdd:TIGR02915 144 SSPGMQKICRTIEKIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  235 GRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLH 314
Cdd:TIGR02915 224 QTLGKIEYAHGGTLFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIA 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  315 VIALKLPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLG 394
Cdd:TIGR02915 304 EISITIPPLRSRDGDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLG 383

                  ..
gi 489342835  395 ID 396
Cdd:TIGR02915 384 LD 385
Sigma54_activat pfam00158
Sigma-54 interaction domain;
152-318 3.15e-112

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 328.21  E-value: 3.15e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  152 IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTG 231
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  232 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYY 311
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 489342835  312 RLHVIAL 318
Cdd:pfam00158 161 RLNVIPI 167
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
4-470 8.22e-107

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 325.67  E-value: 8.22e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQGT----PVLIMTSYA 79
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRhpmlPVIIMTAHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQNapaaappaepraSNGKATAPDKGSAATangeigIIGSCQPM 159
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQE------------QQQPRNIQVNGPTTD------IIGEAPAM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 160 QDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 239
Cdd:PRK10923 148 QDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGR 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 240 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALK 319
Cdd:PRK10923 228 FEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVH 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 320 LPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELLGIDIEL 399
Cdd:PRK10923 308 LPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFE 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 400 SDLEEDDIL---DN--ALVVANAGNASHEPTEDL------SLEDYFQHFVLEH-QDHmtETELARKLGVSRKCLWERRQR 467
Cdd:PRK10923 388 STVPESTSQmqpDSwaTLLAQWADRALRSGHQNLlseaqpELERTLLTTALRHtQGH--KQEAARLLGWGRNTLTRKLKE 465

                 ...
gi 489342835 468 LGI 470
Cdd:PRK10923 466 LGM 468
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
151-390 4.45e-106

Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein for nitrogen fixation. The model produces scores between the trusted and noise cutoffs for a well-described NifA homolog in Aquifex aeolicus (which lacks nitrogenase), for transcriptional activators of alternative nitrogenases (VFe or FeFe instead of MoFe), and truncated forms. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, DNA interactions]


Pssm-ID: 273817 [Multi-domain]  Cd Length: 534  Bit Score: 325.90  E-value: 4.45e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  151 GIIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFT 230
Cdd:TIGR01817 197 GIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFT 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  231 GASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLY 310
Cdd:TIGR01817 277 GAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLY 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  311 YRLHVIALKLPALRERGSDVNEIANVFLARQSARIGRdDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISA 390
Cdd:TIGR01817 357 YRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGR-PLTITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITR 435
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
152-410 8.44e-105

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 323.77  E-value: 8.44e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 152 IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRaKAPMISVNCAAIPETLIESELFGHEKGAFTG 231
Cdd:NF041552 269 IIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGR-KGPFVPVNCSAIPEELFESEFFGYEEGAFTG 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 232 AS-AGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLY 310
Cdd:NF041552 348 ALkKGKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFREDLY 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 311 YRLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISA 390
Cdd:NF041552 428 YRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNGTITK 507
                        250       260
                 ....*....|....*....|
gi 489342835 391 ELLGIDIeLSDLEEDDILDN 410
Cdd:NF041552 508 DSIPEYI-LESVKKKEDEEG 526
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
152-457 1.52e-103

Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 318.67  E-value: 1.52e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 152 IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTG 231
Cdd:COG3283  206 IVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFGN 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 232 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYY 311
Cdd:COG3283  286 AREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLYY 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 312 RLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAE 391
Cdd:COG3283  366 RLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGDELTPE 445
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489342835 392 llgiDIELSDLEEDDILDnalvvanagnashEPTEDLSLEDYFQHF---VLE--HQDHMTETELARKLGVS 457
Cdd:COG3283  446 ----DLQLPEYAASAGLL-------------DDLLEGSLDEIVKRFersLLRrlYPSYPSTRKLAKRLGVS 499
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
151-474 4.65e-102

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 315.27  E-value: 4.65e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 151 GIIGSCQPMQDMYSKIRKVAPTD-SNVLIQGESGTGKELVARALHNLSRRA---KAPMISVNCAAIPETLIESELFGHEK 226
Cdd:NF038308 180 GIATRNAAFNRLIEQIERVALRSrAPILLTGPTGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMSELFGHVK 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 227 GAFTGASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFR 306
Cdd:NF038308 260 GAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFR 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 307 EDLYYRLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDDLhFSAEAEQ------AIRHYSWPGNVRELENAVERAV 380
Cdd:NF038308 340 EDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRQVR-FNKEARFrylafaTSPEALWPGNFRELSASVTRMA 418
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 381 ILSESAEISAELLgiDIELSDLEEDDildnalvvanagNASHEPTEDLSLEDYFQHFVLEHQDHMTETELARKLGVSRKC 460
Cdd:NF038308 419 TLADGGRITEELV--EEEIARLRAAW------------QSAPAAADDDALADLLGGEQLAELDLFDRVQLAAVLRVCRQS 484
                        330
                 ....*....|....*..
gi 489342835 461 LWER---RQRLGIPRRK 474
Cdd:NF038308 485 RSLSaagRRLFGVSRQQ 501
PRK15115 PRK15115
response regulator GlrR; Provisional
3-393 5.03e-99

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 304.84  E-value: 5.03e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPG----TELIKLGQGTPVLIMTSY 78
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGmqlfAEIQKVQPGMPVIILTAH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRqnapaaappaeprasngkATAPDKGSAATangeigIIGSCQP 158
Cdd:PRK15115  87 GSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQS------------------APATDERWREA------IVTRSPL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 159 MQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAG 238
Cdd:PRK15115 143 MLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREG 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 239 LVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIAL 318
Cdd:PRK15115 223 LFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSL 302
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489342835 319 KLPALRERGSDVNEIANvFLARQSARIGRDDLH-FSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELL 393
Cdd:PRK15115 303 KIPALAERTEDIPLLAN-HLLRQAAERHKPFVRaFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALV 377
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
152-380 8.89e-89

psp operon transcriptional activator PspF; Members of this protein family are PspF, the sigma-54-dependent transcriptional activator of the phage shock protein (psp) operon, in Escherichia coli and numerous other species. The psp operon is induced by a number of stress conditions, including heat shock, ethanol, and filamentous phage infection. Changed com_name to adhere to TIGR role notes conventions. 09/15/06 - DMH [Regulatory functions, DNA interactions]


Pssm-ID: 274371 [Multi-domain]  Cd Length: 329  Bit Score: 274.56  E-value: 8.89e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  152 IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTG 231
Cdd:TIGR02974   1 LIGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  232 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYY 311
Cdd:TIGR02974  81 AQKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLD 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  312 RLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDD-LHFSAEAEQAIRHYSWPGNVRELENAVERAV 380
Cdd:TIGR02974 161 RLAFDVITLPPLRERQEDIMLLAEHFAIRMARELGLPLfPGFTPQAREQLLEYHWPGNVRELKNVVERSV 230
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
133-467 7.82e-87

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 276.22  E-value: 7.82e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 133 GKATAPDKGSAATANG-----EIG-IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALH--------NLSR 198
Cdd:PRK15424 196 TRMTLRHNTHYATRNAlrtryVLGdLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHreyfarhdARQG 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 199 RAKAPMISVNCAAIPETLIESELFGHEKGAFTGAS-AGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVG 277
Cdd:PRK15424 276 KKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRrGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVG 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 278 SVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALKLPALRERGSDVNEIANVFLARQSARIgrdDLHFSAEAE 357
Cdd:PRK15424 356 GHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAAL---SAPFSAALR 432
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 358 Q-------AIRHYSWPGNVRELENAVERAVILsesaeISAELLGiDIELSDLEEddiLDNALVVANAGNAShEPTEDLSL 430
Cdd:PRK15424 433 QglqqcetLLLHYDWPGNVRELRNLMERLALF-----LSVEPTP-DLTPQFLQL---LLPELARESAKTPA-PRLLAATL 502
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 489342835 431 EDYFQHFvleHQDHmteTELARKLGVSRKCLWERRQR 467
Cdd:PRK15424 503 QQALERF---NGDK---TAAANYLGISRTTLWRRLKA 533
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
147-473 2.15e-83

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 271.32  E-value: 2.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 147 NGEIG-IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHE 225
Cdd:PRK15429 372 DSEFGeIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHE 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 226 KGAFTGASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQF 305
Cdd:PRK15429 452 RGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREF 531
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 306 REDLYYRLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSES 385
Cdd:PRK15429 532 RSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRG 611
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 386 AEisaellgIDIELSDLEeddildnALVVANAGNASHEPTEDlslEDYFQHFVLEhqdhMTETE--------LARKLGVS 457
Cdd:PRK15429 612 NV-------LQLSLPDIT-------LPEPETPPAATVVAQEG---EDEYQLIVRV----LKETNgvvagpkgAAQRLGLK 670
                        330
                 ....*....|....*.
gi 489342835 458 RKCLWERRQRLGIPRR 473
Cdd:PRK15429 671 RTTLLSRMKRLGIDKS 686
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
152-466 3.79e-83

propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists for the catabolism of propionate by way of propionyl-CoA. Members of this family represent the transcriptional regulatory protein PrpR, whose gene is found in most cases divergently transcribed from an operon for the methylcitric acid cycle of propionate catabolism. 2-methylcitric acid, a catabolite by this pathway, is a coactivator of PrpR. [Regulatory functions, DNA interactions]


Pssm-ID: 274079 [Multi-domain]  Cd Length: 526  Bit Score: 266.34  E-value: 3.79e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  152 IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTG 231
Cdd:TIGR02329 214 LLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTG 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  232 A-SAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLY 310
Cdd:TIGR02329 294 ArRGGRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLF 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  311 YRLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDD----LHFSAEAEQAIRHYSWPGNVRELENAVERAVIlsesa 386
Cdd:TIGR02329 374 YRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPDseaaAQVLAGVADPLQRYPWPGNVRELRNLVERLAL----- 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  387 EISAELLGidielsDLEEDDILDNALVVANAGNASHEPTEDLS----LEDYFQHFVLE-HQDHMTETelARKLGVSRKCL 461
Cdd:TIGR02329 449 ELSAMPAG------ALTPDVLRALAPELAEASGKGKTSALSLRersrVEALAVRAALErFGGDRDAA--AKALGISRTTL 520

                  ....*
gi 489342835  462 WERRQ 466
Cdd:TIGR02329 521 WRRLK 525
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
168-380 7.27e-77

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 243.42  E-value: 7.27e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 168 KVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEAADGGT 247
Cdd:PRK11608  24 RLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRFERADGGT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 248 LFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALKLPALRERG 327
Cdd:PRK11608 104 LFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQLPPLRERQ 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489342835 328 SDVNEIANVFlARQSARigrdDLH------FSAEAEQAIRHYSWPGNVRELENAVERAV 380
Cdd:PRK11608 184 SDIMLMAEHF-AIQMCR----ELGlplfpgFTERARETLLNYRWPGNIRELKNVVERSV 237
PRK10820 PRK10820
transcriptional regulator TyrR;
152-478 3.49e-76

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 247.68  E-value: 3.49e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 152 IIGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEKGAFTG 231
Cdd:PRK10820 206 IVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPN 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 232 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYY 311
Cdd:PRK10820 286 ALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYY 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 312 RLHVIALKLPALRERGSDVNEIANVFLARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAE 391
Cdd:PRK10820 366 RLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLEGYELRPQ 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 392 llgiDIELSDLE-----EDDILDNALvvanagnasheptEDLSleDYFQHFVLE--HQDHMTETELARKLGVSRKCLWER 464
Cdd:PRK10820 446 ----DILLPDYDaavavGEDAMEGSL-------------DEIT--SRFERSVLTrlYRNYPSTRKLAKRLGVSHTAIANK 506
                        330
                 ....*....|....
gi 489342835 465 RQRLGIPRRKSNAT 478
Cdd:PRK10820 507 LREYGLSQKKGEED 520
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
178-470 3.16e-71

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


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 229.35  E-value: 3.16e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 178 IQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESelfghekgaftgasagraglveaadggtlfldeigelp 257
Cdd:COG3604  120 ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 258 leaqarllrvLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALKLPALRERGSDVNEIANVF 337
Cdd:COG3604  162 ----------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHF 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 338 LARQSARIGRDDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEISAELL-GIDIELSDLEEDDILDNALvvan 416
Cdd:COG3604  232 LEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLaPGSREALEEVEREHILEAL---- 307
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489342835 417 agnasheptedlsledyfqhfvLEHQDHMTETelARKLGVSRKCLWERRQRLGI 470
Cdd:COG3604  308 ----------------------ERTGGNIAGA--ARLLGLTPSTLRSRMKKLGI 337
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
167-470 1.42e-51

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 184.88  E-value: 1.42e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 167 RKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGhekGAFTGASAGRAGLVEAADGG 246
Cdd:PRK11388 342 RQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SDRTDSENGRLSKFELAHGG 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 247 TLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIALKLPALRER 326
Cdd:PRK11388 419 TLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMR 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 327 GSDVNEIANVFLARQSARIGRdDLHFSAEAEQAIRHYSWPGNVRELENAVERAVILSESAEisaellgidIELSDLEEDD 406
Cdd:PRK11388 499 REDIPALVNNKLRSLEKRFST-RLKIDDDALARLVSYRWPGNDFELRSVIENLALSSDNGR---------IRLSDLPEHL 568
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489342835 407 ILDNalvVANAGNASHEPTeDLSLEDyFQHFVLEHQDHMTE---TELARKLGVSRKCLWERRQRLGI 470
Cdd:PRK11388 569 FTEQ---ATDDVSATRLST-SLSLAE-LEKEAIINAAQVCGgriQEMAALLGIGRTTLWRKMKQHGI 630
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
166-460 4.55e-50

Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 443688 [Multi-domain]  Cd Length: 534  Bit Score: 178.87  E-value: 4.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 166 IRKVAPtdsnVLIQGESGTGKELVARALHNL--SRRA-KAPMISVNCAaipeTL----IESELFGHEKGAFTGASAGRAG 238
Cdd:COG4650  205 IRSRAP----ILLTGPTGAGKSQLARRIYELkkARHQvSGRFVEVNCA----TLrgdgAMSALFGHVKGAFTGAVSDRAG 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 239 LVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKNLAKAGQFREDLYYRLHVIAL 318
Cdd:COG4650  277 LLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTF 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 319 KLPALRERGSDVNeiANV--FLARQSARIGRdDLHFSAEAEQAIRHY------SWPGNVRELENAVERAVILSESAEISA 390
Cdd:COG4650  357 RLPGLAERREDIE--PNLdyELARFAREQGR-RVRFNKEARARYLAFatspeaLWSGNFRDLNASVTRMATLAEGGRITV 433
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 391 ELlgIDIELSDLEEddildnalvvanAGNASHEPTEDLSLEDYFQHFVLEHQDHMTETELARKLGVSRKC 460
Cdd:COG4650  434 AL--VDEEIARLRR------------LWQRAEAATGDDLLAELLGAEQAAELDLFDRVQLAAVIRVCRRS 489
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
175-455 5.45e-39

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 150.64  E-value: 5.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 175 NVLIQGESGTGKELVARALHNLSRRAK-----APMISVNCAAI---PETLIeSELFGHEKGAFTGASAGRAGLVEAADGG 246
Cdd:COG1221  132 HTLILGPTGVGKSFFAELMYEYAIEIGvlpedAPFVVFNCADYannPQLLM-SQLFGYVKGAFTGADKDKEGLIEKADGG 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 247 TLFLDEIGELPLEAQARLLRVLQEGEIRRVG-SVQSQKVDVRLIAATHRDL-KNLAKAgqF-RedlyyRLHVIaLKLPAL 323
Cdd:COG1221  211 ILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPeSSLLKT--FlR-----RIPMV-IKLPSL 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 324 RERGsdVNE---IANVFLARQSARIGRdDLHFSAEAEQAIRHYSWPGNVRELENAV---------ERAVILSESAEISAE 391
Cdd:COG1221  283 EERS--LEErleLIKHFFKEEAKRLNK-PIKVSKEVLKALLLYDCPGNIGQLKSDIqlacakaflNYITNKKEEIEITLS 359
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 392 LLGIDI---------------ELSDLEEDDIldnaLVVANAGNASHEPTEDLSLEDYFQHFVLE-----HQDHMTETELA 451
Cdd:COG1221  360 DLPENVkkgllklkenreeldKLSEYLEEYL----IISPDTEKKLISEEDEYELPYNFYEIIEDkyeelKSEGLSEEEIN 435

                 ....
gi 489342835 452 RKLG 455
Cdd:COG1221  436 KIIS 439
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1-117 7.88e-30

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: 115.44  E-value: 7.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMT 76
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRrlraRPSDIPIIMLT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRA 121
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-118 4.83e-28

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: 108.01  E-value: 4.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL------GQGTPVLI 74
Cdd:COG0784    5 GKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRiralprLPDIPIIA 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489342835  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQN 118
Cdd:COG0784   85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
5-99 9.87e-28

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 106.16  E-value: 9.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTSYAS 80
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLrklrELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 489342835  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
159-316 1.60e-27

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 107.62  E-value: 1.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 159 MQDMYSKIRKVA--PTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESELFGHEkgaftgASAGR 236
Cdd:cd00009    3 QEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835 237 AGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVgsvqsQKVDVRLIAATHRDLknlakAGQFREDLYYRLHVI 316
Cdd:cd00009   77 FELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRI-----DRENVRVIGATNRPL-----LGDLDRALYDRLDIR 146
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
153-323 3.93e-25

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 100.49  E-value: 3.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  153 IGSCQPMQDMYSKIRKVAPTDSNVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIESelfghekgaftga 232
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  233 sagraglveaADGGTLFLDEIGELPLEAQARLLRVLQEGEirrvgsvqsqKVDVRLIAATHRDLKNLAKAGQFREDLYYR 312
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 489342835  313 LHVIALKLPAL 323
Cdd:pfam14532 128 LSALRLHVPPL 138
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1-114 4.55e-25

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: 101.52  E-value: 4.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL------GQGTPVLI 74
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRlradprTADIPIIF 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489342835  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVAR 120
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1-117 4.66e-25

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 102.94  E-value: 4.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL------GQGTPVLI 74
Cdd:COG3437    6 APTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLlradpsTRDIPVIF 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489342835  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:COG3437   86 LTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRR 128
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
2-112 4.98e-25

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: 101.15  E-value: 4.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTS 77
Cdd:COG4567    5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEalreRDPDARIVVLTG 84
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARI 112
Cdd:COG4567   85 YASIATAVEAIKLGADDYLAKPADADDLLAALERA 119
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
4-110 5.62e-25

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: 99.15  E-value: 5.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKrirrRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 489342835   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVA 110
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
2-108 1.50e-24

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: 97.90  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK-LGQGTP---VLIMTS 77
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPpLRALQPdarIVVLTG 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQA 108
Cdd:cd17563   81 YASIATAVEAIKLGADDYLAKPADADEILAA 111
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-117 6.71e-22

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 91.18  E-value: 6.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLI 74
Cdd:COG4565    3 MIRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLrelrARGPDVDVIV 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489342835  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRR 125
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
4-117 8.77e-22

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: 90.63  E-value: 8.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQGT----PVLIMTSYA 79
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELdpdlPVILITGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRR 118
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
3-117 1.13e-21

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: 92.47  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSY 78
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEelaaRGSPLPVIFLTGH 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489342835  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL-RDRQ 117
Cdd:COG4566   81 GDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALaRDRA 120
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
4-99 2.11e-21

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: 88.68  E-value: 2.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTS 77
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEaireLDPDTKIIILSG 81
                         90       100
                 ....*....|....*....|..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKP 99
Cdd:COG4753   82 YSDFEYAQEAIKLGADDYLLKP 103
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1-113 2.64e-21

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 89.08  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMT 76
Cdd:COG5803    2 MKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKeikeIDPDIPVIMMT 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:COG5803   82 AYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
5-99 5.78e-20

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: 84.38  E-value: 5.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYAS 80
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRrlreKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*....
gi 489342835  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
2-112 1.45e-19

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: 84.22  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK------LGQGTPVLIM 75
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRrlkrdeMTRDIPIIML 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  76 TSYASLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKPFSPREL---VARI 114
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
4-111 1.61e-19

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: 83.86  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI-KLGQ---GTPVLIMTSYA 79
Cdd:cd19919    3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLaQIKQrhpDLPVIIMTAHS 82
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVAR 111
Cdd:cd19919   83 DLDSAVSAYQGGAFEYLPKPFDIDEAVALVER 114
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
4-114 2.75e-19

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: 83.32  E-value: 2.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKeikeKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
4-114 3.06e-19

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 83.16  E-value: 3.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQY---QVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMT 76
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELgfeVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEkireLYPDIKIIILS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489342835  77 SYAS---LRSAvdsMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17536   81 GYDDfeyAQKA---IRLGVVDYLLKPVDEEELEEALEKAKE 118
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
2-114 9.55e-19

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 81.68  E-value: 9.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTE-LIKLGQGTPV---LIMTS 77
Cdd:cd17569    1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAElLKRVRERYPDtvrILLTG 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489342835  78 YASLRSAVDSMKMGAVD-YIAKPFDHDEMLQAVARILR 114
Cdd:cd17569   81 YADLDAAIEAINEGEIYrFLTKPWDDEELKETIRQALE 118
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
4-114 2.53e-18

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: 80.63  E-value: 2.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQ----GTPVLIMTS 77
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEPdiEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRrrypDLKVIVLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
4-117 4.42e-18

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: 79.93  E-value: 4.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQG----TPVLIMTSYA 79
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQErslpTSVIVITAHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRK 118
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
4-111 6.25e-18

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 79.45  E-value: 6.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL----GQGTPVLIMTSYA 79
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRwrrqGQSLPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEM---LQAVAR 111
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEELlarLRALLR 115
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
2-109 7.98e-18

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 79.17  E-value: 7.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPG----TELIKLGQGTPVLIMTS 77
Cdd:cd17537    1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGlelqDELLARGSNIPIIFITG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17537   81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAI 112
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
3-113 9.61e-18

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: 78.88  E-value: 9.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK------LGQGTPVLIMT 76
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKelrklpAYKFTPILMLT 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489342835  77 SYASlrsavDSMKM-----GAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17562   82 TESS-----DEKKQegkaaGATGWLVKPFDPEQLLEVVKKVL 118
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1-114 1.25e-17

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 81.79  E-value: 1.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLER-NQYQ-VSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLI 74
Cdd:COG3279    1 MMKILIVDDEPLARERLERLLEKyPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARqlreLDPPPPIIF 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489342835  75 MTSYASLrsAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:COG3279   81 TTAYDEY--ALEAFEVNAVDYLLKPIDEERLAKALEKAKE 118
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
2-111 2.80e-17

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: 77.63  E-value: 2.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTS 77
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKqitkESPDTPVIVVSG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEML-QAVAR 111
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKPIEDLAVLeHAVRR 115
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
4-116 6.61e-17

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: 76.55  E-value: 6.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRrwrsEGRATPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFdHDEMLQAVARILRDR 116
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPF-HIEELLARLRALIRR 116
fixJ PRK09390
response regulator FixJ; Provisional
2-114 7.27e-17

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 78.89  E-value: 7.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTS 77
Cdd:PRK09390   4 GVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRrlkaRGSPLPVIVMTG 83
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:PRK09390  84 HGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALA 120
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
5-114 1.74e-16

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: 75.34  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL----GQGTPVLIMTSYAS 80
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSlreeGIETPVLLLTALDA 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489342835  81 LRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELLARIRALLR 114
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
4-100 1.08e-15

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: 72.54  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTE---LIK---LGQGTPVLIMTS 77
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEvcrRLKadpATRHIPVIFLTA 80
                         90       100
                 ....*....|....*....|...
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPF 100
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
PRK10643 PRK10643
two-component system response regulator PmrA;
4-118 1.39e-15

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 75.84  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTSYA 79
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLrrwrQKKYTLPVLILTARD 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQN 118
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQG 121
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
4-109 6.16e-15

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: 70.96  E-value: 6.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL-------GQGTPVLIMT 76
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRireleggGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
4-99 9.60e-15

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: 69.87  E-value: 9.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQ----GTPVLIMTSYA 79
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQqrlpQTPVAVITAYG 80
                         90       100
                 ....*....|....*....|
gi 489342835  80 SLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
4-109 1.96e-14

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 69.41  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL------GQGTPVLIMTS 77
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRlrelpwLANTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
5-114 2.24e-14

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: 69.22  E-value: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL------GQGTPVLIMTSY 78
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRIlrsdpkTSSIPIIMLTAK 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489342835  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVLR 116
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
2-113 2.43e-14

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 69.23  E-value: 2.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQ-VSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMT 76
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEvVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKeikkIDPNAKVIMCS 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17542   81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
2-114 6.73e-14

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


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 70.82  E-value: 6.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835    2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK------LGQGTPVLIM 75
Cdd:TIGR02154   3 RRILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRrlrrrpETRAIPIIML 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 489342835   76 TSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:TIGR02154  83 TARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLR 121
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
4-99 7.46e-14

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: 67.08  E-value: 7.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRrlraAGKQTPVLMLTARD 80
                         90       100
                 ....*....|....*....|
gi 489342835  80 SLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVKP 100
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
2-112 1.12e-13

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


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 67.47  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQY-QVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL------GQGTPVLI 74
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRlralpgLEDVPIVM 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489342835  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLqavARI 112
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPFDPVELL---ARV 115
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
4-111 1.26e-13

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: 67.18  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQG------TPVLIMTS 77
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEdpatrdIPVIALTA 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVAR 111
Cdd:cd17548   82 YAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
2-106 1.38e-13

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: 67.03  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK-LGQGTPV-LIMTSya 79
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTReLREQSEVgIILVT-- 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 489342835  80 SLRSAVD---SMKMGAVDYIAKPFDHDEML 106
Cdd:cd17619   79 GRDDEVDrivGLEIGADDYVTKPFNPRELL 108
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
4-113 1.73e-13

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: 66.81  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKrmkvIDENIRVIIMTAYG 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17553   83 ELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
4-114 1.74e-13

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 66.64  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTE----LIKLGQGTPVLIMTSYA 79
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEvcrrLRAAGNDLPILVLTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEELLARVRALLR 115
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
2-112 2.13e-13

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: 66.48  E-value: 2.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTS 77
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLrkirEKKPDLPVIICTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  78 YASLRSavDSMKMGAVDYIAKPFDHDEMLQAVARI 112
Cdd:cd17554   81 YSEYKS--DFSSWAADAYVVKSSDLTELKETIKRL 113
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
4-99 2.63e-13

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 65.65  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQG---TPVLIMTSYAS 80
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREwsaVPVIVLSARDE 80
                         90
                 ....*....|....*....
gi 489342835  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd17620   81 ESDKIAALDAGADDYLTKP 99
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
2-109 3.81e-13

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: 65.89  E-value: 3.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSE-AGSVQEAQERFSIATFDLIVSDLRLPGAP-GTEL---IKLGQGTPVLIMT 76
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKGDMdGIEAareIREKFDIPVIFLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489342835  77 SYAS---LRSAvdsMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17534   81 AYSDeetLERA---KETNPYGYLVKPFNERELKAAI 113
ompR PRK09468
osmolarity response regulator; Provisional
1-117 7.07e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 68.08  E-value: 7.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPG----TELIKLGQGTPVLIMT 76
Cdd:PRK09468   5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGlsicRRLRSQNNPTPIIMLT 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRdRQ 117
Cdd:PRK09468  85 AKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLR-RQ 124
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
3-100 1.35e-12

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: 63.67  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL---IKLGQGT---PVLIMT 76
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVcrrLKEDPETrhiPVIMIT 80
                         90       100
                 ....*....|....*....|....
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPF 100
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
4-113 2.10e-12

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: 63.90  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQ-VSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQ------GTPVLIMT 76
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRadgalsHLPVLMVT 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd19923   83 AEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
4-99 2.18e-12

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: 62.99  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQGT---PVLIMTSYAS 80
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARsnvPVIMVTAKDS 80
                         90
                 ....*....|....*....
gi 489342835  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd17621   81 EIDKVVGLELGADDYVTKP 99
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
4-113 3.45e-12

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 63.11  E-value: 3.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL---IKLGQG---TPVLIMTS 77
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELcrkIKSDPDlkdIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
175-295 3.96e-12

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 63.93  E-value: 3.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   175 NVLIQGESGTGKELVARALHNLSRRAKAPMISVNCAAIPETLIES---ELFGHEKGAFTGASAGRAG--LVEAADGGTLF 249
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 489342835   250 LDEIGELPLEAQARLLRVLQEgeiRRVGSVQSQKVDVRLIAATHRD 295
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTNDE 126
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
4-113 4.63e-12

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 62.68  E-value: 4.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPG---TELIKLGQGTPVLIMTSYAS 80
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGfywCREIRQISNVPIIFISSRDD 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489342835  81 LRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd18159   81 NMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
3-114 4.73e-12

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: 62.78  E-value: 4.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL---IKLGQGTPVLIMTSYA 79
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVcreVREHSHVPILMLTART 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd19939   81 EEMDRVLGLEMGADDYLCKPFSPRELLARVRALLR 115
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
4-114 7.39e-12

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: 62.06  E-value: 7.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL---IKLGQGTPVLIMTSYAS 80
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVcreVRKTSNVPIIMLTAKDS 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489342835  81 LRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17614   81 EVDKVLGLELGADDYVTKPFSNRELLARVKANLR 114
PRK10766 PRK10766
two-component system response regulator TorR;
3-113 7.47e-12

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 64.67  E-value: 7.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK--LGQGTPVLIMTSYAS 80
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRelRSRSTVGIILVTGRT 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489342835  81 lrSAVD---SMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:PRK10766  84 --DSIDrivGLEMGADDYVTKPLELRELLVRVKNLL 117
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
4-114 9.98e-12

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 64.74  E-value: 9.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK------LGQGTPVLIMTS 77
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKhlkresMTRDIPVVMLTA 84
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
4-99 1.05e-11

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: 61.24  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI-KLGQGT-----PVLIMTS 77
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLgKLRKNAdfdtiPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
2-56 1.46e-11

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: 59.50  E-value: 1.46e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489342835     2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLP 56
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
4-117 2.69e-11

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: 60.63  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLER-NQYQ-VSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL--GQGTPVLIM--TS 77
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEhPDIEiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKlsKLAKPPLIVfvTA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489342835  78 YASLrsAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:cd17532   81 YDEY--AVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
PRK11173 PRK11173
two-component response regulator; Provisional
2-116 2.91e-11

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 63.50  E-value: 2.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK-LGQGTPVLIMtsYAS 80
Cdd:PRK11173   4 PHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLAReLREQANVALM--FLT 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489342835  81 LR-SAVD---SMKMGAVDYIAKPFDHDEmLQAVARILRDR 116
Cdd:PRK11173  82 GRdNEVDkilGLEIGADDYITKPFNPRE-LTIRARNLLSR 120
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
3-109 3.03e-11

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 60.15  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL---GQGTPVLIMTSYA 79
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTiraRSDVPIIIISGDR 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489342835  80 SLRSAVD-SMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17594   81 RDEIDRVvGLELGADDYLAKPFGLRELLARV 111
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-104 3.34e-11

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: 60.23  E-value: 3.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEA----QERFSIatfDLIVSDLRLPGAPGTELIKlgqgtpvLIMTSY 78
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEAlevlEQHPDI---KLVITDYNMPEMDGFELVR-------EIRKKY 71
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489342835  79 ASLR------SAVDS-------MKMGAVDYIAKPFDHDE 104
Cdd:cd17544   72 SRDQlaiigiSASGDnalsarfIKAGANDFLTKPFLPEE 110
orf27 CHL00148
Ycf27; Reviewed
3-118 3.74e-11

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 63.20  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL---IKLGQGTPVLIMTSYA 79
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVcqeIRKESDVPIIMLTALG 87
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQN 118
Cdd:CHL00148  88 DVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNK 126
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1-114 4.20e-11

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 62.51  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK-LGQ--GTPVLIMTS 77
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRdLRQwsAIPVIVLSA 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:PRK10529  81 RSEESDKIAALDAGADDYLSKPFGIGELQARLRVALR 117
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
4-114 5.73e-11

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 62.25  E-value: 5.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL----GQGTPVLIMTSYA 79
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMlrsaNKGMPILLLTALG 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:PRK09836  83 TIEHRVKGLELGADDYLVKPFAFAELLARVRTLLR 117
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
3-111 5.86e-11

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: 59.57  E-value: 5.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMT 76
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEQVPGftVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLrelrAAGHDVDVIVVT 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVAR 111
Cdd:cd19925   82 AANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
4-112 8.02e-11

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: 58.96  E-value: 8.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQG----TPVLIMTSYA 79
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLakvkTPILILSGLA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDEL---VARI 110
PRK14084 PRK14084
DNA-binding response regulator;
4-118 8.72e-11

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 62.08  E-value: 8.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL---IKLGQGTPVLIMTSy 78
Cdd:PRK14084   3 ALIVDDEPLARNELTYLLNEIGGfeEINEAENVKETLEALLINQYDIIFLDINLMDESGIELaakIQKMKEPPAIIFAT- 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489342835  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQN 118
Cdd:PRK14084  82 AHDQFAVKAFELNATDYILKPFEQKRIEQAVNKVRATKAK 121
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
4-109 9.07e-11

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 58.96  E-value: 9.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQV-SEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTE---LIKLGQGTPVLIMTSYA 79
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEaakIITSENIAPIVLLTAYS 82
                         90       100       110
                 ....*....|....*....|....*....|
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd19932   83 QQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
4-105 1.13e-10

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 58.79  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQE--RFSIATFDLIVSDLRLPGAPG---TELIKLGQGTPVLIMTSY 78
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSmlRENKDEFDLVITDVHMPDMDGfefLELIRLEMDLPVIMMSAD 80
                         90       100
                 ....*....|....*....|....*..
gi 489342835  79 ASLRSAVDSMKMGAVDYIAKPFDHDEM 105
Cdd:cd17584   81 GSTSTVMKGLAHGACDYLLKPVSIEDL 107
PRK10336 PRK10336
two-component system response regulator QseB;
4-112 1.31e-10

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 61.06  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILRewreKGQREPVLILTARD 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFdhdEMLQAVARI 112
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPF---ALIEVAARL 112
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
4-114 1.99e-10

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: 59.97  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQV-SEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQGT---PVLIMTSYA 79
Cdd:COG3707    6 VLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEErpaPVILLTAYS 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:COG3707   86 DPELIERALEAGVSAYLVKPLDPEDLLPALELALA 120
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1-114 4.95e-10

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 59.82  E-value: 4.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSiATFDLIVSDLRLPGAPGTELIK---LGQGTPVLIMTS 77
Cdd:PRK10955   1 MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKelrQTHQTPVIMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAILR 116
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
4-112 5.20e-10

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 56.67  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQG----TPVLIMTSYA 79
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEkhpsIVVIVLSDNP 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVL---VARI 110
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1-65 7.33e-10

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 56.82  E-value: 7.33e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK 65
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALR 67
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
4-116 8.29e-10

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: 56.63  E-value: 8.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERN-QYQV-SEAGSVQEAQERFSIATFDLIVSDLRLPGAPG---TELIKLGQGTPVLIMTSY 78
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILESDpDIEVvGTARDGEEALEKIKELKPDVITLDIEMPVMDGleaLRRIMAERPTPVVMVSSL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489342835  79 ASLRSAV--DSMKMGAVDYIAKPFDH-DEMLQAVARILRDR 116
Cdd:cd17541   83 TEEGAEItlEALELGAVDFIAKPSGGiSLDLEEIAEELIEK 123
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
4-114 1.09e-09

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: 55.82  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTSYA 79
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRrlraDGPDVPVLFLTAKD 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLR 116
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
4-112 1.58e-09

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: 55.55  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTE---LIKLGQGTPVLIMTSYAS 80
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEvcrQIRAESGVPIVMLTAKSD 82
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489342835  81 LRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17626   83 TVDVVLGLESGADDYVAKPFKPKEL---VARI 111
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-117 2.24e-09

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 57.66  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK--LGQGT--PVLIMT 76
Cdd:PRK11083   3 QPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRqlLAFHPalPVIFLT 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489342835  77 SyaslRSA-VD---SMKMGAVDYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:PRK11083  83 A----RSDeVDrlvGLEIGADDYVAKPFSPREVAARVRTILRRVK 123
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
4-99 3.12e-09

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 54.33  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEA-----QERFSIatfDLIVSDLRLPGAPGTELIKL------GQGTPV 72
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAwdvleDEQNEI---DLILTEVDLPVSSGFKLLSYimrhkiCKNIPV 77
                         90       100
                 ....*....|....*....|....*..
gi 489342835  73 LIMTSYASLRSAVDSMKMGAVDYIAKP 99
Cdd:cd17582   78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
4-100 4.98e-09

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: 53.66  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERF-SIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTSY 78
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELArearKIDPDVKILFISGG 81
                         90       100
                 ....*....|....*....|..
gi 489342835  79 ASLRSAVDSMKMGAVDYIAKPF 100
Cdd:cd18160   82 AAAAPELLSDAVGDNATLKKPF 103
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
3-113 7.07e-09

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 53.54  E-value: 7.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL---IKLGQGTPVLIMTSYA 79
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLcreIRRFSDVPIIMVTARV 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd19938   81 EEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
175-302 8.48e-09

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 53.84  E-value: 8.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  175 NVLIQGESGTGK-ELVARALHNLSRRAKAPMisvncaAIPETLIESELFGH-----EKGAFTGASAGRAglveAADGGTL 248
Cdd:pfam07728   1 GVLLVGPPGTGKtELAERLAAALSNRPVFYV------QLTRDTTEEDLFGRrnidpGGASWVDGPLVRA----AREGEIA 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  249 FLDEIGELPLEAQARLLRVLQEGEIR---RVGSVQSQKVDVRLIAATH---RDLKNLAKA 302
Cdd:pfam07728  71 VLDEINRANPDVLNSLLSLLDERRLLlpdGGELVKAAPDGFRLIATMNpldRGLNELSPA 130
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
4-99 8.97e-09

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 52.89  E-value: 8.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTSYA 79
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIprikKARPDLPIIVMSAQN 80
                         90       100
                 ....*....|....*....|
gi 489342835  80 SLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
2-117 9.55e-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: 53.91  E-value: 9.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLErNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQG---TPV-LIMTS 77
Cdd:cd17596    1 PTILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRErwpEVVrIIISG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489342835  78 YASLRSAVDSMKMGAV-DYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:cd17596   80 YTDSEDIIAGINEAGIyQYLTKPWHPDQLLLTVRNAARLFE 120
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
4-114 1.01e-08

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: 53.08  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK-LGQGT--PVLIMTSYAS 80
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKeLRKTSqvPVLMLTARGD 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489342835  81 LRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17623   81 DIDRILGLELGADDYLPKPFNPRELVARIRAILR 114
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
4-99 1.24e-08

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 52.77  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIA---------TFDLIVSDLRLPGAPGTELIKLGQGTP--- 71
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlskELDLIITDIEMPKMDGYELTFELRDDPrla 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489342835  72 ---VLIMTSYASLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19924   81 nipVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
3-113 1.95e-08

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: 52.55  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLER-NQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK------LGQGTPVLIM 75
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEKlAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKklqanpETQSIPVILL 82
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489342835  76 TSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17552   83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
4-100 2.45e-08

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 51.58  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERF-SIATFDLIVSDLRLPGAP-GTELIK----LGQGTPVLIMTS 77
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLeSGPDIDLLVTDVIMPGGMnGSQLAEearrRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|...
gi 489342835  78 YASLRSAVDSMKMGaVDYIAKPF 100
Cdd:cd18161   81 YAENAIEGGDLAPG-VDVLSKPF 102
PRK10610 PRK10610
chemotaxis protein CheY;
5-113 3.12e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 52.28  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   5 LIVEDETIIRSALRRLL-ERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQG------TPVLIMTS 77
Cdd:PRK10610   9 LVVDDFSTMRRIVRNLLkELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRAdgamsaLPVLMVTA 88
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:PRK10610  89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIF 124
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-114 3.23e-08

first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 51.80  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERN-QYQVSEAGSVQEAQERFSIAT-FDLIVSDLRLPGAPGTELIK--LGQGTPVLIMTSY 78
Cdd:cd19921    1 KVLIVEDSKTFSKVLKHLIAQElGLEVDVAETLAEAKALLEEGDdYFAALVDLNLPDAPNGEAVDlvLEKGIPVIVLTGS 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489342835  79 --ASLRSAVdsMKMGAVDYIAKpfDHDEMLQAVARILR 114
Cdd:cd19921   81 fdEDKRETL--LSKGVVDYVLK--DSRYSYDYVVKLVR 114
PRK10816 PRK10816
two-component system response regulator PhoP;
4-111 4.00e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 53.97  E-value: 4.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQGT----PVLIMTSYA 79
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNdvslPILVLTARE 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEM---LQAVAR 111
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPFHIEEVmarMQALMR 117
PRK15479 PRK15479
transcriptional regulator TctD;
4-116 4.07e-08

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 53.57  E-value: 4.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI----KLGQGTPVLIMTSYA 79
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLqrlrKRGQTLPVLLLTARS 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEmLQAVARILRDR 116
Cdd:PRK15479  83 AVADRVKGLNVGADDYLPKPFELEE-LDARLRALLRR 118
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1-118 1.80e-07

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 52.12  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK-LGQGTPV-LIMTSY 78
Cdd:PRK13856   1 MKHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRsLATKSDVpIIIISG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489342835  79 ASLRSA--VDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQN 118
Cdd:PRK13856  81 DRLEEAdkVVALELGATDFIAKPFGTREFLARIRVALRVRPN 122
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
4-99 2.41e-07

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 48.60  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI-KLGQGT--PVLIMTSYAS 80
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLqRLRQKStlPVIFLTSKDD 80
                         90
                 ....*....|....*....
gi 489342835  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd19936   81 EIDEVFGLRMGADDYITKP 99
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
3-112 2.79e-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: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDE----TIIRSALRRLLERNQYQVSEAGsvQEA------QERFSIATF-DLIVSDLRLPGAPGTEL---IKLGQ 68
Cdd:cd17557    1 TILLVEDNpgdaELIQEAFKEAGVPNELHVVRDG--EEAldflrgEGEYADAPRpDLILLDLNMPRMDGFEVlreIKADP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489342835  69 GT---PVLIMTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARI 112
Cdd:cd17557   79 DLrriPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSL 125
PRK11517 PRK11517
DNA-binding response regulator HprR;
4-114 1.55e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 49.13  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK---LGQGTPVLIMTSYAS 80
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQtlrTAKQTPVICLTARDS 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489342835  81 LRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:PRK11517  83 VDDRVRGLDSGANDYLVKPFSFSELLARVRAQLR 116
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
4-107 1.57e-06

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 46.87  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLER-NQYQVSEAGSVQEAQERFSIATFDLIVSDLRL-PGAPGTELI------KLGQGTPVLIM 75
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSlGVTRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLeelrhkKLISPSTVFIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489342835  76 TSYASLRSAVdsmkMGAV-----DYIAKPFDHDEMLQ 107
Cdd:cd17589   81 VTGESSRAMV----LSALelepdDYLLKPFTVSELRE 113
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
4-114 2.04e-06

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: 46.60  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPG----TELIKLGQGtPVLIMTSYA 79
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGltlcRDLRPKYQG-PILLLTALD 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd17622   82 SDIDHILGLELGADDYVVKPVEPAVLLARLRALLR 116
PRK13435 PRK13435
response regulator; Provisional
1-112 6.90e-06

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 45.81  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVS-EAGSVQEAQERFSIATFDLIVSDLRLP-GAPGTE----LIKLGqGTPVLI 74
Cdd:PRK13435   5 QLKVLIVEDEALIALELEKLVEEAGHEVVgIAMSSEQAIALGRRRQPDVALVDVHLAdGPTGVEvarrLSADG-GVEVVF 83
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489342835  75 MTsyASLRSAVDSMKmGAVDYIAKPFDHDEMLQAVARI 112
Cdd:PRK13435  84 MT--GNPERVPHDFA-GALGVIAKPYSPRGVARALSYL 118
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
4-113 1.16e-05

phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response regulators; This subfamily is composed of stand-alone response regulators (RRs) containing the PFxFATG[G/Y] motif; RRs with such a motif are also called ''FAT GUY'' response regulators. Included in this subfamily are Sphingomonas melonis SdrG, Sinorhizobium meliloti Sma0114, and Erythrobacter litoralis EL_LovR. SdrG is involved in the control of the general stress response. Sma0114 is part of the Sma0113/Sma0114 two-component system (TCS) that is involved in catabolite repression and polyhydroxy butyrate synthesis. EL_LovR is involved in a light-regulated TCS. PFxFATG[G/Y] RRs are typically associated with histidine-tryptophan-glutamate (HWE) histidine kinases that constitute a subclass of the larger histidine kinase superfamily characterized by an altered ATP binding site, which lacks the F-box that is normally an integral component of the ATP lid. The PFxFATG[G/Y] motif is involved in conformational changes after phosphorylation that results in the activation of the RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 44.38  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQ-VSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL--IKLGQGTPVLIMTSYAS 80
Cdd:cd17586    1 VLVLEDEPLIAMNLEDALEDLGGKeVVTAATCAEALRSLADGPIDIAILDVNLGGETSIPVadALKRRAIPFIFATGYGD 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489342835  81 lRSAVDSMKMGaVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17586   81 -SHGIDSRLID-VPVLRKPFDADSALAALAMLL 111
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
4-114 1.47e-05

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 44.19  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPG----TELIKLGQGTPVLIMTS 77
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGlevaAELREELPDTKVLIVTT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489342835  78 YAS---LRSAVDSmkmGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:cd19930   81 FGRpgyFRRALAA---GVDGYVLKDRPIEELADAIRTVHA 117
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
2-109 1.92e-05

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 43.78  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQV-SEAGSVQEAQERFSIATFDLIVSDLRLP-GAPGTELIKLGQGT---PVLIMT 76
Cdd:cd17540    1 TRVLIIEDEPLIAMDLEQIVEDLGHQVvGIARTRDEAVALARRERPDLILADIQLAdGSSGIDAVNEILTThdvPVIFVT 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  77 SY--ASLRSAvdsmKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17540   81 AYpeRLLTGE----RPEPTFLITKPFDPEMVKAAI 111
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
4-99 1.98e-05

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 43.89  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQE-----------RFSIATFDLIVSDLRLPGAPGTELIKLGQGT-- 70
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEflgledeedssNFNEPKVNMIITDYCMPGMTGYDLLKKVKESsa 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489342835  71 ----PVLIMTSYASLRSAVDSMKMGAVDYIAKP 99
Cdd:cd17581   81 lkeiPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
4-114 4.74e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 45.26  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERN-QYQVS-EAGSVQEAQERFSIATFDLIVSDLRLP---GAPGTELIKLGQGTPVLIMTSY 78
Cdd:PRK12555   3 IGIVNDSPLAVEALRRALARDpDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPrmdGVEATRRIMAERPCPILIVTSL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489342835  79 --ASLRSAVDSMKMGAVDYIAKPF--DHDEMLQAVARILR 114
Cdd:PRK12555  83 teRNASRVFEAMGAGALDAVDTPTlgIGAGLEEYAAELLA 122
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
4-113 7.07e-05

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 44.10  E-value: 7.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK----LGQGTPVLIMTS 77
Cdd:PRK09935   6 VIIMDTHPIIRMSIEVLLQKNSelQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKrikqIQSTVKVLFLSS 85
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:PRK09935  86 KSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMIL 121
PRK09483 PRK09483
response regulator; Provisional
1-109 7.86e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 43.94  E-value: 7.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLE--RNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTE----LIKLGQGTPVLI 74
Cdd:PRK09483   1 MINVLLVDDHELVRAGIRRILEdiKGIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEatrkILRYTPDVKIIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489342835  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:PRK09483  81 LTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAI 115
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
2-114 7.96e-05

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 43.91  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   2 PHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTEL---IKLGQGTPVLIMTSY 78
Cdd:PRK10710  11 PRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLcreIRRFSDIPIVMVTAK 90
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489342835  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILR 114
Cdd:PRK10710  91 IEEIDRLLGLEIGADDYICKPYSPREVVARVKTILR 126
PLN03029 PLN03029
type-a response regulator protein; Provisional
3-99 2.22e-04

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 42.71  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFD--------------------LIVSDLRLPGAPGTE 62
Cdd:PLN03029  10 HVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDrsnpdtpsvspnshqevevnLIITDYCMPGMTGYD 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489342835  63 LIKLGQGT------PVLIMTSYASLRSAVDSMKMGAVDYIAKP 99
Cdd:PLN03029  90 LLKKIKESsslrniPVVIMSSENVPSRITRCLEEGAEEFFLKP 132
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
4-113 2.56e-04

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 40.79  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKL----GQGTPVLIMTS 77
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDftVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKAlreeGVSARIVILTV 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489342835  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd19931   81 SDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAA 116
dpiA PRK10046
two-component response regulator DpiA; Provisional
4-117 2.75e-04

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 42.31  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSA----LRRLLERNQYQVseAGSVqeAQERFSIATFD--LIVSDLRLPGAPGT----ELIKLGQGTPVL 73
Cdd:PRK10046   7 LLIVEDETPLAEMhaeyIRHIPGFSQILL--AGNL--AQARMMIERFKpgLILLDNYLPDGRGInllhELVQAHYPGDVV 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489342835  74 IMTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILRDRQ 117
Cdd:PRK10046  83 FTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKH 126
PRK15369 PRK15369
two component system response regulator;
4-98 2.91e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 41.99  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLE---RNQY--QVSEAGSVQEAQERFSIatfDLIVSDLRLPGAPGTELI-KLGQGTP---VLI 74
Cdd:PRK15369   6 ILLVDDHELIINGIKNMLApypRYKIvgQVDNGLEVYNACRQLEP---DIVILDLGLPGMNGLDVIpQLHQRWPamnILV 82
                         90       100
                 ....*....|....*....|....
gi 489342835  75 MTSYASLRSAVDSMKMGAVDYIAK 98
Cdd:PRK15369  83 LTARQEEHMASRTLAAGALGYVLK 106
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
176-294 3.78e-04

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 40.27  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  176 VLIQGESGTGKELVARAlhnLSRRAKAPMISVNCaaipetlieSELFGHEKGAFTGASAGRAGLVEAADGGTLFLDEI-- 253
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKA---VAKELGAPFIEISG---------SELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIda 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489342835  254 ---------GELPLEAQARLLRVLQEgeirrvgsVQSQKVDVRLIAATHR 294
Cdd:pfam00004  69 lagsrgsggDSESRRVVNQLLTELDG--------FTSSNSKVIVIAATNR 110
PRK13557 PRK13557
histidine kinase; Provisional
3-113 4.04e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 42.74  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERF-SIATFDLIVSDLRLPGA-PGTELI----KLGQGTPVLIMT 76
Cdd:PRK13557 417 TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPGGmNGVMLArearRRQPKIKVLLTT 496
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489342835  77 SYAslRSAVDSMKMGA--VDYIAKPFDHDEMLQAVARIL 113
Cdd:PRK13557 497 GYA--EASIERTDAGGseFDILNKPYRRAELARRVRMVL 533
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
5-109 6.33e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 41.03  E-value: 6.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   5 LIVEDETIIRSALRRLLERNQYQV-SEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI---KLGQGTPVLIMTS--- 77
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEIlAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLetlRKRQYSGIIIIVSakn 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489342835  78 --YASLRSAvdsmKMGAVDYIAKPFDHDEMLQAV 109
Cdd:PRK09958  84 dhFYGKHCA----DAGANGFVSKKEGMNNIIAAI 113
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
427-474 1.56e-03

RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the presumed domain. The domain is found in algal minus dominance proteins as well as plant proteins involved in nitrogen-controlled development.


Pssm-ID: 460427  Cd Length: 49  Bit Score: 36.33  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489342835  427 DLSLEDYFQHFvlehqdHMTETELARKLGVSRKCLWERRQRLGIPR---RK 474
Cdd:pfam02042   1 SITLEDLSQYF------HLPIKEAAKELGVSLTTLKRICRRLGIPRwphRK 45
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
29-114 1.83e-03

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 40.99  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835  29 SEAGSVQEAQERfsiaTFDLIVSDLRLPGAPG---TELIK---LGQGTPVLIMTSYAS-------LRSAVDsmkmgavDY 95
Cdd:PRK11107 699 SGHQAVEQAKQR----PFDLILMDIQMPGMDGiraCELIRqlpHNQNTPIIAVTAHAMagererlLSAGMD-------DY 767
                         90
                 ....*....|....*....
gi 489342835  96 IAKPFDhDEMLQAVarILR 114
Cdd:PRK11107 768 LAKPID-EAMLKQV--LLR 783
PRK10430 PRK10430
two-component system response regulator DcuR;
1-100 1.90e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 39.71  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLErnqyQVS------EAGSVQEAQERFSIAT--FDLIVSDLRLPGAPGTELI----KLGQ 68
Cdd:PRK10430   1 MINVLIVDDDAMVAELNRRYVA----QIPgfqccgTASTLEQAKEIIFNSDtpIDLILLDIYMQQENGLDLLpvlhEAGC 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489342835  69 GTPVLIMTSYASLRSAVDSMKMGAVDYIAKPF 100
Cdd:PRK10430  77 KSDVIVISSAADAATIKDSLHYGVVDYLIKPF 108
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
4-65 4.09e-03

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 39.72  E-value: 4.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489342835    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIK 65
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTR 1022
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
4-99 4.25e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 36.87  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   4 ILIVEDETIIRSALRRLLE--RNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELI-KLGQG--TPVLIMTSY 78
Cdd:cd17565    1 FYIVDDDKNIIKILSDIIEddDLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVrKLKDTgsNGKFIMISQ 80
                         90       100
                 ....*....|....*....|..
gi 489342835  79 ASLRSAVDSMKMGAVD-YIAKP 99
Cdd:cd17565   81 VSDKEMIGKAYQAGIEfFINKP 102
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
3-109 4.82e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 38.29  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   3 HILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPG----TELIKLGQGTPVLIMT 76
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELDPGfeVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGldtlNALRRDGVTAQIIILT 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489342835  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:PRK10403  88 VSDASSDVFALIDAGADGYLLKDSDPEVLLEAI 120
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1-98 6.42e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 38.08  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489342835   1 MPHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERFSIATFDLIVSDLRLPGAPGTELIKLGQGT---PVLIMTS 77
Cdd:PRK10701   1 MNKIVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKwqgPIVLLTS 80
                         90       100
                 ....*....|....*....|.
gi 489342835  78 YASLRSAVDSMKMGAVDYIAK 98
Cdd:PRK10701  81 LDSDMNHILALEMGACDYILK 101
 
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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