NCBI Conserved Domain Search

Conserved domains on [gi|499656124|ref|WP_011336858|]

View

sigma-54 dependent transcriptional regulator [Cereibacter sphaeroides]

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

CATH: 3.40.50.2300

Gene Ontology: GO:0006355|GO:0005524|GO:0000160|GO:0000156|GO:0003677

PubMed: 8830233|20226724|12618438|10966457

SCOP: 4003632

Graphical summary

Zoom to residue level

show extra options »

Show site features Horizontal zoom: ×

List of domain hits

Name

Accession

Description

Interval

E-value

AtoC

COG2204

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...

25-483

4.84e-169

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: 482.54 E-value: 4.84e-169

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  25 RPRPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVI 104
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENAslarearparRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSA 184
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERA----------LERRRLRRENAEDSGLIGRSPAMQEVRRLIEKV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 185 ARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLF 264
Cdd:COG2204  151 APSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 265 LDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGND 344
Cdd:COG2204  231 LDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRED 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 345 VIEIAEAALSRFAAEEGREFFgLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLPDAftdhpsppedlpp 424
Cdd:COG2204  311 IPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA------------- 376

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499656124 425 pslpttdeptldgligrtLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRKREAW 483
Cdd:COG2204  377 ------------------LEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417

Name

Accession

Description

Interval

E-value

AtoC

COG2204

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...

25-483

4.84e-169

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: 482.54 E-value: 4.84e-169

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  25 RPRPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVI 104
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENAslarearparRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSA 184
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERA----------LERRRLRRENAEDSGLIGRSPAMQEVRRLIEKV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 185 ARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLF 264
Cdd:COG2204  151 APSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 265 LDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGND 344
Cdd:COG2204  231 LDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRED 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 345 VIEIAEAALSRFAAEEGREFFgLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLPDAftdhpsppedlpp 424
Cdd:COG2204  311 IPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA------------- 376

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499656124 425 pslpttdeptldgligrtLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRKREAW 483
Cdd:COG2204  377 ------------------LEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417

PRK11361

acetoacetate metabolism transcriptional regulator AtoC;

27-479

9.43e-112

acetoacetate metabolism transcriptional regulator AtoC;

Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 337.98 E-value: 9.43e-112

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  27 RPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:PRK11361   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENASLAREARPARRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSAAR 186
Cdd:PRK11361  85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIAL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 187 SMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLFLD 266
Cdd:PRK11361 165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 267 EICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGNDVI 346
Cdd:PRK11361 245 EIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDIS 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 347 EIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLPDAFtdhpsppedLPPPS 426
Cdd:PRK11361 325 LLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQI---------RQPVC 395

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499656124 427 LPTTDEPTLDGliGRTLAEI----EQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:PRK11361 396 NAGEVKTAPVG--ERNLKEEikrvEKRIIMEVLEQQEGNRTRTALMLGISRRALMYK 450

ntrC

TIGR01818

nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...

29-479

6.13e-108

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: 328.62 E-value: 6.13e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124   29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVENAslaREARPARRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSAARSM 188
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERA---LAHAQEQVALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRSD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  189 ATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLFLDEI 268
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  269 CEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGNDVIEI 348
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  349 AEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLPDAFTDHPSPPEDLPPPSLP 428
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQD 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499656124  429 TTD---EPTLD--------GLIGRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:TIGR01818 398 SWDealEAWAKqalsrgeqGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRK 459

Sigma54_activat

pfam00158

Sigma-54 interaction domain;

167-334

2.75e-93

Sigma-54 interaction domain;

Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 280.06 E-value: 2.75e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  167 FLGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTG 246
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  247 AIADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYY 326
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160


                  ....*...
gi 499656124  327 RLFVVPIH 334
Cdd:pfam00158 161 RLNVIPIE 168

TF_PrdR

NF041552

sigma-54 dependent transcriptional regulator PrdR;

168-479

3.51e-85

sigma-54 dependent transcriptional regulator PrdR;

Pssm-ID: 469437 [Multi-domain] Cd Length: 577 Bit Score: 272.92 E-value: 3.51e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 168 LGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAaGPFIALNCGAIPQDLLESEVFGHVKGSFTGA 247
Cdd:NF041552 270 IGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRK-GPFVPVNCSAIPEELFESEFFGYEEGAFTGA 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 248 IAD-KPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYY 326
Cdd:NF041552 349 LKKgKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFREDLYY 428

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 327 RLFVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMR 406
Cdd:NF041552 429 RLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNGTITKD 508

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499656124 407 MLPDAFTDhpsppedlppPSLPTTDEPTLDGL-IGRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:NF041552 509 SIPEYILE----------SVKKKEDEEGDYPLdLNKAVEKLEIDTIKKALEMSNGNKAKAAKLLNIPRSTLYYK 572

REC_NtrC1-like

cd17572

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...

29-141

1.75e-38

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: 136.17 E-value: 1.75e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNA 113

REC

smart00448

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...

29-81

8.22e-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: 57.19 E-value: 8.22e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 499656124    29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLP 81
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55

Name

Accession

Description

Interval

E-value

AtoC

COG2204

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...

25-483

4.84e-169

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: 482.54 E-value: 4.84e-169

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  25 RPRPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVI 104
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENAslarearparRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSA 184
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERA----------LERRRLRRENAEDSGLIGRSPAMQEVRRLIEKV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 185 ARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLF 264
Cdd:COG2204  151 APSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 265 LDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGND 344
Cdd:COG2204  231 LDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRED 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 345 VIEIAEAALSRFAAEEGREFFgLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLPDAftdhpsppedlpp 424
Cdd:COG2204  311 IPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA------------- 376

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499656124 425 pslpttdeptldgligrtLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRKREAW 483
Cdd:COG2204  377 ------------------LEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417

RocR

COG3829

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...

167-479

5.43e-136

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: 399.53 E-value: 5.43e-136

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 167 FLGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTG 246
Cdd:COG3829  140 IIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAFTG 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 247 AIA-DKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLY 325
Cdd:COG3829  220 AKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFREDLY 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 326 YRLFVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTM 405
Cdd:COG3829  300 YRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSEGDVITP 379

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499656124 406 RMLPDAFTDHPSPPEDlpppslptTDEPTLDGligrTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:COG3829  380 EHLPEYLLEEAEAASA--------AEEGSLKE----ALEEVEKELIEEALEKTGGNKSKAAKALGISRSTLYRK 441

PRK11361

acetoacetate metabolism transcriptional regulator AtoC;

27-479

9.43e-112

acetoacetate metabolism transcriptional regulator AtoC;

Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 337.98 E-value: 9.43e-112

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  27 RPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:PRK11361   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENASLAREARPARRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSAAR 186
Cdd:PRK11361  85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIAL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 187 SMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLFLD 266
Cdd:PRK11361 165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 267 EICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGNDVI 346
Cdd:PRK11361 245 EIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDIS 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 347 EIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLPDAFtdhpsppedLPPPS 426
Cdd:PRK11361 325 LLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQI---------RQPVC 395

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499656124 427 LPTTDEPTLDGliGRTLAEI----EQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:PRK11361 396 NAGEVKTAPVG--ERNLKEEikrvEKRIIMEVLEQQEGNRTRTALMLGISRRALMYK 450

ntrC

TIGR01818

nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...

29-479

6.13e-108

Pssm-ID: 273818 [Multi-domain] Cd Length: 463 Bit Score: 328.62 E-value: 6.13e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124   29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVENAslaREARPARRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSAARSM 188
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERA---LAHAQEQVALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRSD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  189 ATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLFLDEI 268
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  269 CEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGNDVIEI 348
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  349 AEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLPDAFTDHPSPPEDLPPPSLP 428
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQD 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499656124  429 TTD---EPTLD--------GLIGRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:TIGR01818 398 SWDealEAWAKqalsrgeqGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRK 459

PEP_resp_reg

TIGR02915

PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...

29-477

1.40e-107

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: 327.09 E-value: 1.40e-107

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124   29 ILLIEDTPSLQMVYRSVLAsaGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPD-----RNGLDLMQDMLRLRPETNVIV 103
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPPdadgaSEGLAALQQILAIAPDTKVIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  104 ITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENASLAREARPARRPPPQPAGPAPVTGaFLGSSEAMARIHAKIRS 183
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRG-LITSSPGMQKICRTIEK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  184 AARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTL 263
Cdd:TIGR02915 158 IAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  264 FLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGN 343
Cdd:TIGR02915 238 FLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  344 DVIEIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLpdAFTDHPSPPEDLP 423
Cdd:TIGR02915 318 DAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDL--GLDARERAETPLE 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499656124  424 PPSLPTTDeptldgligrtlaEIEQIVIEATIARHGGSVPKAARMLDVSPSTLY 477
Cdd:TIGR02915 396 VNLREVRE-------------RAEREAVRKAIARVDGNIARAAELLGITRPTLY 436

AcoR

COG3284

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

166-479

6.47e-106

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

Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 328.40 E-value: 6.47e-106

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 166 AFLGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFT 245
Cdd:COG3284  322 ALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFT 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 246 GAIAD-KPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDL 324
Cdd:COG3284  402 GARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDL 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 325 YYRLFVVPIHMPPLRDRGnDVIEIAEAALSRFAAEEGRefFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVT 404
Cdd:COG3284  482 YYRLNGLTLTLPPLRERE-DLPALIEHLLRELAAGRGP--LRLSPEALALLAAYPWPGNVRELRNVLRTALALADGGVIT 558

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499656124 405 MRMLPDAFTDHPSPPEDLPPPSlpttdeptldgliGRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:COG3284  559 VEDLPDELRAELAAAAPAAAAP-------------LTSLEEAERDAILRALRACGGNVSAAARALGISRSTLYRK 620

PRK10365

sigma-54-dependent response regulator transcription factor ZraR;

29-479

4.18e-96

sigma-54-dependent response regulator transcription factor ZraR;

Pssm-ID: 182412 [Multi-domain] Cd Length: 441 Bit Score: 297.33 E-value: 4.18e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFlgaveNASLAREARPARRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSAARSM 188
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNL-----QATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAPSE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 189 ATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLFLDEI 268
Cdd:PRK10365 163 ATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEI 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 269 CEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGNDVIEI 348
Cdd:PRK10365 243 GDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLL 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 349 AEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLPDAFTdhpsppedlpppslp 428
Cdd:PRK10365 323 AGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIA--------------- 387

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499656124 429 TTDEPTLDGLIGRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:PRK10365 388 STPIPLGQSQDIQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAK 438

Sigma54_activat

pfam00158

Sigma-54 interaction domain;

167-334

2.75e-93

Sigma-54 interaction domain;

Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 280.06 E-value: 2.75e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  167 FLGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTG 246
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  247 AIADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYY 326
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160


                  ....*...
gi 499656124  327 RLFVVPIH 334
Cdd:pfam00158 161 RLNVIPIE 168

PRK15115

response regulator GlrR; Provisional

23-397

2.52e-92

response regulator GlrR; Provisional

Pssm-ID: 185070 [Multi-domain] Cd Length: 444 Bit Score: 287.50 E-value: 2.52e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  23 ASRPRPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVI 102
Cdd:PRK15115   2 SRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 103 VITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENAslarearparRPPPQPAGPAPVTGAFLGSSEAMARIHAKIR 182
Cdd:PRK15115  82 ILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDA----------LEQSAPATDERWREAIVTRSPLMLRLLEQAR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 183 SAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGT 262
Cdd:PRK15115 152 MVAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 263 LFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRG 342
Cdd:PRK15115 232 LFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERT 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499656124 343 NDVIEIAEAALsRFAAEEGREF---FGLDAeVKALFRRhPWPGNVRQVLNVIRNVVVL 397
Cdd:PRK15115 312 EDIPLLANHLL-RQAAERHKPFvraFSTDA-MKRLMTA-SWPGNVRQLVNVIEQCVAL 366

nifA

TIGR01817

Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...

168-473

2.90e-89

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: 282.37 E-value: 2.90e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  168 LGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGA 247
Cdd:TIGR01817 199 IGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  248 IADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYR 327
Cdd:TIGR01817 279 IAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYR 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  328 LFVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFFGLDAEVKALfRRHPWPGNVRQVLNVIRNVVVLNEGGLVT--- 404
Cdd:TIGR01817 359 INVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPLTITPSAIRVL-MSCKWPGNVRELENCLERTATLSRSGTITrsd 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  405 ---------MRML----PDAFTDHPSPPEDLPPPSLPTTDEPTLDGLIGRTLAEIEQIVieATIARHGGSVPKAARMLDV 471
Cdd:TIGR01817 438 fscqsgqclSPMLaktcPHGHISIDPLAGTTPPHSPASAALPGEPGLSGPTLSERERLI--AALEQAGWVQAKAARLLGM 515


                  ..
gi 499656124  472 SP 473
Cdd:TIGR01817 516 TP 517

PRK05022

nitric oxide reductase transcriptional regulator NorR;

165-480

6.58e-89

nitric oxide reductase transcriptional regulator NorR;

Pssm-ID: 235331 [Multi-domain] Cd Length: 509 Bit Score: 280.91 E-value: 6.58e-89

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 165 GAFLGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSF 244
Cdd:PRK05022 187 GEMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAF 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 245 TGAIADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDL 324
Cdd:PRK05022 267 TGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADL 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 325 YYRLFVVPIHMPPLRDRGNDVIeiaeaALSRFAAEEGREFFG-----LDAEVKALFRRHPWPGNVRQVLNVIRNVVVL-- 397
Cdd:PRK05022 347 YHRLSVFPLSVPPLRERGDDVL-----LLAGYFLEQNRARLGlrslrLSPAAQAALLAYDWPGNVRELEHVISRAALLar 421

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 398 --NEGGLVTMRmlpdafTDHPSPPEDLPPPSLPTTDEPTLdgLIGRTLAE-IEQI---VIEATIARHGGSVPKAARMLDV 471
Cdd:PRK05022 422 arGAGRIVTLE------AQHLDLPAEVALPPPEAAAAPAA--VVSQNLREaTEAFqrqLIRQALAQHQGNWAAAARALEL 493

                        330
                 ....*....|.
gi 499656124 472 SPSTLYR--KR 480
Cdd:PRK05022 494 DRANLHRlaKR 504

glnG

PRK10923

nitrogen regulation protein NR(I); Provisional

29-479

2.26e-87

nitrogen regulation protein NR(I); Provisional

Pssm-ID: 182842 [Multi-domain] Cd Length: 469 Bit Score: 275.60 E-value: 2.26e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVENAslarEARPARRPPPQPAGPAPVTGAFLGSSEAMARIHAKIRSAARSM 188
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERA----ISHYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRSS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 189 ATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLFLDEI 268
Cdd:PRK10923 162 ISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 269 CEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGNDVIEI 348
Cdd:PRK10923 242 GDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 349 AEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRMLP-DAFTDHPSPPEDLPPPSL 427
Cdd:PRK10923 322 ARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPgELFESTVPESTSQMQPDS 401

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499656124 428 PTT------DEPTLDG---LIGRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:PRK10923 402 WATllaqwaDRALRSGhqnLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRK 462

TyrR

COG3283

Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...

166-410

1.45e-86

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

Pssm-ID: 442513 [Multi-domain] Cd Length: 514 Bit Score: 274.76 E-value: 1.45e-86

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 166 AFLGSSEAMARIhakIRSAARsMAT----IFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVK 241
Cdd:COG3283  205 HIVASSPKMRQV---IRQAKK-MAMldapLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAP 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 242 GSFTGAIADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFR 321
Cdd:COG3283  281 GAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFR 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 322 EDLYYRLFVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGG 401
Cdd:COG3283  361 EDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGD 440

                        250
                 ....*....|.
gi 499656124 402 LVTMR--MLPD 410
Cdd:COG3283  441 ELTPEdlQLPE 451

TF_PrdR

NF041552

sigma-54 dependent transcriptional regulator PrdR;

168-479

3.51e-85

sigma-54 dependent transcriptional regulator PrdR;

Pssm-ID: 469437 [Multi-domain] Cd Length: 577 Bit Score: 272.92 E-value: 3.51e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 168 LGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAaGPFIALNCGAIPQDLLESEVFGHVKGSFTGA 247
Cdd:NF041552 270 IGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRK-GPFVPVNCSAIPEELFESEFFGYEEGAFTGA 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 248 IAD-KPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYY 326
Cdd:NF041552 349 LKKgKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFREDLYY 428

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 327 RLFVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMR 406
Cdd:NF041552 429 RLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNGTITKD 508

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499656124 407 MLPDAFTDhpsppedlppPSLPTTDEPTLDGL-IGRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:NF041552 509 SIPEYILE----------SVKKKEDEEGDYPLdLNKAVEKLEIDTIKKALEMSNGNKAKAAKLLNIPRSTLYYK 572

PRK10820

transcriptional regulator TyrR;

168-410

1.37e-70

transcriptional regulator TyrR;

Pssm-ID: 236769 [Multi-domain] Cd Length: 520 Bit Score: 233.43 E-value: 1.37e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 168 LGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGA 247
Cdd:PRK10820 207 VAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPNA 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 248 IADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYR 327
Cdd:PRK10820 287 LEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYYR 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 328 LFVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMR- 406
Cdd:PRK10820 367 LNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLEGYELRPQd 446


                 ....*
gi 499656124 407 -MLPD 410
Cdd:PRK10820 447 iLLPD 451

propionate_PrpR

TIGR02329

propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...

163-482

1.81e-67

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: 225.51 E-value: 1.81e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  163 VTGAFLGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKG 242
Cdd:TIGR02329 210 RLDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEG 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  243 SFTGA-IADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFR 321
Cdd:TIGR02329 290 AFTGArRGGRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFR 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  322 EDLYYRLFVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFFGLDAEVKA----LFRRHPWPGNVRQVLNVIRNVVV- 396
Cdd:TIGR02329 370 RDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPDSEAAAQVLAgvadPLQRYPWPGNVRELRNLVERLALe 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  397 --LNEGGLVTMRMLpdaftdHPSPPEDLPPPSLPTTDEPTLdgligRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPS 474
Cdd:TIGR02329 450 lsAMPAGALTPDVL------RALAPELAEASGKGKTSALSL-----RERSRVEALAVRAALERFGGDRDAAAKALGISRT 518


                  ....*...
gi 499656124  475 TLYRKREA 482
Cdd:TIGR02329 519 TLWRRLKA 526

FhlA

COG3604

FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...

187-479

4.95e-66

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: 215.87 E-value: 4.95e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 187 SMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESevfghvkgsftgaiadkpgaaaaadggtlfld 266
Cdd:COG3604  114 SLAAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 267 eicemapalqtkllrfLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGNDVI 346
Cdd:COG3604  162 ----------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIP 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 347 EIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVtmrmlpdaftdhpsppedlppps 426
Cdd:COG3604  226 LLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVL----------------------- 282

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499656124 427 lpttDEPTLDGLIGRTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:COG3604  283 ----DADDLAPGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSR 331

PRK15424

propionate catabolism operon regulatory protein PrpR; Provisional

165-482

1.57e-64

propionate catabolism operon regulatory protein PrpR; Provisional

Pssm-ID: 237963 [Multi-domain] Cd Length: 538 Bit Score: 217.66 E-value: 1.57e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 165 GAFLGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSP--------RAAGPFIALNCGAIPQDLLESEV 236
Cdd:PRK15424 219 GDLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHREYFarhdarqgKKSHPFVAVNCGAIAESLLEAEL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 237 FGHVKGSFTGAI-ADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAV 315
Cdd:PRK15424 299 FGYEEGAFTGSRrGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDV 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 316 RRGHFREDLYYRLFVVPIHMPPLRDRGNDVIEIAE-------AAL-SRFAAEEGREffgLDAEVKALFRRHpWPGNVRQV 387
Cdd:PRK15424 379 RQGRFRRDLFYRLSILRLQLPPLRERVADILPLAEsflkqslAALsAPFSAALRQG---LQQCETLLLHYD-WPGNVREL 454

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 388 LNVI-RNVVVLNEGGLVTM------RMLPDAFTDHPSPPEdlpppslpttdeptldgligrtlAEIEQIVIEATIARHGG 460
Cdd:PRK15424 455 RNLMeRLALFLSVEPTPDLtpqflqLLLPELARESAKTPA-----------------------PRLLAATLQQALERFNG 511

                        330       340
                 ....*....|....*....|..
gi 499656124 461 SVPKAARMLDVSPSTLYRKREA 482
Cdd:PRK15424 512 DKTAAANYLGISRTTLWRRLKA 533

phageshock_pspF

TIGR02974

psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...

168-469

2.20e-62

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: 206.38 E-value: 2.20e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  168 LGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGA 247
Cdd:TIGR02974   2 IGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  248 IADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYR 327
Cdd:TIGR02974  82 QKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLDR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  328 L-FVVpIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFF-GLDAEVKALFRRHPWPGNVRQVLNVI-RNVVVLNEGGLVT 404
Cdd:TIGR02974 162 LaFDV-ITLPPLRERQEDIMLLAEHFAIRMARELGLPLFpGFTPQAREQLLEYHWPGNVRELKNVVeRSVYRHGLEEAPI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499656124  405 MRMLPDAFT---DHPSPPEDLPPPSLPTTDEPTLDGL-------IGRTLAEIEQIVIEATIARHGGSVPKAARML 469
Cdd:TIGR02974 241 DEIIIDPFAspwRPKQAAPAVDEVNSTPTDLPSPSSIaaafpldLKQAQQDYEIELLQQALAEAQFNQRKAAELL 315

PRK15429

formate hydrogenlyase transcriptional activator FlhA;

165-410

7.01e-61

formate hydrogenlyase transcriptional activator FlhA;

Pssm-ID: 237965 [Multi-domain] Cd Length: 686 Bit Score: 211.23 E-value: 7.01e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 165 GAFLGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSF 244
Cdd:PRK15429 376 GEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAF 455

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 245 TGAIADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDL 324
Cdd:PRK15429 456 TGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDL 535

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 325 YYRLFVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREFFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVT 404
Cdd:PRK15429 536 YYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVLQ 615


                 ....*.
gi 499656124 405 MRmLPD 410
Cdd:PRK15429 616 LS-LPD 620

pspF

PRK11608

phage shock protein operon transcriptional activator; Provisional

191-394

3.30e-56

phage shock protein operon transcriptional activator; Provisional

Pssm-ID: 236936 [Multi-domain] Cd Length: 326 Bit Score: 189.88 E-value: 3.30e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 191 IFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGAAAAADGGTLFLDEICe 270
Cdd:PRK11608  32 VLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRFERADGGTLFLDELA- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 271 MAPAL-QTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIHMPPLRDRGNDVIEIA 349
Cdd:PRK11608 111 TAPMLvQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQLPPLRERQSDIMLMA 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499656124 350 EaalsRFAAEEGRE-----FFGLDAEVKALFRRHPWPGNVRQVLNVI-RNV 394
Cdd:PRK11608 191 E----HFAIQMCRElglplFPGFTERARETLLNYRWPGNIRELKNVVeRSV 237

PRK11388

DNA-binding transcriptional regulator DhaR; Provisional

169-479

2.99e-49

DNA-binding transcriptional regulator DhaR; Provisional

Pssm-ID: 183114 [Multi-domain] Cd Length: 638 Bit Score: 178.72 E-value: 2.99e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 169 GSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGhvkGSFTGAI 248
Cdd:PRK11388 329 QDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SDRTDSE 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 249 ADKPGAAAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRL 328
Cdd:PRK11388 406 NGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYAL 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 329 FVVPIHMPPLRDRGNDVIEIAEAALSRFAAEEGREfFGLDAEVKALFRRHPWPGNVRQVLNVIRNVVVLNEGGLVTMRML 408
Cdd:PRK11388 486 HAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTR-LKIDDDALARLVSYRWPGNDFELRSVIENLALSSDNGRIRLSDL 564

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499656124 409 PDAFTDHpsppedlppPSLPTTDEPTLDGLIgrTLAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRK 479
Cdd:PRK11388 565 PEHLFTE---------QATDDVSATRLSTSL--SLAELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRK 624

REC_NtrC1-like

cd17572

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...

29-141

1.75e-38

Pssm-ID: 381114 [Multi-domain] Cd Length: 121 Bit Score: 136.17 E-value: 1.75e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNA 113

RtcR

COG4650

Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...

182-404

3.04e-32

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: 129.18 E-value: 3.04e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 182 RSAARSMATIFITGESGTGKELCA-------LAVHDTSpraaGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADKPGA 254
Cdd:COG4650  202 RVAIRSRAPILLTGPTGAGKSQLArriyelkKARHQVS----GRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGL 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 255 AAAADGGTLFLDEICEMAPALQTKLLRFLQTSMVQPVGATRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYRLFVVPIH 334
Cdd:COG4650  278 LRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFR 357

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499656124 335 MPPLRDRGNDVIEIAEAALSRFAAEEGREfFGLDAEVKALF------RRHPWPGNVRQvLN--VIRnVVVLNEGGLVT 404
Cdd:COG4650  358 LPGLAERREDIEPNLDYELARFAREQGRR-VRFNKEARARYlafatsPEALWSGNFRD-LNasVTR-MATLAEGGRIT 432

Response_reg

pfam00072

Response regulator receiver domain; This domain receives the signal from the sensor partner in ...

29-139

3.56e-28

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

Pssm-ID: 395025 [Multi-domain] Cd Length: 111 Bit Score: 108.01 E-value: 3.56e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124   29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 499656124  109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVE 139
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111

REC

cd00156

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...

30-128

2.73e-27

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: 105.00 E-value: 2.73e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  30 LLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGS 109
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80

                         90
                 ....*....|....*....
gi 499656124 110 INKAVEAMRAGAHEFLVKP 128
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99

OmpR

COG0745

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...

29-140

7.70e-27

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: 107.35 E-value: 7.70e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARD 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVEN 140
Cdd:COG0745   84 DEEDRVRGLEAGADDYLTKPFDPEELLARIRA 115

PleD

COG3706

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...

29-139

1.76e-26

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: 105.38 E-value: 1.76e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---VIVIT 105
Cdd:COG3706    4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCR-RLRADPRTAdipIIFLT 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVE 139
Cdd:COG3706   83 ALDDEEDRARALEAGADDYLTKPFDPEELLARVD 116

PspF

COG1221

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...

191-394

2.11e-26

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: 113.28 E-value: 2.11e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 191 IFITGESGTGKELCALAVH------DTSPRAAgPFIALNCgAI----PQdLLESEVFGHVKGSFTGAIADKPGAAAAADG 260
Cdd:COG1221  133 TLILGPTGVGKSFFAELMYeyaieiGVLPEDA-PFVVFNC-ADyannPQ-LLMSQLFGYVKGAFTGADKDKEGLIEKADG 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 261 GTLFLDEICEMAPALQTKLLRFLQTSMVQPVGAT-RPRKVNVRIVCATNRDPLDA-----VRRghfredlyyrlfvVP-- 332
Cdd:COG1221  210 GILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGETeKTRKANVRIIFATTEDPESSllktfLRR-------------IPmv 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499656124 333 IHMPPLRDRG-NDVIEIaeaaLSRFAAEE----GREFFgLDAEVKALFRRHPWPGNVRQVLNVIRNV 394
Cdd:COG1221  277 IKLPSLEERSlEERLEL----IKHFFKEEakrlNKPIK-VSKEVLKALLLYDCPGNIGQLKSDIQLA 338

CitB

COG4565

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...

29-141

1.19e-25

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

Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 101.97 E-value: 1.19e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLAS-AGHR-VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:COG4565    6 VLIVEDDPMVAELLRRYLERlPGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVITA 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:COG4565   86 ARDPETVREALRAGVVDYLIKPFTFERLREALERY 120

Sigma54_activ_2

pfam14532

Sigma-54 interaction domain;

168-338

1.89e-25

Sigma-54 interaction domain;

Pssm-ID: 434021 [Multi-domain] Cd Length: 138 Bit Score: 101.27 E-value: 1.89e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  168 LGSSEAMARIHAKIRSAARSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESevfghvkgsftga 247
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  248 iadkpgaaaaADGGTLFLDEICEMAPALQTKLLRFLQtsmvqpvgatRPRKVNVRIVCATNRDPLDAVRRGHFREDLYYR 327
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLA----------KAEGYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127

                         170
                  ....*....|.
gi 499656124  328 LFVVPIHMPPL 338
Cdd:pfam14532 128 LSALRLHVPPL 138

CheY

COG0784

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...

23-141

9.20e-25

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: 99.15 E-value: 9.20e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  23 ASRPRPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRL--RPETN 100
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALprLPDIP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499656124 101 VIVITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:COG0784   82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122

FixJ

COG4566

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...

43-141

1.31e-24

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: 100.95 E-value: 1.31e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  43 RSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGSINKAVEAMRAGAH 122
Cdd:COG4566   16 AFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHGDVPMAVRAMKAGAV 95

                         90
                 ....*....|....*....
gi 499656124 123 EFLVKPFDEQRFLGAVENA 141
Cdd:COG4566   96 DFLEKPFDDQALLDAVRRA 114

REC_NtrX-like

cd17550

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...

29-141

1.64e-24

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: 97.95 E-value: 1.64e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERA 113

COG4567

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...

24-141

1.72e-24

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: 99.99 E-value: 1.72e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  24 SRPRPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIV 103
Cdd:COG4567    2 AEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVV 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499656124 104 ITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:COG4567   82 LTGYASIATAVEAIKLGADDYLAKPADADDLLAALERA 119

REC_DctD-like

cd17549

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...

29-141

2.43e-24

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: 97.95 E-value: 2.43e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRA 113

REC_RegA-like

cd17563

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...

29-137

7.41e-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: 95.97 E-value: 7.41e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDtpslQMVYRSVLASA----GHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVI 104
Cdd:cd17563    3 LLLVDD----DEVFAERLARAlerrGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVL 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKPFDEQRFLGA 137
Cdd:cd17563   79 TGYASIATAVEAIKLGADDYLAKPADADEILAA 111

RpfG

COG3437

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...

22-141

2.27e-23

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: 98.31 E-value: 2.27e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  22 EASRPRPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN- 100
Cdd:COG3437    2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLR-LLRADPSTRd 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499656124 101 --VIVITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:COG3437   81 ipVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123

REC_RssB-like

cd17555

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...

29-141

3.16e-22

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: 91.49 E-value: 3.16e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17555    3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAG 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLG-AVENA 141
Cdd:cd17555   83 VMSDAVEALRLGAWDYLTKPIEDLAVLEhAVRRA 116

AAA

cd00009

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...

174-337

2.16e-21

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: 90.28 E-value: 2.16e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 174 MARIHAKIRSAA--RSMATIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTGAIADK 251
Cdd:cd00009    3 QEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124 252 pgaaaaADGGTLFLDEICEMAPALQTKLLRFLQTSMVqpvgaTRPRKVNVRIVCATNRDPLdavrrGHFREDLYYRlFVV 331
Cdd:cd00009   83 ------AKPGVLFIDEIDSLSRGAQNALLRVLETLND-----LRIDRENVRVIGATNRPLL-----GDLDRALYDR-LDI 145


                 ....*.
gi 499656124 332 PIHMPP 337
Cdd:cd00009  146 RIVIPL 151

REC_CheY

cd17542

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...

29-141

2.62e-21

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: 88.87 E-value: 2.62e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAG-HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITAN 107
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124 108 GSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd17542   83 GQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116

YesN

COG4753

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...

29-128

3.90e-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: 87.91 E-value: 3.90e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAG--HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81

                         90       100
                 ....*....|....*....|..
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKP 128
Cdd:COG4753   82 YSDFEYAQEAIKLGADDYLLKP 103

REC_OmpR

cd17574

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...

30-128

1.33e-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: 86.31 E-value: 1.33e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  30 LLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGS 109
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80

                         90
                 ....*....|....*....
gi 499656124 110 INKAVEAMRAGAHEFLVKP 128
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99

REC_citrate_TCS

cd19925

phosphoacceptor receiver (REC) domain of citrate family two-component system response ...

29-134

5.44e-20

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: 85.37 E-value: 5.44e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAG--HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:cd19925    3 VLIVEDDPMVAEIHRAYVEQVPgfTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTA 82

                         90       100
                 ....*....|....*....|....*...
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFDEQRF 134
Cdd:cd19925   83 ANDVETVREALRLGVVDYLIKPFTFERL 110

REC_NarL-like

cd17535

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...

29-139

7.34e-20

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: 84.87 E-value: 7.34e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHR--VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEPDIevVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVE 139
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIR 113

REC_OmpR_KdpE-like

cd17620

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...

29-128

1.83e-19

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: 83.37 E-value: 1.83e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETNVIVITANG 108
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIR-RLREWSAVPVIVLSARD 79

                         90       100
                 ....*....|....*....|
gi 499656124 109 SINKAVEAMRAGAHEFLVKP 128
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99

REC_FixJ

cd17537

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...

28-141

9.25e-19

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: 81.87 E-value: 9.25e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  28 PILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITAN 107
Cdd:cd17537    2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGH 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124 108 GSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd17537   82 GDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQA 115

REC_OmpR_PmrA-like

cd17624

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...

29-130

1.18e-17

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: 78.68 E-value: 1.18e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80

                         90       100
                 ....*....|....*....|..
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFA 102

REC_OmpR_CusR-like

cd19935

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...

29-128

1.82e-17

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: 77.48 E-value: 1.82e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80

                         90       100
                 ....*....|....*....|
gi 499656124 109 SINKAVEAMRAGAHEFLVKP 128
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVKP 100

LytT

COG3279

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...

29-141

3.17e-17

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

Pssm-ID: 442510 [Multi-domain] Cd Length: 235 Bit Score: 80.63 E-value: 3.17e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAG--HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:COG3279    4 ILIVDDEPLARERLERLLEKYPdlEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTA 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499656124 107 ngSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:COG3279   84 --YDEYALEAFEVNAVDYLLKPIDEERLAKALEKA 116

REC_RpfG-like

cd17551

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...

29-140

5.79e-17

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: 76.71 E-value: 5.79e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAG-HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---VIVI 104
Cdd:cd17551    3 ILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIR-RLRALPGLEdvpIVMI 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVEN 140
Cdd:cd17551   82 TADTDREVRLRALEAGATDFLTKPFDPVELLARVRN 117

fixJ

PRK09390

response regulator FixJ; Provisional

46-141

4.09e-16

response regulator FixJ; Provisional

Pssm-ID: 181815 [Multi-domain] Cd Length: 202 Bit Score: 76.96 E-value: 4.09e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  46 LASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGSINKAVEAMRAGAHEFL 125
Cdd:PRK09390  23 LDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDVPLAVEAMKLGAVDFI 102

                         90
                 ....*....|....*.
gi 499656124 126 VKPFDEQRFLGAVENA 141
Cdd:PRK09390 103 EKPFEDERLIGAIERA 118

REC_D1_PleD-like

cd17538

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...

29-129

7.14e-16

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: 73.30 E-value: 7.14e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---VIVIT 105
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCR-RLKEDPETRhipVIMIT 80

                         90       100
                 ....*....|....*....|....
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKPI 104

AmiR

COG3707

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...

25-141

7.86e-16

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: 75.76 E-value: 7.86e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  25 RPRPILLIEDTPSLQMVYRSVLASAGHRV-AVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETnVIV 103
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPAP-VIL 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499656124 104 ITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:COG3707   81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELA 118

REC_CheY4-like

cd17562

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...

27-138

1.39e-15

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: 72.72 E-value: 1.39e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  27 RPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPE---TNVIV 103
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKE-LRKLPAykfTPILM 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499656124 104 ITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAV 138
Cdd:cd17562   80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114

REC_OmpR_DrrD-like

cd17625

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...

30-135

1.66e-15

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: 72.64 E-value: 1.66e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  30 LLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGS 109
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80

                         90       100
                 ....*....|....*....|....*.
gi 499656124 110 INKAVEAMRAGAHEFLVKPFDEQRFL 135
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELL 106

REC_OmpR_MtPhoP-like

cd17615

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...

29-129

2.93e-15

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: 72.00 E-value: 2.93e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81

                         90       100
                 ....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPF 129
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKPF 102

REC_YesN-like

cd17536

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...

53-141

3.21e-15

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: 71.98 E-value: 3.21e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  53 VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGSINKAVEAMRAGAHEFLVKPFDEQ 132
Cdd:cd17536   28 VGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILSGYDDFEYAQKAIRLGVVDYLLKPVDEE 107


                 ....*....
gi 499656124 133 RFLGAVENA 141
Cdd:cd17536  108 ELEEALEKA 116

REC_hyHK_CKI1_RcsC-like

cd17546

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...

29-138

4.27e-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: 71.35 E-value: 4.27e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQ---DMLRLRPETNVIVIT 105
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRrirELEGGGRRTPIIALT 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAV 138
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113

REC_OmpR_EcPhoP-like

cd19934

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...

29-129

6.40e-15

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: 70.77 E-value: 6.40e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdmlRLRPE---TNVIVIT 105
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLR---RWRSEgraTPVLILT 77

                         90       100
                 ....*....|....*....|....
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd19934   78 ARDSWQDKVEGLDAGADDYLTKPF 101

REC_TrrA-like

cd17554

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...

29-106

1.14e-14

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: 69.94 E-value: 1.14e-14

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:cd17554    3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80

REC_NtrC

cd19919

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...

28-130

2.50e-14

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: 69.22 E-value: 2.50e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  28 PILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITAN 107
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81

                         90       100
                 ....*....|....*....|...
gi 499656124 108 GSINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd19919   82 SDLDSAVSAYQGGAFEYLPKPFD 104

REC_OmpR_PhoB

cd17618

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...

29-129

3.03e-14

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: 68.82 E-value: 3.03e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdmlRLRPETN-----VIV 103
Cdd:cd17618    3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIR---RLKRDEMtrdipIIM 79

                         90       100
                 ....*....|....*....|....*.
gi 499656124 104 ITANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd17618   80 LTARGEEEDKVRGLEAGADDYITKPF 105

REC_RcNtrC-like

cd19928

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...

29-128

3.64e-14

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: 68.30 E-value: 3.64e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80

                         90       100
                 ....*....|....*....|
gi 499656124 109 SINKAVEAMRAGAHEFLVKP 128
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100

REC_2_DhkD-like

cd17580

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...

29-130

9.08e-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: 67.48 E-value: 9.08e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTP-SLQMVyRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPE---TNVIVI 104
Cdd:cd17580    1 ILVVDDNEdAAEML-ALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELAR-RLRELPWlanTPAIAL 78

                         90       100
                 ....*....|....*....|....*.
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd17580   79 TGYGQPEDRERALEAGFDAHLVKPVD 104

REC_PA4781-like

cd19920

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...

29-129

9.54e-14

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: 67.15 E-value: 9.54e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---VIVIT 105
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCR-RLKADPATRhipVIFLT 79

                         90       100
                 ....*....|....*....|....
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd19920   80 ALTDTEDKVKGFELGAVDYITKPF 103

REC_DC-like

cd17534

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...

29-141

9.70e-14

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: 67.43 E-value: 9.70e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRV-AVAGTAAEGLSRFRETLPNVVLLDLMLP-DRNGLDLMQdmlRLRPETN--VIVI 104
Cdd:cd17534    3 ILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAR---EIREKFDipVIFL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499656124 105 TAN---GSINKAVEAMRAGaheFLVKPFDEQRFLGAVENA 141
Cdd:cd17534   80 TAYsdeETLERAKETNPYG---YLVKPFNERELKAAIELA 116

REC_OmpR_CpxR

cd17623

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...

29-130

1.50e-13

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: 66.95 E-value: 1.50e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITANG 108
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKE-LRKTSQVPVLMLTARG 79

                         90       100
                 ....*....|....*....|..
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFN 101

REC_DivK-like

cd17548

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...

29-139

4.39e-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: 65.64 E-value: 4.39e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---VIVIT 105
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATR-LLKEDPATRdipVIALT 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVE 139
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114

REC_PilR

cd19926

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...

29-128

5.54e-13

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: 64.87 E-value: 5.54e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80

                         90       100
                 ....*....|....*....|
gi 499656124 109 SINKAVEAMRAGAHEFLVKP 128
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100

REC_RR468-like

cd17552

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...

26-130

6.33e-13

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: 65.27 E-value: 6.33e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  26 PRPILLIEDTPSLQMVYRSVLAS-AGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---V 101
Cdd:cd17552    1 SKRILVIDDEEDIREVVQACLEKlAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLK-KLQANPETQsipV 79

                         90       100
                 ....*....|....*....|....*....
gi 499656124 102 IVITANGSINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd17552   80 ILLTAKAQPSDRQRFASLGVAGVIAKPFD 108

REC_OmpR_ArcA_TorR-like

cd17619

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...

29-140

2.10e-12

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: 63.56 E-value: 2.10e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITA-N 107
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRE-LREQSEVGIILVTGrD 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 108 GSINKAVeAMRAGAHEFLVKPFDEQRFLGAVEN 140
Cdd:cd17619   82 DEVDRIV-GLEIGADDYVTKPFNPRELLVRAKN 113

orf27

CHL00148

Ycf27; Reviewed

29-129

4.17e-12

Ycf27; Reviewed

Pssm-ID: 214376 [Multi-domain] Cd Length: 240 Bit Score: 65.89 E-value: 4.17e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmlrLRPETNV--IVITA 106
Cdd:CHL00148   9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQE---IRKESDVpiIMLTA 85

                         90       100
                 ....*....|....*....|...
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPF 129
Cdd:CHL00148  86 LGDVSDRITGLELGADDYVVKPF 108

REC_Spo0F-like

cd17553

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...

29-130

4.41e-12

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: 62.96 E-value: 4.41e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82

                         90       100
                 ....*....|....*....|..
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd17553   83 ELDMIQESKELGALTHFAKPFD 104

PRK10955

envelope stress response regulator transcription factor CpxR;

29-132

5.19e-12

envelope stress response regulator transcription factor CpxR;

Pssm-ID: 182864 [Multi-domain] Cd Length: 232 Bit Score: 65.59 E-value: 5.19e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLpNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITANG 108
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSI-DLLLLDVMMPKKNGIDTLKE-LRQTHQTPVIMLTARG 81

                         90       100
                 ....*....|....*....|....
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQ 132
Cdd:PRK10955  82 SELDRVLGLELGADDYLPKPFNDR 105

PRK10529

DNA-binding transcriptional activator KdpE; Provisional

29-129

6.49e-12

DNA-binding transcriptional activator KdpE; Provisional

Pssm-ID: 182522 [Multi-domain] Cd Length: 225 Bit Score: 65.21 E-value: 6.49e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITANG 108
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRD-LRQWSAIPVIVLSARS 82

                         90       100
                 ....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPF 129
Cdd:PRK10529  83 EESDKIAALDAGADDYLSKPF 103

PRK10643

two-component system response regulator PmrA;

29-129

1.10e-11

two-component system response regulator PmrA;

Pssm-ID: 182612 [Multi-domain] Cd Length: 222 Bit Score: 64.29 E-value: 1.10e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82

                         90       100
                 ....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPF 129
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPF 103

REC_HupR-like

cd17569

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...

29-141

1.13e-11

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

Pssm-ID: 381113 [Multi-domain] Cd Length: 118 Bit Score: 61.65 E-value: 1.13e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPS-LQMVYRsVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITAN 107
Cdd:cd17569    3 ILLVDDEPNiLKALKR-LLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGY 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499656124 108 GSINKAVEAMRAGA-HEFLVKPFDEQRFLGAVENA 141
Cdd:cd17569   82 ADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQA 116

REC_OmpR_MtrA-like

cd17626

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...

29-129

1.25e-11

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: 61.33 E-value: 1.25e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETNVIVITANG 108
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCR-QIRAESGVPIVMLTAKS 81

                         90       100
                 ....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPF 129
Cdd:cd17626   82 DTVDVVLGLESGADDYVAKPF 102

REC_OmpR_kpRstA-like

cd17622

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...

29-130

1.64e-11

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: 61.24 E-value: 1.64e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmlrLRPETN--VIVITA 106
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRD---LRPKYQgpILLLTA 79

                         90       100
                 ....*....|....*....|....
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVKPVE 103

REC_hyHK

cd17598

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...

29-135

1.68e-11

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

Pssm-ID: 381128 [Multi-domain] Cd Length: 118 Bit Score: 61.19 E-value: 1.68e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETN---VIVIT 105
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRK-IKSDPDLKdipVILLT 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPFDEQRFL 135
Cdd:cd17598   80 TLSDPRDVIRGLECGADNFITKPYDEKYLL 109

REC_HP-RR-like

cd17573

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...

29-130

3.36e-11

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: 60.14 E-value: 3.36e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGlsrfrETLPNV-----VLLDLMLPDRNGLDLMQDMLRLRPETNVIV 103
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDG-----EYYIDIrnydlVLVSDKLPDGNGLSIVSRIKEKHPSIVVIV 75

                         90       100
                 ....*....|....*....|....*..
gi 499656124 104 ITANGSINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd17573   76 LSDNPKTEQEIEAFKEGADDYIAKPFD 102

REC_OmpR_BaeR-like

cd19938

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...

29-129

3.39e-11

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

Pssm-ID: 381165 [Multi-domain] Cd Length: 114 Bit Score: 60.08 E-value: 3.39e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITANG 108
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCRE-IRRFSDVPIIMVTARV 80

                         90       100
                 ....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPF 129
Cdd:cd19938   81 EEIDRLLGLELGADDYICKPY 101

REC_OmpR_RegX3-like

cd17621

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...

29-128

3.58e-11

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: 59.52 E-value: 3.58e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITANG 108
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQ-LRARSNVPVIMVTAKD 79

                         90       100
                 ....*....|....*....|
gi 499656124 109 SINKAVEAMRAGAHEFLVKP 128
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99

REC_typeB_ARR-like

cd17584

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...

29-131

4.25e-11

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: 59.95 E-value: 4.25e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLP--NVVLLDLMLPDRNGLDLMQdMLRLRPETNVIVITA 106
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDefDLVITDVHMPDMDGFEFLE-LIRLEMDLPVIMMSA 79

                         90       100
                 ....*....|....*....|....*
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFDE 131
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLKPVSI 104

REC_CheB-like

cd17541

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...

29-128

6.75e-11

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: 59.71 E-value: 6.75e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGhRVAVAGTAA---EGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPeTNVIVIT 105
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILESDP-DIEVVGTARdgeEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVS 80

                         90       100
                 ....*....|....*....|....*
gi 499656124 106 ANGSIN--KAVEAMRAGAHEFLVKP 128
Cdd:cd17541   81 SLTEEGaeITLEALELGAVDFIAKP 105

REC_OmpR_BsPhoP-like

cd19937

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...

30-129

7.71e-11

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: 59.21 E-value: 7.71e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  30 LLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---VIVITA 106
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCR-ILRSDPKTSsipIIMLTA 79

                         90       100
                 ....*....|....*....|...
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd19937   80 KGEEFDKVLGLELGADDYITKPF 102

REC

smart00448

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...

29-81

8.22e-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: 57.19 E-value: 8.22e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 499656124    29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLP 81
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55

REC_OmpR_CtrA

cd17616

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...

29-132

8.60e-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: 8.60e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80

                         90       100
                 ....*....|....*....|....
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQ 132
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKD 104

REC_OmpR_YycF-like

cd17614

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...

29-139

1.93e-10

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: 58.20 E-value: 1.93e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITANG 108
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCRE-VRKTSNVPIIMLTAKD 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVE 139
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKPFSNRELLARVK 110

PRK15369

two component system response regulator;

29-143

1.98e-10

two component system response regulator;

Pssm-ID: 185267 [Multi-domain] Cd Length: 211 Bit Score: 60.48 E-value: 1.98e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLAsAGHRVAVAGTAAEGLSRF---RETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVIT 105
Cdd:PRK15369   6 ILLVDDHELIINGIKNMLA-PYPRYKIVGQVDNGLEVYnacRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNILVLT 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENASL 143
Cdd:PRK15369  85 ARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAV 122

PRK11517

DNA-binding response regulator HprR;

29-138

2.81e-10

DNA-binding response regulator HprR;

Pssm-ID: 183172 [Multi-domain] Cd Length: 223 Bit Score: 60.30 E-value: 2.81e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETNVIVITANG 108
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQ-TLRTAKQTPVICLTARD 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAV 138
Cdd:PRK11517  82 SVDDRVRGLDSGANDYLVKPFSFSELLARV 111

PRK11091

aerobic respiration control sensor protein ArcB; Provisional

21-128

3.49e-10

aerobic respiration control sensor protein ArcB; Provisional

Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 62.27 E-value: 3.49e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  21 AEASRPRP---ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRP 97
Cdd:PRK11091 517 DEDDMPLPalnILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYP 596

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124  98 ETN---VIVITANgSINKAVEAMRAGAHEFLVKP 128
Cdd:PRK11091 597 REDlppLVALTAN-VLKDKKEYLDAGMDDVLSKP 629

REC_NarL

cd19931

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...

29-141

4.98e-10

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

Pssm-ID: 381158 [Multi-domain] Cd Length: 117 Bit Score: 56.97 E-value: 4.98e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGH--RVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMqDMLRLRPETNVIVI-T 105
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDftVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTL-KALREEGVSARIVIlT 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd19931   80 VSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQA 115

REC_OmpR_VirG

cd17594

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...

29-138

5.08e-10

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: 56.69 E-value: 5.08e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETNVIVITANG 108
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLR-TIRARSDVPIIIISGDR 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499656124 109 SINKA-VEAMRAGAHEFLVKPFDEQRFLGAV 138
Cdd:cd17594   81 RDEIDrVVGLELGADDYLAKPFGLRELLARV 111

HTH_8

pfam02954

Bacterial regulatory protein, Fis family;

443-482

6.81e-10

Bacterial regulatory protein, Fis family;

Pssm-ID: 427077 [Multi-domain] Cd Length: 40 Bit Score: 54.32 E-value: 6.81e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 499656124  443 LAEIEQIVIEATIARHGGSVPKAARMLDVSPSTLYRKREA 482
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40

REC_OmpR_PrrA-like

cd17627

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...

29-129

7.63e-10

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: 56.24 E-value: 7.63e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdmlRLRPETN---VIVIT 105
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCR---RLRAAGNdlpILVLT 77

                         90       100
                 ....*....|....*....|....
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd17627   78 ARDSVSDRVAGLDAGADDYLVKPF 101

REC_Rcp-like

cd17557

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...

28-139

9.39e-10

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: 56.66 E-value: 9.39e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  28 PILLIEDTPSLQMVYRSVLASAG--HRVAVAGTAAEGLSRFRET-------LPNVVLLDLMLPDRNGLDLMQDM-----L 93
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIkadpdL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499656124  94 RLRPetnVIVITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVE 139
Cdd:cd17557   81 RRIP---VVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIR 123

dpiA

PRK10046

two-component response regulator DpiA; Provisional

24-134

1.52e-09

two-component response regulator DpiA; Provisional

Pssm-ID: 182208 [Multi-domain] Cd Length: 225 Bit Score: 58.11 E-value: 1.52e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  24 SRPRPILLIED-TPSLQMVYRSVLASAG-HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNV 101
Cdd:PRK10046   2 TAPLTLLIVEDeTPLAEMHAEYIRHIPGfSQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDV 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 102 IVITANGSINKAVEAMRAGAHEFLVKPFDEQRF 134
Cdd:PRK10046  82 VFTTAASDMETVSEAVRCGVFDYLIKPIAYERL 114

PRK11083

DNA-binding response regulator CreB; Provisional

29-129

1.56e-09

DNA-binding response regulator CreB; Provisional

Pssm-ID: 236838 [Multi-domain] Cd Length: 228 Bit Score: 58.05 E-value: 1.56e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSL--QMVYrsVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:PRK11083   6 ILLVEDEQAIadTLVY--ALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTA 83

                         90       100
                 ....*....|....*....|....
gi 499656124 107 -NGSINKAVeAMRAGAHEFLVKPF 129
Cdd:PRK11083  84 rSDEVDRLV-GLEIGADDYVAKPF 106

REC_hyHK_blue-like

cd18161

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...

29-129

4.69e-09

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

Pssm-ID: 381145 [Multi-domain] Cd Length: 102 Bit Score: 53.89 E-value: 4.69e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETL-PNVVLLDLMLPDR-NGLDLMQDMLRLRPETNVIVITa 106
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPGGmNGSQLAEEARRRRPDLKVLLTS- 79

                         90       100
                 ....*....|....*....|....
gi 499656124 107 nGSINKAVEAMRAGAH-EFLVKPF 129
Cdd:cd18161   80 -GYAENAIEGGDLAPGvDVLSKPF 102

REC_PdtaR-like

cd19932

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...

29-141

5.00e-09

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: 53.96 E-value: 5.00e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRV-AVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPeTNVIVITAN 107
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI-APIVLLTAY 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124 108 GSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd19932   82 SQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMA 115

REC_LytTR_AlgR-like

cd17532

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...

53-139

5.99e-09

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: 53.70 E-value: 5.99e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  53 VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETNVIV-ITANGSInkAVEAMRAGAHEFLVKPFDE 131
Cdd:cd17532   27 VGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAK-KLSKLAKPPLIVfVTAYDEY--AVEAFELNAVDYLLKPFSE 103


                 ....*...
gi 499656124 132 QRFLGAVE 139
Cdd:cd17532  104 ERLAEALA 111

PRK10816

two-component system response regulator PhoP;

29-129

6.71e-09

two-component system response regulator PhoP;

Pssm-ID: 182755 [Multi-domain] Cd Length: 223 Bit Score: 56.29 E-value: 6.71e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82

                         90       100
                 ....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPF 129
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPF 103

REC_PhyR

cd17540

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...

29-141

9.43e-09

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: 53.41 E-value: 9.43e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVA-VAGTAAEGLSRFRETLPNVVLLDLMLPDR-NGLDLMQDMLRLRpETNVIVITA 106
Cdd:cd17540    3 VLIIEDEPLIAMDLEQIVEDLGHQVVgIARTRDEAVALARRERPDLILADIQLADGsSGIDAVNEILTTH-DVPVIFVTA 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499656124 107 ngsinkAVEAMRAGAHE---FLV-KPFDEQRFLGAVENA 141
Cdd:cd17540   82 ------YPERLLTGERPeptFLItKPFDPEMVKAAISQA 114

REC_Spo0A

cd17561

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...

53-129

1.47e-08

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

Pssm-ID: 381109 [Multi-domain] Cd Length: 108 Bit Score: 52.61 E-value: 1.47e-08

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499656124  53 VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDM--LRLRPETNVIVITANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd17561   30 VGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLrrMRLEKRPKIIMLTAFGQEDITQRAVELGASYYILKPF 108

CitB

COG2197

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...

29-114

1.54e-08

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: 52.97 E-value: 1.54e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAG--HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRpETNVIVITA 106
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLLTPR-EREVLRLLA 82


                 ....*...
gi 499656124 107 NGSINKAV 114
Cdd:COG2197   83 EGLSNKEI 90

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

190-329

1.92e-08

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: 53.15 E-value: 1.92e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124   190 TIFITGESGTGKELCALAVHDTSPRAAGPFIALNCGAIPQDLLESEVFGHVKGSFTG-----------AIADKPgaaaaa 258
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASgsgelrlrlalALARKL------ 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499656124   259 DGGTLFLDEICEMAPALQTKLLRFLQTSMvqpVGATRPRKVNVRIVCATNR--DPLDAVRRGHFREDLYYRLF 329
Cdd:smart00382  78 KPDVLILDEITSLLDAEQEALLLLLEELR---LLLLLKSEKNLTVILTTNDekDLGPALLRRRFDRRIVLLLI 147

REC_OmpR_ChvI-like

cd19936

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...

29-128

2.30e-08

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: 51.68 E-value: 2.30e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdmlRLRPETN--VIVITA 106
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQ---RLRQKSTlpVIFLTS 77

                         90       100
                 ....*....|....*....|..
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKP 128
Cdd:cd19936   78 KDDEIDEVFGLRMGADDYITKP 99

PRK10651

transcriptional regulator NarL; Provisional

26-143

3.09e-08

transcriptional regulator NarL; Provisional

Pssm-ID: 182619 [Multi-domain] Cd Length: 216 Bit Score: 53.88 E-value: 3.09e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  26 PRPILLIEDTPSLQMVYRSVLASAGHR--VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMqDMLRLRP-ETNVI 102
Cdd:PRK10651   6 PATILLIDDHPMLRTGVKQLISMAPDItvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETL-DKLREKSlSGRIV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499656124 103 VITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENASL 143
Cdd:PRK10651  85 VFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAA 125

REC_OmpR_BfmR-like

cd19939

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...

29-139

3.66e-08

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: 51.61 E-value: 3.66e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITANG 108
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCRE-VREHSHVPILMLTART 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPFDEQRFLGAVE 139
Cdd:cd19939   81 EEMDRVLGLEMGADDYLCKPFSPRELLARVR 111

REC_CpdR_CckA-like

cd18160

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...

29-129

4.21e-08

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: 50.96 E-value: 4.21e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLP-NVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITAN 107
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81

                         90       100
                 ....*....|....*....|..
gi 499656124 108 GSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd18160   82 AAAAPELLSDAVGDNATLKKPF 103

PRK10766

two-component system response regulator TorR;

29-140

6.22e-08

two-component system response regulator TorR;

Pssm-ID: 182711 [Multi-domain] Cd Length: 221 Bit Score: 53.12 E-value: 6.22e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITA-N 107
Cdd:PRK10766   5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRE-LRSRSTVGIILVTGrT 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499656124 108 GSINKAVeAMRAGAHEFLVKPFDEQRFLGAVEN 140
Cdd:PRK10766  84 DSIDRIV-GLEMGADDYVTKPLELRELLVRVKN 115

PRK10161

phosphate response regulator transcription factor PhoB;

27-139

6.79e-08

phosphate response regulator transcription factor PhoB;

Pssm-ID: 182277 [Multi-domain] Cd Length: 229 Bit Score: 53.18 E-value: 6.79e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  27 RPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLR--LRPETNVIVI 104
Cdd:PRK10161   3 RRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKResMTRDIPVVML 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVE 139
Cdd:PRK10161  83 TARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117

PRK10710

DNA-binding transcriptional regulator BaeR; Provisional

28-129

7.51e-08

DNA-binding transcriptional regulator BaeR; Provisional

Pssm-ID: 182665 [Multi-domain] Cd Length: 240 Bit Score: 53.15 E-value: 7.51e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  28 PILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITAn 107
Cdd:PRK10710  12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCRE-IRRFSDIPIVMVTA- 89

                         90       100
                 ....*....|....*....|....*..
gi 499656124 108 gsinKAVEAMR-----AGAHEFLVKPF 129
Cdd:PRK10710  90 ----KIEEIDRllgleIGADDYICKPY 112

ompR

PRK09468

osmolarity response regulator; Provisional

29-130

9.30e-08

osmolarity response regulator; Provisional

Pssm-ID: 181883 [Multi-domain] Cd Length: 239 Bit Score: 53.05 E-value: 9.30e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAaEGLSRF--RETLpNVVLLDLMLPDRNGLDLMQdmlRLRPETN---VIV 103
Cdd:PRK09468   8 ILVVDDDMRLRALLERYLTEQGFQVRSAANA-EQMDRLltRESF-HLMVLDLMLPGEDGLSICR---RLRSQNNptpIIM 82

                         90       100
                 ....*....|....*....|....*..
gi 499656124 104 ITANGSINKAVEAMRAGAHEFLVKPFD 130
Cdd:PRK09468  83 LTAKGEEVDRIVGLEIGADDYLPKPFN 109

PRK12555

chemotaxis-specific protein-glutamate methyltransferase CheB;

29-128

1.43e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;

Pssm-ID: 237135 [Multi-domain] Cd Length: 337 Bit Score: 53.35 E-value: 1.43e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLAS-AGHRVA-VAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPeTNVIVITA 106
Cdd:PRK12555   3 IGIVNDSPLAVEALRRALARdPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERP-CPILIVTS 81

                         90       100
                 ....*....|....*....|....
gi 499656124 107 NGSIN--KAVEAMRAGAHEFLVKP 128
Cdd:PRK12555  82 LTERNasRVFEAMGAGALDAVDTP 105

REC_CheC-like

cd17593

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...

30-132

2.08e-07

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

Pssm-ID: 381124 [Multi-domain] Cd Length: 117 Bit Score: 49.46 E-value: 2.08e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  30 LLIEDTPSL---QMVyRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITa 106
Cdd:cd17593    3 VLICDDSSMarkQLA-RALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS- 80

                         90       100
                 ....*....|....*....|....*...
gi 499656124 107 nGSIN-KAVE-AMRAGAHEFLVKPFDEQ 132
Cdd:cd17593   81 -GDVQpEAKErVLELGALAFLKKPFDPE 107

PRK11466

hybrid sensory histidine kinase TorS; Provisional

15-107

2.82e-07

hybrid sensory histidine kinase TorS; Provisional

Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 53.37 E-value: 2.82e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  15 RPAAGSAEASRP------RPILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLP-NVVLLDLMLPDRNGLD 87
Cdd:PRK11466 664 VATAPVPKTVNQavrldgLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPfAAALVDFDLPDYDGIT 743

                         90       100
                 ....*....|....*....|
gi 499656124  88 LMQDMLRLRPETNVIVITAN 107
Cdd:PRK11466 744 LARQLAQQYPSLVLIGFSAH 763

PRK09836

DNA-binding transcriptional activator CusR; Provisional

29-138

3.19e-07

DNA-binding transcriptional activator CusR; Provisional

Pssm-ID: 182102 [Multi-domain] Cd Length: 227 Bit Score: 51.08 E-value: 3.19e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPE-TNVIVITAN 107
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVR-MLRSANKgMPILLLTAL 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499656124 108 GSINKAVEAMRAGAHEFLVKPFDEQRFLGAV 138
Cdd:PRK09836  82 GTIEHRVKGLELGADDYLVKPFAFAELLARV 112

pleD

PRK09581

response regulator PleD; Reviewed

53-131

8.77e-07

response regulator PleD; Reviewed

Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 51.05 E-value: 8.77e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  53 VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---VIVITANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:PRK09581  29 VLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCR-RLKSDPATThipVVMVTALDDPEDRVRGLEAGADDFLTKPI 107


                 ..
gi 499656124 130 DE 131
Cdd:PRK09581 108 ND 109

PRK10336

two-component system response regulator QseB;

29-129

1.84e-06

two-component system response regulator QseB;

Pssm-ID: 182387 [Multi-domain] Cd Length: 219 Bit Score: 48.74 E-value: 1.84e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82

                         90       100
                 ....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPF 129
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPF 103

PRK15479

transcriptional regulator TctD;

29-130

1.95e-06

transcriptional regulator TctD;

Pssm-ID: 185376 [Multi-domain] Cd Length: 221 Bit Score: 48.95 E-value: 1.95e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVA--GTAAEGLsrFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPET-NVIVIT 105
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAVDCVfdGLAADHL--LQSEMYALAVLDINMPGMDGLEVLQ-RLRKRGQTlPVLLLT 79

                         90       100
                 ....*....|....*....|....*
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKPFD 130
Cdd:PRK15479  80 ARSAVADRVKGLNVGADDYLPKPFE 104

REC_CheY_CheY3

cd19923

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...

29-132

2.64e-06

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: 46.18 E-value: 2.64e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHR-VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdmlRLRPETN-----VI 102
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLK---TIRADGAlshlpVL 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 499656124 103 VITANGSINKAVEAMRAGAHEFLVKPFDEQ 132
Cdd:cd19923   80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAA 109

REC_Ycf29

cd19927

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...

29-128

3.38e-06

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: 45.45 E-value: 3.38e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLRLRPETN---VIVIT 105
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLG-KLRKNADFDtipVIFLT 79

                         90       100
                 ....*....|....*....|...
gi 499656124 106 ANGSINKAVEAMRAGAHEFLVKP 128
Cdd:cd19927   80 AKGMTSDRIKGYNAGCDGYLSKP 102

REC_RitR-like

cd19922

receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...

29-129

4.41e-06

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

Pssm-ID: 381149 [Multi-domain] Cd Length: 110 Bit Score: 45.55 E-value: 4.41e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd19922    1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDHWE 80

                         90       100
                 ....*....|....*....|.
gi 499656124 109 SINKAVEAMRAGAHEFLVKPF 129
Cdd:cd19922   81 DLQEELEEVQRFAVSYVVKPV 101

REC_PatA-like

cd17602

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...

29-128

4.83e-06

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

Pssm-ID: 381129 [Multi-domain] Cd Length: 102 Bit Score: 45.05 E-value: 4.83e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQdMLR----LRpETNVIVI 104
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCS-LLRkssaLK-DTPIIML 78

                         90       100
                 ....*....|....*....|....
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKP 128
Cdd:cd17602   79 TGKDGLVDRIRAKMAGASGYLTKP 102

REC_TPR

cd17589

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...

29-129

6.54e-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: 44.95 E-value: 6.54e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAG-HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPD-RNGLDLMQDmLR----LRPETNVI 102
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGvTRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEE-LRhkklISPSTVFI 79

                         90       100
                 ....*....|....*....|....*..
gi 499656124 103 VITANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:cd17589   80 MVTGESSRAMVLSALELEPDDYLLKPF 106

PRK09191

two-component response regulator; Provisional

29-106

7.11e-06

two-component response regulator; Provisional

Pssm-ID: 236402 [Multi-domain] Cd Length: 261 Bit Score: 47.54 E-value: 7.11e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVA-VAGTAAEGLSRFRETLPNVVLLDLMLPD-RNGLDLMQDMLRLRpETNVIVITA 106
Cdd:PRK09191 140 VLIIEDEPIIAMDLEQLVESLGHRVTgIARTRAEAVALAKKTRPGLILADIQLADgSSGIDAVNDILKTF-DVPVIFITA 218

REC_DesR-like

cd19930

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...

53-127

1.08e-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: 44.57 E-value: 1.08e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499656124  53 VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGSINKAVEAMRAGAHEFLVK 127
Cdd:cd19930   27 VAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTTFGRPGYFRRALAAGVDGYVLK 101

REC_OmpR_NsrR-like

cd18159

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...

29-130

1.09e-05

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

Pssm-ID: 381143 [Multi-domain] Cd Length: 113 Bit Score: 44.58 E-value: 1.09e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMlrlRPETNV--IVITA 106
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREI---RQISNVpiIFISS 77

                         90       100
                 ....*....|....*....|....
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFD 130
Cdd:cd18159   78 RDDNMDQVMAINMGGDDYITKPFD 101

PRK10610

chemotaxis protein CheY;

30-129

1.11e-05

chemotaxis protein CheY;

Pssm-ID: 170568 [Multi-domain] Cd Length: 129 Bit Score: 44.97 E-value: 1.11e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  30 LLIEDTPSLQMVYRSVLASAG-HRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDM-----LRLRPetnVIV 103
Cdd:PRK10610   9 LVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIradgaMSALP---VLM 85

                         90       100
                 ....*....|....*....|....*.
gi 499656124 104 ITANGSINKAVEAMRAGAHEFLVKPF 129
Cdd:PRK10610  86 VTAEAKKENIIAAAQAGASGYVVKPF 111

PRK10430

two-component system response regulator DcuR;

29-134

1.46e-05

two-component system response regulator DcuR;

Pssm-ID: 182454 [Multi-domain] Cd Length: 239 Bit Score: 46.25 E-value: 1.46e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLA--SAGHRVAVAGTaaegLSRFRETLPN------VVLLDLMLPDRNGLDLMQDMLRLRPETN 100
Cdd:PRK10430   4 VLIVDDDAMVAELNRRYVAqiPGFQCCGTAST----LEQAKEIIFNsdtpidLILLDIYMQQENGLDLLPVLHEAGCKSD 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124 101 VIVITANGSINKAVEAMRAGAHEFLVKPFDEQRF 134
Cdd:PRK10430  80 VIVISSAADAATIKDSLHYGVVDYLIKPFQASRF 113

PRK10403

nitrate/nitrite response regulator protein NarP;

26-138

2.16e-05

nitrate/nitrite response regulator protein NarP;

Pssm-ID: 182431 [Multi-domain] Cd Length: 215 Bit Score: 45.61 E-value: 2.16e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  26 PRPILLIEDTPSLQMVYRSVLAS-AGHRV-AVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIV 103
Cdd:PRK10403   6 PFQVLIVDDHPLMRRGVRQLLELdPGFEVvAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIII 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499656124 104 ITANGSINKAVEAMRAGAHEFLVKPFDEQRFLGAV 138
Cdd:PRK10403  86 LTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAI 120

PRK13557

histidine kinase; Provisional

10-129

5.07e-05

histidine kinase; Provisional

Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 45.82 E-value: 5.07e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  10 SEGHARPAAGSAEASRPRP----ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFrETLPNVVLL--DLMLP-D 82
Cdd:PRK13557 395 SDQAENPEQEPKARAIDRGgtetILIVDDRPDVAELARMILEDFGYRTLVASNGREALEIL-DSHPEVDLLftDLIMPgG 473

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499656124  83 RNGLDLMQDMLRLRPETNVIVITanGSINKAVEAMRAGAHEFLV--KPF 129
Cdd:PRK13557 474 MNGVMLAREARRRQPKIKVLLTT--GYAEASIERTDAGGSEFDIlnKPY 520

REC_HupR

cd17596

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...

29-141

5.34e-05

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: 43.12 E-value: 5.34e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASaGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANG 108
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499656124 109 SINKAVEAMR-AGAHEFLVKPFDEQRFLGAVENA 141
Cdd:cd17596   82 DSEDIIAGINeAGIYQYLTKPWHPDQLLLTVRNA 115

PRK09958

acid-sensing system DNA-binding response regulator EvgA;

30-141

6.19e-05

acid-sensing system DNA-binding response regulator EvgA;

Pssm-ID: 182168 [Multi-domain] Cd Length: 204 Bit Score: 44.12 E-value: 6.19e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  30 LLIEDTPSLQMVYRSVLASagHRVAVAGTAAEG---LSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIK--NDIEILAELTEGgsaVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSA 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499656124 107 NGSINKAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:PRK09958  82 KNDHFYGKHCADAGANGFVSKKEGMNNIIAAIEAA 116

REC_2_GGDEF

cd17544

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...

29-129

7.07e-05

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: 42.51 E-value: 7.07e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETlPNV--VLLDLMLPDRNGLDLMQDMLRLRPETNVIVITA 106
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQH-PDIklVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81

                         90       100
                 ....*....|....*....|....*
gi 499656124 107 NGSINKAVEA--MRAGAHEFLVKPF 129
Cdd:cd17544   82 SASGDNALSArfIKAGANDFLTKPF 106

psREC_PRR

cd17582

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...

29-128

1.61e-04

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

Pssm-ID: 381120 [Multi-domain] Cd Length: 104 Bit Score: 40.85 E-value: 1.61e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNV--VLLDLMLPDRNGLDLMQDMLRLRPETN--VIVI 104
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIdlILTEVDLPVSSGFKLLSYIMRHKICKNipVIMM 80

                         90       100
                 ....*....|....*....|....
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKP 128
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104

PRK09483

response regulator; Provisional

55-127

2.34e-04

response regulator; Provisional

Pssm-ID: 236538 [Multi-domain] Cd Length: 217 Bit Score: 42.40 E-value: 2.34e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499656124  55 VAGTAAEG---LSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGSINKAVEAMRAGAHEFLVK 127
Cdd:PRK09483  29 VVGEACCGedaVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLTVHTENPLPAKVMQAGAAGYLSK 104

PRK14084

DNA-binding response regulator;

72-141

2.71e-04

DNA-binding response regulator;

Pssm-ID: 184495 [Multi-domain] Cd Length: 246 Bit Score: 42.43 E-value: 2.71e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  72 NVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGSInkAVEAMRAGAHEFLVKPFDEQRFLGAVENA 141
Cdd:PRK14084  48 DIIFLDINLMDESGIELAAKIQKMKEPPAIIFATAHDQF--AVKAFELNATDYILKPFEQKRIEQAVNKV 115

PRK00742

chemotaxis-specific protein-glutamate methyltransferase CheB;

53-129

4.32e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;

Pssm-ID: 234828 [Multi-domain] Cd Length: 354 Bit Score: 42.44 E-value: 4.32e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  53 VAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPeTNVIVI---TANGSiNKAVEAMRAGAHEFLVKPF 129
Cdd:PRK00742  32 VGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRP-TPVVMVsslTERGA-EITLRALELGAVDFVTKPF 109

PRK10693

two-component system response regulator RssB;

54-128

5.88e-04

two-component system response regulator RssB;

Pssm-ID: 182652 [Multi-domain] Cd Length: 303 Bit Score: 41.90 E-value: 5.88e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499656124  54 AVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGSINKAVEAMRAGAHEFLVKP 128
Cdd:PRK10693   1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75

REC_GlnL-like

cd17565

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...

54-128

5.92e-04

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

Pssm-ID: 381112 [Multi-domain] Cd Length: 103 Bit Score: 39.18 E-value: 5.92e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499656124  54 AVAGTAAEGLSRFRETL---PNVVLLDLMLPDRNGLDLMQDMLRLRPETNVIVITANGSINKAVEAMRAGAHEFLVKP 128
Cdd:cd17565   25 EVVGEADNGAQAYDEILflqPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQVSDKEMIGKAYQAGIEFFINKP 102

PRK15347

two component system sensor kinase;

29-128

7.06e-04

two component system sensor kinase;

Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 42.32 E-value: 7.06e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQ----DMLRLRPETNVIVI 104
Cdd:PRK15347 693 ILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQlwrdDPNNLDPDCMIVAL 772

                         90       100
                 ....*....|....*....|....
gi 499656124 105 TANGSINKAVEAMRAGAHEFLVKP 128
Cdd:PRK15347 773 TANAAPEEIHRCKKAGMNHYLTKP 796

REC_TrxB

cd17595

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...

29-134

4.82e-03

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

Pssm-ID: 381126 [Multi-domain] Cd Length: 135 Bit Score: 37.32 E-value: 4.82e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPS-LQMVYRSVLASAG--HRVAVAGTAAEGLSRFREtLPN------VVLLDLMLPDRNGLDLMQDMLRLRPET 99
Cdd:cd17595    3 ILTVDDDPQvLRAVARDLRRQYGkdYRVLRADSGAEALDALKE-LKLrgeavaLFLVDQRMPEMDGVEFLEKAMELFPEA 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499656124 100 NVIVITANGSINKAVEAMR-AGAHEFLVKPFD--EQRF 134
Cdd:cd17595   82 KRVLLTAYADTDAAIRAINdVQLDYYLLKPWDppEEKL 119

REC_WspR-like

cd17575

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...

68-127

5.46e-03

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

Pssm-ID: 381117 [Multi-domain] Cd Length: 128 Bit Score: 37.00 E-value: 5.46e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499656124  68 ETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETN---VIVITANGSINKAVEAMRAGAHEFLVK 127
Cdd:cd17575   43 QIKPTVILQDLVMPGVDGLTLVRF-FRANPATRdipIIVLSTKEEPEVKSEAFALGANDYLVK 104

PRK11173

two-component response regulator; Provisional

29-130

5.89e-03

two-component response regulator; Provisional

Pssm-ID: 183013 [Multi-domain] Cd Length: 237 Bit Score: 38.46 E-value: 5.89e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmlrLRPETNVIVITANG 108
Cdd:PRK11173   6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARE---LREQANVALMFLTG 82

                         90       100
                 ....*....|....*....|....
gi 499656124 109 SINKA--VEAMRAGAHEFLVKPFD 130
Cdd:PRK11173  83 RDNEVdkILGLEIGADDYITKPFN 106

PRK10701

DNA-binding transcriptional regulator RstA; Provisional

29-127

7.94e-03

DNA-binding transcriptional regulator RstA; Provisional

Pssm-ID: 236738 [Multi-domain] Cd Length: 240 Bit Score: 38.08 E-value: 7.94e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656124  29 ILLIEDTPSLQMVYRSVLASAGHRVAVAGTAAEGLSRFRETLPNVVLLDLMLPDRNGLDLMQDmLRLRPETNVIVITANG 108
Cdd:PRK10701   4 IVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRD-LRPKWQGPIVLLTSLD 82

                         90
                 ....*....|....*....
gi 499656124 109 SINKAVEAMRAGAHEFLVK 127
Cdd:PRK10701  83 SDMNHILALEMGACDYILK 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