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Conserved domains on  [gi|1100968853|ref|WP_071476248|]
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MULTISPECIES: sigma-54 dependent transcriptional regulator [Shewanella]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
7-443 0e+00

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


:

Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 527.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRklkqelesqslPGPRILGNSPGIRQMRHLIHQVLD 166
Cdd:COG2204    84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENA-----------EDSGLIGRSPAMQEVRRLIEKVAP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 167 TPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFLD 246
Cdd:COG2204   153 SDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 247 EIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIP 326
Cdd:COG2204   233 EIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 327 LLFLHFARIASARYHKAlIALGGEQQARLSTHEWPGNVRELRNLAERYVLLGAEaafaGAIGSSDslqsgmsLTQRVEFF 406
Cdd:COG2204   313 LLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADG----EVITAED-------LPEALEEV 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1100968853 407 ERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKY 443
Cdd:COG2204   381 ERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
7-443 0e+00

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 527.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRklkqelesqslPGPRILGNSPGIRQMRHLIHQVLD 166
Cdd:COG2204    84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENA-----------EDSGLIGRSPAMQEVRRLIEKVAP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 167 TPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFLD 246
Cdd:COG2204   153 SDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 247 EIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIP 326
Cdd:COG2204   233 EIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 327 LLFLHFARIASARYHKAlIALGGEQQARLSTHEWPGNVRELRNLAERYVLLGAEaafaGAIGSSDslqsgmsLTQRVEFF 406
Cdd:COG2204   313 LLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADG----EVITAED-------LPEALEEV 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1100968853 407 ERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKY 443
Cdd:COG2204   381 ERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
6-446 9.66e-129

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 380.35  E-value: 9.66e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITG 85
Cdd:PRK11361    5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQELeSQSLPGPRILGNSPGIRQMRHLIHQVL 165
Cdd:PRK11361   85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQAL-STSWQWGHILTNSPAMMDICKDTAKIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 166 DTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFL 245
Cdd:PRK11361  164 LSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 246 DEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDI 325
Cdd:PRK11361  244 DEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDI 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 326 PLLFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVLLGAEAAF------------AGAIGSSDSL 393
Cdd:PRK11361  324 SLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIfsedlppqirqpVCNAGEVKTA 403
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1100968853 394 QSG-MSLTQRVEFFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKYALE 446
Cdd:PRK11361  404 PVGeRNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
8-441 1.27e-126

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: 375.23  E-value: 1.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSltlENRKLKQElESQSLPGPRILGNSPGIRQMRHLIHQVLDT 167
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQ---EQVALPAD-AGEAEDSAELIGEAPAMQEVFRAIGRLSRS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 168 PADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFLDE 247
Cdd:TIGR01818 157 DITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 248 IESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIPL 327
Cdd:TIGR01818 237 IGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 328 LFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVLLG-----------AEAAFAGAIGSSDSLQSG 396
Cdd:TIGR01818 317 LARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMAsgdevlvsdlpAELALTGRPASAPDSDGQ 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100968853 397 MSLTQRVE--------------------FFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMR 441
Cdd:TIGR01818 397 DSWDEALEawakqalsrgeqglldralpEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLK 461
Sigma54_activat pfam00158
Sigma-54 interaction domain;
147-313 3.89e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 301.63  E-value: 3.89e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 147 ILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTG 226
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 227 ADKTRIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFY 306
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 1100968853 307 RLNLVTV 313
Cdd:pfam00158 161 RLNVIPI 167
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
8-137 8.83e-70

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: 217.36  E-value: 8.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQEL 137
Cdd:cd17549    81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
171-287 4.54e-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: 51.99  E-value: 4.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  171 ILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIES---ELFGAEAGAFTGADKTRIG--KFEYANGGTLFL 245
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLIL 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1100968853  246 DEIESTPMALQVKLLRVLEDrrvERLGSNKSIALDIRVIAAT 287
Cdd:smart00382  85 DEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTT 123
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
7-443 0e+00

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 527.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRklkqelesqslPGPRILGNSPGIRQMRHLIHQVLD 166
Cdd:COG2204    84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENA-----------EDSGLIGRSPAMQEVRRLIEKVAP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 167 TPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFLD 246
Cdd:COG2204   153 SDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 247 EIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIP 326
Cdd:COG2204   233 EIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 327 LLFLHFARIASARYHKAlIALGGEQQARLSTHEWPGNVRELRNLAERYVLLGAEaafaGAIGSSDslqsgmsLTQRVEFF 406
Cdd:COG2204   313 LLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADG----EVITAED-------LPEALEEV 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1100968853 407 ERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKY 443
Cdd:COG2204   381 ERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
129-446 1.03e-141

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: 413.01  E-value: 1.03e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 129 ENRKLKQELESQSLPGPR--------ILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFV 200
Cdd:COG3829   114 ELKRLERKLREEELERGLsakytfddIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFV 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 201 AINCGAIPENIIESELFGAEAGAFTGADKT-RIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIAL 279
Cdd:COG3829   194 AVNCAAIPENLLESELFGYEKGAFTGAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPV 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 280 DIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIPLLFLHFARIASARYHKALIALGGEQQARLSTHE 359
Cdd:COG3829   274 DVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYD 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 360 WPGNVRELRNLAERYVLLGAE--------AAFAGAIGSSDSLQSGMSLTQRVEFFERLLIEEALAHNKGSIKLTMEQLEL 431
Cdd:COG3829   354 WPGNVRELENVIERAVVLSEGdvitpehlPEYLLEEAEAASAAEEGSLKEALEEVEKELIEEALEKTGGNKSKAAKALGI 433
                         330
                  ....*....|....*
gi 1100968853 432 PRKTLYDKMRKYALE 446
Cdd:COG3829   434 SRSTLYRKLKKYGIK 448
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
6-446 9.66e-129

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 380.35  E-value: 9.66e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITG 85
Cdd:PRK11361    5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQELeSQSLPGPRILGNSPGIRQMRHLIHQVL 165
Cdd:PRK11361   85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQAL-STSWQWGHILTNSPAMMDICKDTAKIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 166 DTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFL 245
Cdd:PRK11361  164 LSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 246 DEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDI 325
Cdd:PRK11361  244 DEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDI 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 326 PLLFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVLLGAEAAF------------AGAIGSSDSL 393
Cdd:PRK11361  324 SLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIfsedlppqirqpVCNAGEVKTA 403
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1100968853 394 QSG-MSLTQRVEFFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKYALE 446
Cdd:PRK11361  404 PVGeRNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
8-441 1.27e-126

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: 375.23  E-value: 1.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSltlENRKLKQElESQSLPGPRILGNSPGIRQMRHLIHQVLDT 167
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQ---EQVALPAD-AGEAEDSAELIGEAPAMQEVFRAIGRLSRS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 168 PADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFLDE 247
Cdd:TIGR01818 157 DITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 248 IESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIPL 327
Cdd:TIGR01818 237 IGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 328 LFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVLLG-----------AEAAFAGAIGSSDSLQSG 396
Cdd:TIGR01818 317 LARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMAsgdevlvsdlpAELALTGRPASAPDSDGQ 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100968853 397 MSLTQRVE--------------------FFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMR 441
Cdd:TIGR01818 397 DSWDEALEawakqalsrgeqglldralpEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLK 461
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
8-445 5.66e-118

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: 352.51  E-value: 5.66e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQpkEILRHLSRDWMGIVITDVNMP-----GMDGISVMQQIKQLDADLPVIL 82
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFADYELAVAADRE--SAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQELESQSLPGprILGNSPGIRQMRHLIH 162
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRG--LITSSPGMQKICRTIE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 163 QVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGT 242
Cdd:TIGR02915 157 KIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 243 LFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERR 322
Cdd:TIGR02915 237 LFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRD 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 323 EDIPLLFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVLLGAEAAFAGA-----IGSSDSLQSGM 397
Cdd:TIGR02915 317 GDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEdlgldARERAETPLEV 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1100968853 398 SLTQRVEFFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKYAL 445
Cdd:TIGR02915 397 NLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
143-443 6.40e-107

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 329.94  E-value: 6.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 143 PGPRILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAG 222
Cdd:COG3284   319 ALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPG 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 223 AFTGADKT-RIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFR 301
Cdd:COG3284   399 AFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFR 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 302 EDLFYRLNLVTVAIPPLRErREDIPLLFLHFARIASARYHkaLIALGGEQQARLSTHEWPGNVRELRNLAERYVLLgaea 381
Cdd:COG3284   479 EDLYYRLNGLTLTLPPLRE-REDLPALIEHLLRELAAGRG--PLRLSPEALALLAAYPWPGNVRELRNVLRTALAL---- 551
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100968853 382 AFAGAIGSSD---SLQSGMSLTQRVEFF--------ERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKY 443
Cdd:COG3284   552 ADGGVITVEDlpdELRAELAAAAPAAAApltsleeaERDAILRALRACGGNVSAAARALGISRSTLYRKLKRY 624
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-442 4.37e-106

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 321.98  E-value: 4.37e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   1 MSEQEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPV 80
Cdd:PRK10365    1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  81 ILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALdkrsltLENRKLKQELESQSLPGPRILGNSPGIRQMRHL 160
Cdd:PRK10365   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL------AHTHSIDAETPAVTASQFGMVGKSPAMQHLLSE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 161 IHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANG 240
Cdd:PRK10365  155 IALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 241 GTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRE 320
Cdd:PRK10365  235 GTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 321 RREDIPLLFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVLLG-----AEAAFAGAIGSSDSLQS 395
Cdd:PRK10365  315 RREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLtgeyiSERELPLAIASTPIPLG 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1100968853 396 GMSLTQRVEFFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRK 442
Cdd:PRK10365  395 QSQDIQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
4-446 5.11e-104

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 317.58  E-value: 5.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   4 QEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILI 83
Cdd:PRK10923    2 QRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  84 TGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALdkrSLTLEnrklKQELESQSLPGP--RILGNSPGIRQMRHLI 161
Cdd:PRK10923   82 TAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI---SHYQE----QQQPRNIQVNGPttDIIGEAPAMQDVFRII 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 162 HQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGG 241
Cdd:PRK10923  155 GRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 242 TLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRER 321
Cdd:PRK10923  235 TLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRER 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 322 REDIPLLFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVLLGAEAA----------FAGAIGSS- 390
Cdd:PRK10923  315 REDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEvliqdlpgelFESTVPESt 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100968853 391 -----------------DSLQSGMS--LTQRVEFFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKYALE 446
Cdd:PRK10923  395 sqmqpdswatllaqwadRALRSGHQnlLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
PRK15115 PRK15115
response regulator GlrR; Provisional
1-377 2.22e-102

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 312.54  E-value: 2.22e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   1 MSEQEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPV 80
Cdd:PRK15115    1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  81 ILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQelesqslpgprILGNSPGIRQMRHL 160
Cdd:PRK15115   81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDERWREA-----------IVTRSPLMLRLLEQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 161 IHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANG 240
Cdd:PRK15115  150 ARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 241 GTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRE 320
Cdd:PRK15115  230 GTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAE 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1100968853 321 RREDIPLLFLHFARIASARyHKALI-ALGGEQQARLSTHEWPGNVRELRNLAERYVLL 377
Cdd:PRK15115  310 RTEDIPLLANHLLRQAAER-HKPFVrAFSTDAMKRLMTASWPGNVRQLVNVIEQCVAL 366
Sigma54_activat pfam00158
Sigma-54 interaction domain;
147-313 3.89e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 301.63  E-value: 3.89e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 147 ILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTG 226
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 227 ADKTRIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFY 306
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 1100968853 307 RLNLVTV 313
Cdd:pfam00158 161 RLNVIPI 167
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
119-437 2.85e-94

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 293.62  E-value: 2.85e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 119 RALDKRSLtlENRKLKQELESQSLPGPRILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGAN 198
Cdd:PRK05022  163 EQLESQAE--LPQDVAEFLRQEALKEGEMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKP 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 199 FVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIA 278
Cdd:PRK05022  241 LVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLR 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 279 LDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIPLLFLHFARIASARYHKALIALGGEQQARLSTH 358
Cdd:PRK05022  321 VDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAY 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 359 EWPGNVRELRNLAERYVLL--------------------GAEAAFAGAIGSSDSLQSGMSLTQRVEFFERLLIEEALAHN 418
Cdd:PRK05022  401 DWPGNVRELEHVISRAALLarargagrivtleaqhldlpAEVALPPPEAAAAPAAVVSQNLREATEAFQRQLIRQALAQH 480
                         330
                  ....*....|....*....
gi 1100968853 419 KGSIKLTMEQLELPRKTLY 437
Cdd:PRK05022  481 QGNWAAAARALELDRANLH 499
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
146-412 7.93e-90

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 282.46  E-value: 7.93e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 146 RILGNSPgirQMRHLIHQ-----VLDTPadILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAE 220
Cdd:COG3283   205 HIVASSP---KMRQVIRQakkmaMLDAP--LLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYA 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 221 AGAFTGADKTRIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSF 300
Cdd:COG3283   280 PGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEF 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 301 REDLFYRLNLVTVAIPPLRERREDIPLLFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRN-------LAER 373
Cdd:COG3283   360 REDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENalyravsLLEG 439
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1100968853 374 YVlLGAE----AAFAGAIGSSDSLQSGmSLTQRVEFFERLLIE 412
Cdd:COG3283   440 DE-LTPEdlqlPEYAASAGLLDDLLEG-SLDEIVKRFERSLLR 480
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
120-402 3.27e-88

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: 278.91  E-value: 3.27e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 120 ALDKRSLTLENRKLKQELESQSLPGPR--------ILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDH 191
Cdd:TIGR01817 163 AQRRERLIAEAVQLSKQLRDKAPEIARrrsgkedgIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYL 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 192 SPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFLDEI-ESTPmALQVKLLRVLEDRRVER 270
Cdd:TIGR01817 243 SPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIgEISP-AFQAKLLRVLQEGEFER 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 271 LGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIPLLFLHFARIASARYHKALiALGGE 350
Cdd:TIGR01817 322 VGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPL-TITPS 400
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1100968853 351 QQARLSTHEWPGNVRELRNLAERYVLLGAEaafaGAIGSSD-SLQSGMSLTQR 402
Cdd:TIGR01817 401 AIRVLMSCKWPGNVRELENCLERTATLSRS----GTITRSDfSCQSGQCLSPM 449
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
147-447 1.36e-87

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 277.37  E-value: 1.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 147 ILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLH-DHSPRHGAN-------FVAINCGAIPENIIESELFG 218
Cdd:PRK15424  221 LLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHrEYFARHDARqgkkshpFVAVNCGAIAESLLEAELFG 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 219 AEAGAFTGADKT-RIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQ 297
Cdd:PRK15424  301 YEEGAFTGSRRGgRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQ 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 298 GSFREDLFYRLNLVTVAIPPLRERREDIPLLFLHFARIA----SARYHKALIALGGEQQARLSTHEWPGNVRELRNLAER 373
Cdd:PRK15424  381 GRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSlaalSAPFSAALRQGLQQCETLLLHYDWPGNVRELRNLMER 460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 374 YVL-LGAEAAFAgaiGSSDSLQSGMSLTQRVEF------FERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKYALE 446
Cdd:PRK15424  461 LALfLSVEPTPD---LTPQFLQLLLPELARESAktpaprLLAATLQQALERFNGDKTAAANYLGISRTTLWRRLKAEAKA 537

                  .
gi 1100968853 447 R 447
Cdd:PRK15424  538 Q 538
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
147-442 5.29e-82

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: 262.49  E-value: 5.29e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 147 ILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTG 226
Cdd:TIGR02329 214 LLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTG 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 227 ADKT-RIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLF 305
Cdd:TIGR02329 294 ARRGgRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLF 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 306 YRLNLVTVAIPPLRERREDIPLLFLHFARIA----SARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVL-LGAE 380
Cdd:TIGR02329 374 YRLSILRIALPPLRERPGDILPLAAEYLVQAaaalRLPDSEAAAQVLAGVADPLQRYPWPGNVRELRNLVERLALeLSAM 453
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1100968853 381 AAFA------------GAIGSSDSLQSGMSLTQRvEFFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRK 442
Cdd:TIGR02329 454 PAGAltpdvlralapeLAEASGKGKTSALSLRER-SRVEALAVRAALERFGGDRDAAAKALGISRTTLWRRLKA 526
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
123-377 8.58e-73

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 242.43  E-value: 8.58e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 123 KRSLTLENRKLKQELESQSLPGPRILGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAI 202
Cdd:PRK15429  354 KERLVDENLALTEQLNNVDSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKM 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 203 NCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIR 282
Cdd:PRK15429  434 NCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVR 513
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 283 VIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERREDIPLLFLHFARIASARYHKALIALGGEQQARLSTHEWPG 362
Cdd:PRK15429  514 LIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPG 593
                         250
                  ....*....|....*
gi 1100968853 363 NVRELRNLAERYVLL 377
Cdd:PRK15429  594 NVRELENVIERAVLL 608
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
165-375 2.74e-71

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 228.40  E-value: 2.74e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 165 LDTPadILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKFEYANGGTLF 244
Cdd:PRK11608   28 LDKP--VLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRFERADGGTLF 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 245 LDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERRED 324
Cdd:PRK11608  106 LDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQLPPLRERQSD 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1100968853 325 IPLLFLHFArIASARYHKALIALGGEQQAR--LSTHEWPGNVRELRNLAERYV 375
Cdd:PRK11608  186 IMLMAEHFA-IQMCRELGLPLFPGFTERARetLLNYRWPGNIRELKNVVERSV 237
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
163-446 6.28e-70

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: 225.11  E-value: 6.28e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 163 QVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESelfgaeagaftgadktrigkfeyanggt 242
Cdd:COG3604   110 ETLASLAAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES---------------------------- 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 243 lfldeiestpmalqvkllrvLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLVTVAIPPLRERR 322
Cdd:COG3604   162 --------------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERR 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 323 EDIPLLFLHFARIASARYHKALIALGGEQQARLSTHEWPGNVRELRNLAERYVLLgaeaAFAGAIGSSDSLQSGMsltQR 402
Cdd:COG3604   222 EDIPLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVIL----AEGGVLDADDLAPGSR---EA 294
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1100968853 403 VEFFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKYALE 446
Cdd:COG3604   295 LEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
8-137 8.83e-70

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: 217.36  E-value: 8.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQEL 137
Cdd:cd17549    81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
PRK10820 PRK10820
transcriptional regulator TyrR;
147-448 2.87e-64

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 215.71  E-value: 2.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 147 ILGNSPgirQMRHLIHQ-----VLDTPadILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEA 221
Cdd:PRK10820  206 IVAVSP---KMRQVVEQarklaMLDAP--LLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAP 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 222 GAFTGADKTRIGKFEYANGGTLFLDEI-ESTPMaLQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSF 300
Cdd:PRK10820  281 GAYPNALEGKKGFFEQANGGSVLLDEIgEMSPR-MQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEF 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 301 REDLFYRLNLVTVAIPPLRERREDI-PLLFLHFARIASARyHKALIALGGEQQARLSTHEWPGNVRELRNLAERYV--LL 377
Cdd:PRK10820  360 REDLYYRLNVLTLNLPPLRDRPQDImPLTELFVARFADEQ-GVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALtqLE 438
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1100968853 378 GAE--------AAFAGAIGSSDSLQSGmSLTQRVEFFERLLIEEALAHNKGSIKLTmEQLELPRKTLYDKMRKYALERK 448
Cdd:PRK10820  439 GYElrpqdillPDYDAAVAVGEDAMEG-SLDEITSRFERSVLTRLYRNYPSTRKLA-KRLGVSHTAIANKLREYGLSQK 515
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
155-451 2.32e-56

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 197.21  E-value: 2.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 155 RQMRHLIH---QVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGaeaGAFTGADKTR 231
Cdd:PRK11388  332 PQMRRLIHfgrQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SDRTDSENGR 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 232 IGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNLV 311
Cdd:PRK11388  409 LSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAF 488
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 312 TVAIPPLRERREDIPLLFLHFARIASARYHKALiALGGEQQARLSTHEWPGNVRELRNLAERyVLLGAEaafAGAIGSSD 391
Cdd:PRK11388  489 EITIPPLRMRREDIPALVNNKLRSLEKRFSTRL-KIDDDALARLVSYRWPGNDFELRSVIEN-LALSSD---NGRIRLSD 563
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100968853 392 ----------SLQSGMSLTQRVEFF---ERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRKYALERKDYL 451
Cdd:PRK11388  564 lpehlfteqaTDDVSATRLSTSLSLaelEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGIDAGQFK 636
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
7-138 3.62e-36

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: 131.76  E-value: 3.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGH 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQELE 138
Cdd:COG4566    81 GDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELR 132
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
6-121 1.02e-34

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: 125.40  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITG 85
Cdd:cd17537     1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17537    81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
161-367 1.16e-33

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: 132.65  E-value: 1.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 161 IHQV-LDTPADILIEGETGTGKELVARYLHD-HSPRH--GANFVAINC------GAIpeniieSELFGAEAGAFTGADKT 230
Cdd:COG4650   200 IERVaIRSRAPILLTGPTGAGKSQLARRIYElKKARHqvSGRFVEVNCatlrgdGAM------SALFGHVKGAFTGAVSD 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 231 RIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNKSIALDIRVIAATKVDLKELCRQGSFREDLFYRLNL 310
Cdd:COG4650   274 RAGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINL 353
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100968853 311 VTVAIPPLRERREDIP--LLFL--HFARI----------ASARYhkalIALGGEQQARlstheWPGNVREL 367
Cdd:COG4650   354 WTFRLPGLAERREDIEpnLDYElaRFAREqgrrvrfnkeARARY----LAFATSPEAL-----WSGNFRDL 415
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
8-122 3.06e-32

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: 118.75  E-value: 3.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALD 122
Cdd:cd17550    81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
7-121 6.55e-30

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: 112.37  E-value: 6.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd19919    82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
8-118 4.46e-29

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: 109.93  E-value: 4.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVK 118
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
2-142 8.22e-29

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: 112.95  E-value: 8.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   2 SEQEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD--ADLP 79
Cdd:COG3437     3 TGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPstRDIP 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100968853  80 VILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQELESQSL 142
Cdd:COG3437    83 VIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAP 145
fixJ PRK09390
response regulator FixJ; Provisional
5-156 2.20e-26

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 105.47  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   5 EYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILIT 84
Cdd:PRK09390    3 KGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMT 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRsltleNRKLKQELESQSLPGpRILGNSPGIRQ 156
Cdd:PRK09390   83 GHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQA-----PEAAKSEAVAADIRA-RIASLSERERQ 148
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
9-107 8.04e-26

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: 100.76  E-value: 8.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   9 LILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFGD 88
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                          90
                  ....*....|....*....
gi 1100968853  89 IAMAVSAVKQGAYDFLEKP 107
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-125 1.28e-24

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: 98.38  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   1 MSEQEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD--ADL 78
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPrlPDI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1100968853  79 PVILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRS 125
Cdd:COG0784    81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
6-119 1.62e-23

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: 96.90  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD--ADLPVILI 83
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPrtADIPIIFL 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1100968853  84 TGFGDIAMAVSAVKQGAYDFLEKPFNNEHIL---DVVKR 119
Cdd:COG3706    82 TALDDEEDRARALEAGADDYLTKPFDPEELLarvDLVAR 120
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
6-121 1.66e-23

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 94.86  E-value: 1.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEGISAK-ASTQPK--EILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVIL 82
Cdd:COG5803     3 KKILIVDDQAGIRMLLKEVLKKEGYEVFqAANGKEalEKVKELKPD---LVLLDMKMPGMDGIEILKEIKEIDPDIPVIM 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:COG5803    80 MTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
6-122 1.76e-23

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: 94.78  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITG 85
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1100968853  86 FGDIAMAVSAVKQGA-YDFLEKPFNNEHILDVVKRALD 122
Cdd:cd17569    81 YADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
8-123 2.09e-23

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: 94.71  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEG----ISAKAST--QPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVI 81
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEElgfeVVGEAENgeEALELIEEHKPD---IVITDIRMPGMDGLELIEKIRELYPDIKII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1100968853  82 LITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDK 123
Cdd:cd17536    78 ILSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
7-107 2.27e-23

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: 94.07  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFE-LEGIS--AKASTqPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILI 83
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEwEAGFEvvGEAEN-GEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIIL 79
                          90       100
                  ....*....|....*....|....
gi 1100968853  84 TGFGDIAMAVSAVKQGAYDFLEKP 107
Cdd:COG4753    80 SGYSDFEYAQEAIKLGADDYLLKP 103
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
6-125 1.31e-22

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 95.02  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITG 85
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTA 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRS 125
Cdd:COG0745    82 RDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRA 121
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
6-132 3.04e-21

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 89.26  E-value: 3.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFE-LEGIS--AKASTqPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVIL 82
Cdd:COG4565     4 IRVLIVEDDPMVAELLRRYLErLPGFEvvGVASS-GEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIV 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRK 132
Cdd:COG4565    83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQE 132
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
8-127 4.27e-21

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: 88.41  E-value: 4.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLT 127
Cdd:cd17572    81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLT 120
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
152-311 4.82e-20

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: 86.43  E-value: 4.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 152 PGIRQMRHLIHQVLDTPAD--ILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEagaftgADK 229
Cdd:cd00009     1 VGQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 230 TRIGKFEYANGGTLFLDEIESTPMALQVKLLRVLEDRRVERLGSNksialDIRVIAATKVDLkelcrQGSFREDLFYRLN 309
Cdd:cd00009    75 LLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRPL-----LGDLDRALYDRLD 144

                  ..
gi 1100968853 310 LV 311
Cdd:cd00009   145 IR 146
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
7-116 3.51e-19

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: 82.49  E-value: 3.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDV 116
Cdd:cd17563    82 ASIATAVEAIKLGADDYLAKPADADEILAA 111
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
7-109 3.53e-19

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: 82.87  E-value: 3.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFE-LEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQL--DADLPVILI 83
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRsAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIVMI 81
                          90       100
                  ....*....|....*....|....*.
gi 1100968853  84 TGFGDIAMAVSAVKQGAYDFLEKPFN 109
Cdd:cd17551    82 TADTDREVRLRALEAGATDFLTKPFD 107
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
2-138 4.51e-19

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: 84.58  E-value: 4.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   2 SEQEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVI 81
Cdd:COG4567     1 SAEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1100968853  82 LITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQELE 138
Cdd:COG4567    81 VLTGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENPMSLDRLE 137
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
6-121 1.32e-18

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: 81.17  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEG--ISAKAST--QPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVI 81
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTKAGyeVVGEAANgeEAVEKYKELKPD---LVTMDITMPEMDGIEALKEIKKIDPNAKVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  82 LITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17542    78 MCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
148-318 2.88e-18

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 80.85  E-value: 2.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 148 LGNSPGIRQMRHLIHQVLDTPADILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESelfgaeagaftga 227
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 228 dktrigkfeyANGGTLFLDEIESTPMALQVKLLrvledrrvERLGSNKSiaLDIRVIAATKVDLKELCRQGSFREDLFYR 307
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLL--------LLLAKAEG--YRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 1100968853 308 LNLVTVAIPPL 318
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
9-107 4.22e-18

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: 78.99  E-value: 4.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   9 LILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFGD 88
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                          90
                  ....*....|....*....
gi 1100968853  89 IAMAVSAVKQGAYDFLEKP 107
Cdd:cd17574    81 EEDKVLGLELGADDYITKP 99
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
171-369 9.22e-18

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: 86.31  E-value: 9.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 171 ILIEGETGTGKELVARYLHDHSPRHG-----ANFVAINCGAIPEN--IIESELFGAEAGAFTGADKTRIGKFEYANGGTL 243
Cdd:COG1221   133 TLILGPTGVGKSFFAELMYEYAIEIGvlpedAPFVVFNCADYANNpqLLMSQLFGYVKGAFTGADKDKEGLIEKADGGIL 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 244 FLDEIESTPMALQVKLLRVLeDR---RveRLG-SNKSIALDIRVIAATKVDLKelcrqgSFREDLFYRLNLVTVAIPPLR 319
Cdd:COG1221   213 FLDEVHRLPPEGQEMLFTFM-DKgiyR--RLGeTEKTRKANVRIIFATTEDPE------SSLLKTFLRRIPMVIKLPSLE 283
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1100968853 320 ER----REDiplLFLHFARIASARYHKALIAlggEQQA--RLSTHEWPGNVRELRN 369
Cdd:COG1221   284 ERsleeRLE---LIKHFFKEEAKRLNKPIKV---SKEVlkALLLYDCPGNIGQLKS 333
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
7-107 3.32e-17

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 77.24  E-value: 3.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEG---ISAKASTQPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVILI 83
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGfqvLQAADGRQGLELFRSEQPD---LVLCDLRMPEMDGLEVLKQITKESPDTPVIVV 78
                          90       100
                  ....*....|....*....|....
gi 1100968853  84 TGFGDIAMAVSAVKQGAYDFLEKP 107
Cdd:cd17555    79 SGAGVMSDAVEALRLGAWDYLTKP 102
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
7-137 7.09e-17

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: 77.02  E-value: 7.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFElEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1100968853  87 GDIAMAVSAVKQ-GAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQEL 137
Cdd:cd17596    81 TDSEDIIAGINEaGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERLSLEL 132
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
6-138 1.10e-16

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 79.09  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFE-LEGISAKASTQ-PKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILI 83
Cdd:COG3279     2 MKILIVDDEPLARERLERLLEkYPDLEVVGEASnGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFT 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1100968853  84 TGFGDiaMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLENRKLKQELE 138
Cdd:COG3279    82 TAYDE--YALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKD 134
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
8-121 4.50e-16

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: 73.82  E-value: 4.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLS--RDWMGIVITDVNMPGMDGISVMQQIKqLDADLPVILITG 85
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIR-LEMDLPVIMMSA 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17584    80 DGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQHVV 115
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
8-121 9.65e-16

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: 73.36  E-value: 9.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17553    83 ELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
7-101 9.84e-16

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: 73.02  E-value: 9.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81
                          90
                  ....*....|....*
gi 1100968853  87 GDIAMAVSAVKQGAY 101
Cdd:cd17554    82 SEYKSDFSSWAADAY 96
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
8-124 2.18e-15

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: 72.03  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVkRALDKR 124
Cdd:cd17627    81 SVSDRVAGLDAGADDYLVKPFALEELLARV-RALLRR 116
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
8-107 1.08e-14

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 69.49  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                          90       100
                  ....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKP 107
Cdd:cd19926    81 SLDTAIEALKAGAFDFLTKP 100
orf27 CHL00148
Ycf27; Reviewed
1-120 1.28e-14

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 73.21  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   1 MSEQEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPV 80
Cdd:CHL00148    2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK-ESDVPI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1100968853  81 ILITGFGDIAMAVSAVKQGAYDFLEKPFN----NEHILDVVKRA 120
Cdd:CHL00148   81 IMLTALGDVSDRITGLELGADDYVVKPFSpkelEARIRSVLRRT 124
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
8-121 1.49e-14

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: 69.85  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEG---ISAKAST--QPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVIL 82
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPdieVVGEAADgeEALALLRELRPD---VVLMDLSMPGMDGIEALRRLRRRYPDLKVIV 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17535    78 LTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
8-117 4.28e-14

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 68.26  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD---ADLPVILIT 84
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEgggRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVV 117
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
4-139 4.75e-14

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: 70.37  E-value: 4.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   4 QEYTVLILDDEPHIGTVLSQLFELEGISAKAS-TQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVIL 82
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAEaADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISE-ERPAPVIL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDK----RSLTLENRKLKQELES 139
Cdd:COG3707    81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARfrelRALRRELAKLREALEE 141
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
7-125 6.38e-14

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: 68.15  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDVVkRALDKRS 125
Cdd:cd17615    81 DSVEDRIAGLTAGGDDYVTKPFSLEEVVARL-RALLRRS 118
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
8-107 7.13e-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: 67.14  E-value: 7.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                          90       100
                  ....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKP 107
Cdd:cd19928    81 TLMTAVKAAERGAFEYLPKP 100
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
7-108 7.31e-14

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 67.52  E-value: 7.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQ--LDADLPVILIT 84
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEdpETRHIPVIMIT 80
                          90       100
                  ....*....|....*....|....
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPF 108
Cdd:cd17538    81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
7-121 1.15e-13

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: 67.33  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDA--DLPVILIT 84
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAykFTPILMLT 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17562    82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
ompR PRK09468
osmolarity response regulator; Provisional
1-142 2.84e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 69.23  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   1 MSEQEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPV 80
Cdd:PRK09468    1 MMQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  81 ILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKR--------------------SLTLENRKLKQELESQ 140
Cdd:PRK09468   81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQapelpgapsqeeeviafgkfKLNLGTRELFRGDEPM 160

                  ..
gi 1100968853 141 SL 142
Cdd:PRK09468  161 PL 162
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
8-108 3.89e-13

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: 65.22  E-value: 3.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQ--LDADLPVILITG 85
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKAdpATRHIPVIFLTA 80
                          90       100
                  ....*....|....*....|...
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPF 108
Cdd:cd19920    81 LTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
8-109 9.22e-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: 64.63  E-value: 9.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILITGFG 87
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTARG 79
                          90       100
                  ....*....|....*....|..
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFN 109
Cdd:cd17623    80 DDIDRILGLELGADDYLPKPFN 101
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
8-121 1.46e-12

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 64.27  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD--ADLPVILITG 85
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPdlKDIPVILLTT 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17598    81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
6-118 1.84e-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: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILITG 85
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE-QSEVGIILVTG 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVK 118
Cdd:cd17619    80 RDDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
8-111 2.21e-12

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: 63.69  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDW-MGIVITDVNMPGMDGISVMQQIKQLDA--DLPVILIT 84
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSrdQLAIIGIS 82
                          90       100
                  ....*....|....*....|....*..
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPFNNE 111
Cdd:cd17544    83 ASGDNALSARFIKAGANDFLTKPFLPE 109
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
7-108 2.71e-12

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: 62.90  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISA-KASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITG 85
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVtEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                          90       100
                  ....*....|....*....|...
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPF 108
Cdd:cd18160    81 GAAAAPELLSDAVGDNATLKKPF 103
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
8-123 2.82e-12

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 63.51  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPH----IGTVLSQLFELEGISAKASTQPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDA--DLPVI 81
Cdd:cd19923     3 VLVVDDFSTmrriIKNLLKELGFNNVEEAEDGVDALEKLKAGGFD---FVITDWNMPNMDGLELLKTIRADGAlsHLPVL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1100968853  82 LITGFGDIAMAVSAVKQGAYDFLEKPFNNehilDVVKRALDK 123
Cdd:cd19923    80 MVTAEAKKENVIAAAQAGVNNYIVKPFTA----ATLKEKLEK 117
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
9-108 4.12e-12

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: 62.62  E-value: 4.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   9 LILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFGD 88
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                          90       100
                  ....*....|....*....|
gi 1100968853  89 IAMAVSAVKQGAYDFLEKPF 108
Cdd:cd17625    81 VEDRVKGLDLGADDYLPKPF 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
8-125 3.13e-11

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: 60.37  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVkRALDKRS 125
Cdd:cd19934    81 SWQDKVEGLDAGADDYLTKPFHIEELLARL-RALIRRA 117
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
8-107 4.11e-11

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 59.31  E-value: 4.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD--ADLPVILITG 85
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNAdfDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKP 107
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
PRK15479 PRK15479
transcriptional regulator TctD;
52-133 4.86e-11

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 62.43  E-value: 4.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  52 IVITDVNMPGMDGISVMQQIKQLDADLPVILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHiLDVVKRALDKRS--LTLE 129
Cdd:PRK15479   47 LAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARSAVADRVKGLNVGADDYLPKPFELEE-LDARLRALLRRSagQVQE 125

                  ....
gi 1100968853 130 NRKL 133
Cdd:PRK15479  126 VQQL 129
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
7-121 6.85e-11

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: 59.34  E-value: 6.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEG--ISAKASTqPKEILRHLSR---DwmgIVITDVNMPG-MDGISVMQQIKQLdADLPV 80
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGyeVVGIADS-GEEAIELAEEnkpD---LILMDINLKGdMDGIEAAREIREK-FDIPV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1100968853  81 ILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17534    77 IFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
9-121 1.02e-10

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: 58.82  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   9 LILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD--ADLPVILITGF 86
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPktSSIPIIMLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
8-87 3.47e-10

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: 57.08  E-value: 3.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD--ADLPVILITG 85
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPwlANTPAIALTG 80

                  ..
gi 1100968853  86 FG 87
Cdd:cd17580    81 YG 82
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
8-121 4.35e-10

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 57.40  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEG---ISAKASTqPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLdADLPVILIT 84
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDPdieVVGTARD-GEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE-RPTPVVMVS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  85 GF--GDIAMAVSAVKQGAYDFLEKPFNNEHI-LDVVKRAL 121
Cdd:cd17541    81 SLteEGAEITLEALELGAVDFIAKPSGGISLdLEEIAEEL 120
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
52-119 4.76e-10

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 56.78  E-value: 4.76e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  52 IVITDVNMPGMDGISVMQQIKQLDADLPVILITgfGDI-AMAVSAVKQ-GAYDFLEKPFNNEHILDVVKR 119
Cdd:cd17593    48 VLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS--GDVqPEAKERVLElGALAFLKKPFDPEKLAQLLEE 115
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
8-125 7.25e-10

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: 56.39  E-value: 7.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEP----HIGTVLSQLFELEGI-SAKASTQPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVIL 82
Cdd:cd17532     1 ALIVDDEPlareELRYLLEEHPDIEIVgEAENGEEALEAIEELKPD---VVFLDIQMPGLDGLELAKKLSKLAKPPLIVF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1100968853  83 ITGFGDiaMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRS 125
Cdd:cd17532    78 VTAYDE--YAVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
8-107 9.17e-10

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 55.52  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                          90       100
                  ....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKP 107
Cdd:cd19935    81 SVEDRVKGLDLGADDYLVKP 100
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
7-118 1.07e-09

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: 55.92  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILITG- 85
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA-RSDVPIIIISGd 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVK 118
Cdd:cd17594    80 RRDEIDRVVGLELGADDYLAKPFGLRELLARVR 112
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
7-108 1.67e-09

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: 55.33  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIK--QLDADLPVILIT 84
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKrdEMTRDIPIIMLT 81
                          90       100
                  ....*....|....*....|....
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPF 108
Cdd:cd17618    82 ARGEEEDKVRGLEAGADDYITKPF 105
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
8-107 2.11e-09

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 54.37  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILITGFG 87
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQ-KSTLPVIFLTSKD 79
                          90       100
                  ....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKP 107
Cdd:cd19936    80 DEIDEVFGLRMGADDYITKP 99
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
8-166 2.12e-09

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 57.51  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSrDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILITGFG 87
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQ-THQTPVIMLTARG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVkRALDKRSltleNRKLKQELESQSLPGPRI--LGNSPGiRQMRHLIHQVL 165
Cdd:PRK10955   82 SELDRVLGLELGADDYLPKPFNDRELVARI-RAILRRS----HWSEQQQNNDNGSPTLEVdaLSLNPG-RQEASFDGQTL 155

                  .
gi 1100968853 166 D 166
Cdd:PRK10955  156 E 156
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
8-108 3.76e-09

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: 54.41  E-value: 3.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                          90       100
                  ....*....|....*....|.
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPF 108
Cdd:cd17624    81 GVDDRVAGLDAGADDYLVKPF 101
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
8-123 6.65e-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: 53.57  E-value: 6.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEG--ISAKAS--TQPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDAdLPVILI 83
Cdd:cd19932     3 VLIAEDEALIRMDLREMLEEAGyeVVGEASdgEEAVELAKKHKPD---LVIMDVKMPRLDGIEAAKIITSENI-APIVLL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  84 TGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDK 123
Cdd:cd19932    79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
8-122 6.70e-09

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: 53.82  E-value: 6.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEG---ISAKASTQPkEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILIT 84
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDdleVVAQASNGQ-EALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVT 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALD 122
Cdd:cd19930    80 TFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
6-108 8.00e-09

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: 53.40  E-value: 8.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFE-LEG--ISAKAST--QPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPV 80
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEqVPGftVIGTAGTgeEALKLLKERQPD---LILLDIYLPDGNGLDLLRELRAAGHDVDV 77
                          90       100
                  ....*....|....*....|....*...
gi 1100968853  81 ILITGFGDIAMAVSAVKQGAYDFLEKPF 108
Cdd:cd19925    78 IVVTAANDVETVREALRLGVVDYLIKPF 105
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
8-109 8.71e-09

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 53.24  E-value: 8.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKqLDADLPVILITGFG 87
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR-AESGVPIVMLTAKS 81
                          90       100
                  ....*....|....*....|..
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFN 109
Cdd:cd17626    82 DTVDVVLGLESGADDYVAKPFK 103
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
8-107 9.48e-09

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: 52.59  E-value: 9.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILITGFG 87
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA-RSNVPVIMVTAKD 79
                          90       100
                  ....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKP 107
Cdd:cd17621    80 SEIDKVVGLELGADDYVTKP 99
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
7-119 1.27e-08

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: 52.93  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDA--DLPVILIT 84
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPAtrDIPVIALT 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1100968853  85 GFgdiAM---AVSAVKQGAYDFLEKPFNNEHILDVVKR 119
Cdd:cd17548    81 AY---AMkgdREKILEAGCDGYISKPIDTREFLETVAK 115
PRK10766 PRK10766
two-component system response regulator TorR;
6-140 1.57e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 55.04  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   6 YTVLILDDEPHIGTVLSQLFELEG---ISAKASTQPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQlDADLPVIL 82
Cdd:PRK10766    3 YHILVVEDEPVTRARLQGYFEQEGytvSEAASGAGMREIMQNQHVD---LILLDINLPGEDGLMLTRELRS-RSTVGIIL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTlenRKLKQELESQ 140
Cdd:PRK10766   79 VTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLLWRISLA---RQAQPHAQEE 133
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
8-114 1.73e-08

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: 52.41  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                          90       100
                  ....*....|....*....|....*..
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHIL 114
Cdd:cd17616    81 DIEDKVKGLGFGADDYMTKPFHKDELV 107
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
7-121 1.88e-08

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 56.91  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLS-QLFELeGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITg 85
Cdd:PRK10841  803 MILVVDDHPINRRLLAdQLGSL-GYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVT- 880
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1100968853  86 fgdiAMAVSAVKQ-----GAYDFLEKPFNnehiLDVVKRAL 121
Cdd:PRK10841  881 ----ANALAEEKQrcleaGMDSCLSKPVT----LDVLKQTL 913
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
171-287 4.54e-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: 51.99  E-value: 4.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  171 ILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIES---ELFGAEAGAFTGADKTRIG--KFEYANGGTLFL 245
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLIL 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1100968853  246 DEIESTPMALQVKLLRVLEDrrvERLGSNKSIALDIRVIAAT 287
Cdd:smart00382  85 DEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTT 123
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
8-121 6.03e-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: 50.83  E-value: 6.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILITGFG 87
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE-HSHVPILMLTART 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd19939    81 EEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
7-121 6.39e-08

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 50.84  E-value: 6.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLdADLPVILITGF 86
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRF-SDVPIIMVTAR 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd19938    80 VEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
8-107 1.15e-07

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: 49.47  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDaDLPVILITGFG 87
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSARD 79
                          90       100
                  ....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKP 107
Cdd:cd17620    80 EESDKIAALDAGADDYLTKP 99
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
10-107 1.19e-07

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: 49.58  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  10 ILDDEPHIGTVLSQLFELE------GISAKASTQPKEILRhLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVILI 83
Cdd:cd17565     3 IVDDDKNIIKILSDIIEDDdlgevvGEADNGAQAYDEILF-LQPD---IVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMI 78
                          90       100
                  ....*....|....*....|....
gi 1100968853  84 TGFGDIAMAVSAVKQGAYDFLEKP 107
Cdd:cd17565    79 SQVSDKEMIGKAYQAGIEFFINKP 102
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1-120 1.22e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 52.34  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   1 MSEQEYTVLILDDEPHIGTVLSQLFELEG---ISAKAS--TQPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLD 75
Cdd:PRK10651    2 SNQEPATILLIDDHPMLRTGVKQLISMAPditVVGEASngEQGIELAESLDPD---LILLDLNMPGMNGLETLDKLREKS 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1100968853  76 ADLPVILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRA 120
Cdd:PRK10651   79 LSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQA 123
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
7-108 1.26e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 52.27  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:PRK11083    5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTAR 84
                          90       100
                  ....*....|....*....|..
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPF 108
Cdd:PRK11083   85 SDEVDRLVGLEIGADDYVAKPF 106
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
8-125 1.53e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 52.03  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQ--LDADLPVILITG 85
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKResMTRDIPVVMLTA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRS 125
Cdd:PRK10161   85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRIS 124
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
7-120 2.08e-07

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 49.36  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFE-LEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITG 85
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEdLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSG 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  86 FGDIAMAVSAVKQGAYDF-----LEKPFNNEHILDVVKRA 120
Cdd:cd17530    82 LDGGILESAETLAGANGLnllgtLSKPFSPEELTELLTKY 121
pleD PRK09581
response regulator PleD; Reviewed
52-109 2.15e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 52.98  E-value: 2.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  52 IVITDVNMPGMDGISVMQQIK--QLDADLPVILITGFGDIAMAVSAVKQGAYDFLEKPFN 109
Cdd:PRK09581   49 IILLDVMMPGMDGFEVCRRLKsdPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPIN 108
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
8-121 2.31e-07

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


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 49.00  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGIS--AKASTQpKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQldADLPVILITG 85
Cdd:cd17586     1 VLVLEDEPLIAMNLEDALEDLGGKevVTAATC-AEALRSLADGPIDIAILDVNLGGETSIPVADALKR--RAIPFIFATG 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1100968853  86 FGDIAMaVSAVKQGAyDFLEKPFNNEHILDVVKRAL 121
Cdd:cd17586    78 YGDSHG-IDSRLIDV-PVLRKPFDADSALAALAMLL 111
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
8-122 2.49e-07

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: 49.09  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFEL-------------EGISAKASTQPKEILrhlsrdwmgiviTDVNMPGMDGISVMQQIKQL 74
Cdd:cd17552     4 ILVIDDEEDIREVVQACLEKlagwevltassgqEGLEKAATEQPDAIL------------LDVMMPDMDGLATLKKLQAN 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1100968853  75 DA--DLPVILITGFGDIA-------MAVSAVkqgaydfLEKPFNNEHILDVVKRALD 122
Cdd:cd17552    72 PEtqSIPVILLTAKAQPSdrqrfasLGVAGV-------IAKPFDPLTLAEQIAKLLG 121
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
7-127 2.94e-07

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 51.34  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISA-KASTQPKEILRHLSRDwMGIVITDVNMPGMDGISVMQQIKQLDAdLPVILITG 85
Cdd:PRK10529    3 NVLIVEDEQAIRRFLRTALEGDGMRVfEAETLQRGLLEAATRK-PDLIILDLGLPDGDGIEFIRDLRQWSA-IPVIVLSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLT 127
Cdd:PRK10529   81 RSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSAT 122
PRK10610 PRK10610
chemotaxis protein CheY;
1-108 5.97e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 48.43  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   1 MSEQEYTVLILDDEPHIGTVLSQLF-ELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLD--AD 77
Cdd:PRK10610    1 MADKELKFLVVDDFSTMRRIVRNLLkELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1100968853  78 LPVILITGFGDIAMAVSAVKQGAYDFLEKPF 108
Cdd:PRK10610   81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPF 111
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
2-121 7.06e-07

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 50.07  E-value: 7.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   2 SEQEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLdADLPVI 81
Cdd:PRK10710    7 DENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRF-SDIPIV 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  82 LITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:PRK10710   86 MVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTIL 125
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
8-121 7.41e-07

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: 47.66  E-value: 7.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLdADLPVILITGFG 87
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI-SNVPIIFISSRD 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd18159    80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
7-122 9.21e-07

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: 47.63  E-value: 9.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEG--ISAKASTQpKEILRHLSRDWMGIVITDVNMP-GMDGISVMQQIkQLDADLPVILI 83
Cdd:cd17540     2 RVLIIEDEPLIAMDLEQIVEDLGhqVVGIARTR-DEAVALARRERPDLILADIQLAdGSSGIDAVNEI-LTTHDVPVIFV 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1100968853  84 TGFGDiaMAVSAVKQGAYDFLEKPFNNEHILDVVKRALD 122
Cdd:cd17540    80 TAYPE--RLLTGERPEPTFLITKPFDPEMVKAAISQALF 116
PRK10643 PRK10643
two-component system response regulator PmrA;
8-124 1.11e-06

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 49.26  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVkRALDKR 124
Cdd:PRK10643   83 TLEDRVAGLDVGADDYLVKPFALEELHARI-RALIRR 118
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
8-108 1.15e-06

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: 46.96  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHI-GTVLSQLFELEGISAKASTQPkEILRHLSRDW-MGIVITDVNMPG-MDGISVMQQIKQLDADLPVILIT 84
Cdd:cd18161     1 VLVVEDDPDVrRLTAEVLEDLGYTVLEAASGD-EALDLLESGPdIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTS 79
                          90       100
                  ....*....|....*....|....
gi 1100968853  85 GFGDIAMAVSAVKQGaYDFLEKPF 108
Cdd:cd18161    80 GYAENAIEGGDLAPG-VDVLSKPF 102
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
170-287 1.33e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 47.67  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853 170 DILIEGETGTGKELVARYLHDHSPRHGANFVAINCGAIPENIIESELFGAEAGAFTGADKTRIGKfeyaNGGTLFLDEIE 249
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAR----EGEIAVLDEIN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1100968853 250 STPMALQVKLLRVLEDRR--VERLGSNKSIALD-IRVIAAT 287
Cdd:pfam07728  77 RANPDVLNSLLSLLDERRllLPDGGELVKAAPDgFRLIATM 117
PRK11173 PRK11173
two-component response regulator; Provisional
4-109 2.47e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 48.47  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   4 QEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILI 83
Cdd:PRK11173    2 QTPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELRE-QANVALMFL 80
                          90       100
                  ....*....|....*....|....*.
gi 1100968853  84 TGFGDIAMAVSAVKQGAYDFLEKPFN 109
Cdd:PRK11173   81 TGRDNEVDKILGLEIGADDYITKPFN 106
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
8-107 3.39e-06

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 45.83  E-value: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLS---------RDWMGIVITDVNMPGMDGISVMQQIKQ--LDA 76
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1100968853  77 DLPVILITGFGDIAMAVSAVKQGAYDFLEKP 107
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
8-109 3.57e-06

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 45.72  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGIS-AKASTQPKEILRHLSRDWMGIVITDVNM-PGMDGISVMQQI---KQLDADLPVIL 82
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVTrIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELrhkKLISPSTVFIM 80
                          90       100
                  ....*....|....*....|....*..
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFN 109
Cdd:cd17589    81 VTGESSRAMVLSALELEPDDYLLKPFT 107
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
6-60 5.95e-06

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: 43.33  E-value: 5.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1100968853    6 YTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMP 60
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
4-123 6.68e-06

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 48.58  E-value: 6.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853    4 QEYTVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILI 83
Cdd:PRK09959   957 EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGL 1036
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1100968853   84 TGFGDIAMAVSAVKQGAYDFLEKPFNnehiLDVVKRALDK 123
Cdd:PRK09959  1037 TANAQANEREKGLSCGMNLCLFKPLT----LDVLKTHLSQ 1072
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
8-107 7.20e-06

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: 44.70  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEP---HIGTVLSQLFELEGISAKASTQPKEILRHLSRDwMGIVITDVNMPGMDGISVMQQIKQLDA--DLPVIL 82
Cdd:cd17582     1 VLLVENDDstrQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNE-IDLILTEVDLPVSSGFKLLSYIMRHKIckNIPVIM 79
                          90       100
                  ....*....|....*....|....*
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKP 107
Cdd:cd17582    80 MSSQDSVGVVFKCLSKGAADYLVKP 104
PRK13856 PRK13856
two-component response regulator VirG; Provisional
8-125 7.28e-06

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 47.12  E-value: 7.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQlDADLPVILITGFG 87
Cdd:PRK13856    4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLAT-KSDVPIIIISGDR 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1100968853  88 -DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRS 125
Cdd:PRK13856   83 lEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRP 121
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
52-108 7.61e-06

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: 44.52  E-value: 7.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1100968853  52 IVITDVNMPGMDGISVMQQIKQ--LDADLPVILITGFGDIAMAVSAVKQGAYDFLEKPF 108
Cdd:cd17561    50 VLLLDIIMPHLDGIGVLEKLRRmrLEKRPKIIMLTAFGQEDITQRAVELGASYYILKPF 108
PRK13557 PRK13557
histidine kinase; Provisional
7-122 1.07e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 47.74  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHL-SRDWMGIVITDVNMPG-MDGISVMQQIKQLDADLPVILIT 84
Cdd:PRK13557  417 TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPGgMNGVMLAREARRRQPKIKVLLTT 496
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALD 122
Cdd:PRK13557  497 GYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLD 534
PRK11517 PRK11517
DNA-binding response regulator HprR;
8-142 1.76e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 45.66  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADlPVILITGFG 87
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT-PVICLTARD 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRS---LTLENRKLKQELESQSL 142
Cdd:PRK11517   82 SVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHHalnSTLEISGLRMDSVSQSV 139
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
403-442 2.20e-05

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 41.22  E-value: 2.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1100968853 403 VEFFERLLIEEALAHNKGSIKLTMEQLELPRKTLYDKMRK 442
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
PRK10336 PRK10336
two-component system response regulator QseB;
8-143 2.40e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 45.27  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:PRK10336    3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFNnehILDVVKR--ALDKRS------------LTLENRKLKQELESQSLP 143
Cdd:PRK10336   83 ALAERVEGLRLGADDYLCKPFA---LIEVAARleALMRRTngqasnelrhgnVMLDPGKRIATLAGEPLT 149
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
8-121 3.32e-05

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: 43.11  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELE---GISAKAST--QPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVIL 82
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDpdfTVVGEASSgeEGIELAERLDPD---LILLDLNMKGMSGLDTLKALREEGVSARIVI 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:cd19931    78 LTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAA 116
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
7-148 3.43e-05

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 46.38  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPH----IGTVLSQLFElEGISAKASTQPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQ--LDADLPV 80
Cdd:PRK11107  669 TVMAVDDNPAnlklIGALLEEQVE-HVVLCDSGHQAVEQAKQRPFD---LILMDIQMPGMDGIRACELIRQlpHNQNTPI 744
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1100968853  81 ILITgfgdiAMAVSA-----VKQGAYDFLEKPFnNEHIL-DVVKRALDKRSLTleNRKLKQELESQSLPGPRIL 148
Cdd:PRK11107  745 IAVT-----AHAMAGererlLSAGMDDYLAKPI-DEAMLkQVLLRYKPGPKFT--SRVVAPEPPEPVHFPNATL 810
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
52-84 4.10e-05

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: 43.17  E-value: 4.10e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1100968853  52 IVITDVNMPGMDGISVMQQIKQlDADL---PVILIT 84
Cdd:cd17557    55 LILLDLNMPRMDGFEVLREIKA-DPDLrriPVVVLT 89
PRK10816 PRK10816
two-component system response regulator PhoP;
8-124 8.41e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 43.57  E-value: 8.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLS-QLFELeGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGF 86
Cdd:PRK10816    3 VLVVEDNALLRHHLKvQLQDA-GHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1100968853  87 GDIAMAVSAVKQGAYDFLEKPFnneHILDVVKR--ALDKR 124
Cdd:PRK10816   82 ESWQDKVEVLSAGADDYVTKPF---HIEEVMARmqALMRR 118
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
8-107 8.59e-05

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: 41.59  E-value: 8.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDA--DLPVILITG 85
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSAlkDTPIIMLTG 80
                          90       100
                  ....*....|....*....|..
gi 1100968853  86 FGDIAMAVSAVKQGAYDFLEKP 107
Cdd:cd17602    81 KDGLVDRIRAKMAGASGYLTKP 102
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
52-123 8.76e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 43.76  E-value: 8.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100968853  52 IVITDVNMPGMDGISVMQQIKQLDADLPVILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDK 123
Cdd:PRK09836   47 LIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRR 118
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
7-121 1.47e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 42.94  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFEL-EGISAKAST-QPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILIT 84
Cdd:PRK09935    5 SVIIMDTHPIIRMSIEVLLQKnSELQIVLKTdDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLS 84
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100968853  85 GFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRAL 121
Cdd:PRK09935   85 SKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMIL 121
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
7-71 1.49e-04

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: 41.42  E-value: 1.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEG---ISAKASTqPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQI 71
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEPdieVVGEAAD-GEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
8-143 2.13e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 43.21  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLF----ELEGIsAKASTqPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDaDLPVILI 83
Cdd:PRK00742    6 VLVVDDSAFMRRLISEILnsdpDIEVV-GTAPD-GLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLR-PTPVVMV 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100968853  84 ---TGFG-DIAMAvsAVKQGAYDFLEKPFNNEHI-LDVVKRALDKRSLTLENRKLKQELESQSLP 143
Cdd:PRK00742   83 sslTERGaEITLR--ALELGAVDFVTKPFLGISLgMDEYKEELAEKVRAAARARVRALPPRAAAA 145
PRK10693 PRK10693
two-component system response regulator RssB;
39-110 6.54e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 41.51  E-value: 6.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100968853  39 KEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFGDIAMAVSAVKQGAYDFLEKPFNN 110
Cdd:PRK10693    7 VDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKD 78
dpiA PRK10046
two-component response regulator DpiA; Provisional
51-136 6.80e-04

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 41.16  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853  51 GIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALDKRSLTLEN 130
Cdd:PRK10046   52 GLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLESI 131

                  ....*.
gi 1100968853 131 RKLKQE 136
Cdd:PRK10046  132 DSASQK 137
PRK15369 PRK15369
two component system response regulator;
52-100 9.57e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 40.45  E-value: 9.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1100968853  52 IVITDVNMPGMDGISVMQQIKQLDADLPVILITGFGDIAMAVSAVKQGA 100
Cdd:PRK15369   52 IVILDLGLPGMNGLDVIPQLHQRWPAMNILVLTARQEEHMASRTLAAGA 100
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
154-204 1.09e-03

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 40.99  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1100968853 154 IRQMRHLIHQVLD--TPADILIEGETGTGKELVARY----LHDHSPRHGAN--FVAINC 204
Cdd:COG1474    35 IEELASALRPALRgeRPSNVLIYGPTGTGKTAVAKYvleeLEEEAEERGVDvrVVYVNC 93
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
7-120 1.57e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 39.88  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   7 TVLILDDEPHIGTVLSQLFELEGISAKAS----TQPKEILRHLSRDwmgIVITDVNMPGMDGISVMQQIKQLDADLPVIL 82
Cdd:PRK09958    2 NAIIIDDHPLAIAAIRNLLIKNDIEILAEltegGSAVQRVETLKPD---IVIIDVDIPGVNGIQVLETLRKRQYSGIIII 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1100968853  83 ITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRA 120
Cdd:PRK09958   79 VSAKNDHFYGKHCADAGANGFVSKKEGMNNIIAAIEAA 116
PRK13558 PRK13558
bacterio-opsin activator; Provisional
8-103 2.01e-03

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 40.59  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:PRK13558   10 VLFVGDDPEAGPVDCDLDEDGRLDVTQIRDFVAARDRVEAGEIDCVVADHEPDGFDGLALLEAVRQTTAVPPVVVVPTAG 89
                          90
                  ....*....|....*.
gi 1100968853  88 DIAMAVSAVKQGAYDF 103
Cdd:PRK13558   90 DEAVARRAVDADAAAY 105
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
56-122 2.17e-03

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; 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 AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 37.99  E-value: 2.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100968853  56 DVNMPGMDGISVMQQIKQLDADLPVILITGFGDIAMAVSAVKQGAYDFLEKPFNNEHILDVVKRALD 122
Cdd:cd17533    60 DIKMEEKNGLEVAQKIRKYDPYAIIIFVTTHSEFAPLTFEYKVAALDFILKPLKLEEFKKRIEECIK 126
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
8-107 2.70e-03

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: 37.74  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLdADLPVILITGFG 87
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLLTALD 81
                          90       100
                  ....*....|....*....|
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKP 107
Cdd:cd17622    82 SDIDHILGLELGADDYVVKP 101
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
52-107 4.46e-03

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 36.96  E-value: 4.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1100968853  52 IVITDVNMPGMDGISVMQQIKQLDA--DLPVILITGFGDIAMAVSAVKQGAYDFLEKP 107
Cdd:cd17581    56 MIITDYCMPGMTGYDLLKKVKESSAlkEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1-118 4.46e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 38.29  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   1 MSEQ-EYTVLILDDEPHIGTVLSQLFELEG---ISAKASTQpKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDA 76
Cdd:PRK10403    1 MPEAtPFQVLIVDDHPLMRRGVRQLLELDPgfeVVAEAGDG-ASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGV 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1100968853  77 DLPVILITgFGDIAMAVSA-VKQGAYDFLEKPFNNEHILDVVK 118
Cdd:PRK10403   80 TAQIIILT-VSDASSDVFAlIDAGADGYLLKDSDPEVLLEAIR 121
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
8-109 6.07e-03

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: 36.25  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968853   8 VLILDDEPHIGTVLSQLFELEGISAKASTQPKEILRHLSRDWMGIVITDVNMPGMDGISVMQQIKQLDADLPVILITGFG 87
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                          90       100
                  ....*....|....*....|..
gi 1100968853  88 DIAMAVSAVKQGAYDFLEKPFN 109
Cdd:cd17573    81 KTEQEIEAFKEGADDYIAKPFD 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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