NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1490467431|gb|RLA99011|]
View 

sigma-54-dependent Fis family transcriptional regulator [Deltaproteobacteria bacterium]

Protein Classification

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

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

CATH:  3.40.50.2300
Gene Ontology:  GO:0006355|GO:0005524|GO:0000160|GO:0000156|GO:0003677
PubMed:  8830233|20226724|12618438|10966457
SCOP:  4003632

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 1-455 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: 596.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMI 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQlveqryqfwnIVGKSPRMLKVFDLIEKV 160
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----------LIGRSPAMQEVRRLIEKV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 161 SQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLF 240
Cdd:COG2204   151 APSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 241 LDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERRED 320
Cdd:COG2204   231 LDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRED 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 321 IPLLVQHFVDKYSREMEKEIKgVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITdkhirsymserllARDLPik 400
Cdd:COG2204   311 IPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVIT-------------AEDLP-- 374

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431 401 veipeegidlnRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYG 455
Cdd:COG2204   375 -----------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 1-455 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: 596.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMI 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQlveqryqfwnIVGKSPRMLKVFDLIEKV 160
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----------LIGRSPAMQEVRRLIEKV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 161 SQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLF 240
Cdd:COG2204   151 APSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 241 LDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERRED 320
Cdd:COG2204   231 LDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRED 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 321 IPLLVQHFVDKYSREMEKEIKgVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITdkhirsymserllARDLPik 400
Cdd:COG2204   311 IPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVIT-------------AEDLP-- 374

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431 401 veipeegidlnRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYG 455
Cdd:COG2204   375 -----------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-456 2.81e-169

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 483.58  E-value: 2.81e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQLVEQRYQFWNIVGKSPRMLKVFDLIEKVSQA 163
Cdd:PRK11361   86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 164 KVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLFLDE 243
Cdd:PRK11361  166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 244 IGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPL 323
Cdd:PRK11361  246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 324 LVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYItdkhirsymserlLARDLPIKVEI 403
Cdd:PRK11361  326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPII-------------FSEDLPPQIRQ 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490467431 404 PEEGI-----------DLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:PRK11361  393 PVCNAgevktapvgerNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 5-456 2.33e-137

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: 401.82  E-value: 2.33e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKkeGYKVTATTDPKEALTALEKDFFHMVLTDIRMP-----EVDGFEILRRAKELNPDTLVIM 79
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQLVEQRyQFWNIVGKSPRMLKVFDLIEK 159
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGT-ALRGLITSSPGMQKICRTIEK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 160 VSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTL 239
Cdd:TIGR02915 158 IAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 240 FLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERRE 319
Cdd:TIGR02915 238 FLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 320 DIPLLVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITdkhirsymserllARDL-- 397
Cdd:TIGR02915 318 DAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQIT-------------AEDLgl 384

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 398 -PIKVEIPEEGIDLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:TIGR02915 385 dARERAETPLEVNLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
139-455 1.19e-125

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 376.54  E-value: 1.19e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 139 QFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKnGPFVPINCGAIPETLLESELFGYVRG 218
Cdd:NF041552  265 SFGKIIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRK-GPFVPVNCSAIPEELFESEFFGYEEG 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 219 AFTGAVTS-KRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFR 297
Cdd:NF041552  344 AFTGALKKgKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFR 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 298 EDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETES 377
Cdd:NF041552  424 EDLYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNG 503

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467431 378 YITDKHIRSYMserlLARDLPIKVEIPEEGIDLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYG 455
Cdd:NF041552  504 TITKDSIPEYI----LESVKKKEDEEGDYPLDLNKAVEKLEIDTIKKALEMSNGNKAKAAKLLNIPRSTLYYKLKQYG 577
Sigma54_activat pfam00158
Sigma-54 interaction domain;
143-309 1.45e-110

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 323.20  E-value: 1.45e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 143 IVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTG 222
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 223 AVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYY 302
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160


                  ....*..
gi 1490467431 303 RLNVVQI 309
Cdd:pfam00158 161 RLNVIPI 167
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 5-132 4.33e-40

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: 140.32  E-value: 4.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQ 132
Cdd:cd17549    81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQ 128
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 4-57 1.44e-12

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: 62.20  E-value: 1.44e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1490467431    4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMP 57
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 1-455 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: 596.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMI 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQlveqryqfwnIVGKSPRMLKVFDLIEKV 160
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----------LIGRSPAMQEVRRLIEKV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 161 SQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLF 240
Cdd:COG2204   151 APSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 241 LDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERRED 320
Cdd:COG2204   231 LDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRED 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 321 IPLLVQHFVDKYSREMEKEIKgVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITdkhirsymserllARDLPik 400
Cdd:COG2204   311 IPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVIT-------------AEDLP-- 374

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431 401 veipeegidlnRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYG 455
Cdd:COG2204   375 -----------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 50-456 0e+00

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: 516.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  50 VLTDIRMPEV--DGFEILRRAKELNPDTLVIMITAY-----GSPEGAVEAMKEgaydyitkpfqVDEVKLTIRKAleryl 122
Cdd:COG3829    59 LIPNSPLLEVlkTGKPVTGVIQKTGGKGKTVIVTAIpifedGEVIGAVETFRD-----------ITELKRLERKL----- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 123 lweENLRLRQLVEQRYQFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGA 202
Cdd:COG3829   123 ---REEELERGLSAKYTFDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAA 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 203 IPETLLESELFGYVRGAFTGAVTS-KRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIA 281
Cdd:COG3829   200 IPENLLESELFGYEKGAFTGAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIA 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 282 ASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVR 361
Cdd:COG3829   280 ATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVR 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 362 ELENIIERSVTLETESYITDKHIRSYMSERLLARDlpikveiPEEGIDLNRVIEEIEKAFLLKALERTGGMKKKAAELLG 441
Cdd:COG3829   360 ELENVIERAVVLSEGDVITPEHLPEYLLEEAEAAS-------AAEEGSLKEALEEVEKELIEEALEKTGGNKSKAAKALG 432

                         410
                  ....*....|....*
gi 1490467431 442 MNFRAIRYKLAKYGL 456
Cdd:COG3829   433 ISRSTLYRKLKKYGI 447
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-456 2.81e-169

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 483.58  E-value: 2.81e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQLVEQRYQFWNIVGKSPRMLKVFDLIEKVSQA 163
Cdd:PRK11361   86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 164 KVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLFLDE 243
Cdd:PRK11361  166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 244 IGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPL 323
Cdd:PRK11361  246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 324 LVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYItdkhirsymserlLARDLPIKVEI 403
Cdd:PRK11361  326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPII-------------FSEDLPPQIRQ 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490467431 404 PEEGI-----------DLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:PRK11361  393 PVCNAgevktapvgerNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
5-453 1.74e-147

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 427.52  E-value: 1.74e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERylLWEENLRLRQLVEQRyqfWNIVGKSPRMLKVFDLIEKVSQAK 164
Cdd:PRK10365   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAH--THSIDAETPAVTASQ---FGMVGKSPAMQHLLSEIALVAPSE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 165 VNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLFLDEI 244
Cdd:PRK10365  163 ATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 245 GDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLL 324
Cdd:PRK10365  243 GDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 325 VQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITDkhirsymserllaRDLPIKVE-- 402
Cdd:PRK10365  323 AGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISE-------------RELPLAIAst 389

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1490467431 403 -IPEEGIDLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAK 453
Cdd:PRK10365  390 pIPLGQSQDIQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 5-456 2.33e-137

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: 401.82  E-value: 2.33e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKkeGYKVTATTDPKEALTALEKDFFHMVLTDIRMP-----EVDGFEILRRAKELNPDTLVIM 79
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQLVEQRyQFWNIVGKSPRMLKVFDLIEK 159
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGT-ALRGLITSSPGMQKICRTIEK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 160 VSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTL 239
Cdd:TIGR02915 158 IAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 240 FLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERRE 319
Cdd:TIGR02915 238 FLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 320 DIPLLVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITdkhirsymserllARDL-- 397
Cdd:TIGR02915 318 DAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQIT-------------AEDLgl 384

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 398 -PIKVEIPEEGIDLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:TIGR02915 385 dARERAETPLEVNLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
 110-456 2.59e-127

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: 379.44  E-value: 2.59e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 110 VKLTIRKALERYLLWEENLRLRQ--------LVEQRYQFWN-IVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELV 180
Cdd:TIGR01817 156 VRLHRLVAQRRERLIAEAVQLSKqlrdkapeIARRRSGKEDgIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELI 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 181 AKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQ 260
Cdd:TIGR01817 236 AKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQ 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 261 EREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEI 340
Cdd:TIGR01817 316 EGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPL 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 341 KgVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITDKHI-------RSYM--------------SERLLARDLPI 399
Cdd:TIGR01817 396 T-ITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITRSDFscqsgqcLSPMlaktcphghisidpLAGTTPPHSPA 474

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467431 400 KVEIPEEGIDLNRVIEEIEKafLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:TIGR01817 475 SAALPGEPGLSGPTLSERER--LIAALEQAGWVQAKAARLLGMTPRQVGYALRKLNI 529
PRK15115 PRK15115
response regulator GlrR; Provisional
 3-451 3.19e-127

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 376.10  E-value: 3.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:PRK15115    6 AHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYL-----LWEENlrlrqlveqryqfwnIVGKSPRMLKVFDLI 157
Cdd:PRK15115   86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSApatdeRWREA---------------IVTRSPLMLRLLEQA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 158 EKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGG 237
Cdd:PRK15115  151 RMVAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 238 TLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRER 317
Cdd:PRK15115  231 TLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAER 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 318 REDIPLLVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITDKHIRSYMSERLLArdL 397
Cdd:PRK15115  311 TEDIPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTA--L 388

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490467431 398 PIKVEiPEEGIDLNrvieeiekaFLLKALERTGGMKKKAAELLGMNfRAIRYKL 451
Cdd:PRK15115  389 PTFVE-ARNQFELN---------YLRKLLQITKGNVTHAARMAGRN-RTEFYKL 431
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 5-456 1.07e-125

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 373.05  E-value: 1.07e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLlwEENLRLRQLVEQRYQfwNIVGKSPRMLKVFDLIEKVSQAK 164
Cdd:PRK10923   86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQ--EQQQPRNIQVNGPTT--DIIGEAPAMQDVFRIIGRLSRSS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 165 VNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLFLDEI 244
Cdd:PRK10923  162 ISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEI 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 245 GDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLL 324
Cdd:PRK10923  242 GDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 325 VQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIeRSVTLETEsyitdkhirsymSERLLARDLP---IKV 401
Cdd:PRK10923  322 ARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTC-RWLTVMAA------------GQEVLIQDLPgelFES 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 402 EIPEEGID-------------------------LNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:PRK10923  389 TVPESTSQmqpdswatllaqwadralrsghqnlLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGM 468
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
139-455 1.19e-125

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 376.54  E-value: 1.19e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 139 QFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKnGPFVPINCGAIPETLLESELFGYVRG 218
Cdd:NF041552  265 SFGKIIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRK-GPFVPVNCSAIPEELFESEFFGYEEG 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 219 AFTGAVTS-KRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFR 297
Cdd:NF041552  344 AFTGALKKgKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFR 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 298 EDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETES 377
Cdd:NF041552  424 EDLYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNG 503

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467431 378 YITDKHIRSYMserlLARDLPIKVEIPEEGIDLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYG 455
Cdd:NF041552  504 TITKDSIPEYI----LESVKKKEDEEGDYPLDLNKAVEKLEIDTIKKALEMSNGNKAKAAKLLNIPRSTLYYKLKQYG 577
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
135-455 2.15e-125

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 377.70  E-value: 2.15e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 135 EQRYQFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFG 214
Cdd:COG3284   315 PAPAALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFG 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 215 YVRGAFTGAVTS-KRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRK 293
Cdd:COG3284   395 YEPGAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAA 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 294 KEFREDLYYRLNVVQINLPPLRErREDIPLLVQHFVDKYSREMekEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTL 373
Cdd:COG3284   475 GRFREDLYYRLNGLTLTLPPLRE-REDLPALIEHLLRELAAGR--GPLRLSPEALALLAAYPWPGNVRELRNVLRTALAL 551

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 374 ETESYITDKHIRSYMSERLLARDlpikveiPEEGIDLNRvIEEIEKAFLLKALERTGGMKKKAAELLGMNfRAIRY-KLA 452
Cdd:COG3284   552 ADGGVITVEDLPDELRAELAAAA-------PAAAAPLTS-LEEAERDAILRALRACGGNVSAAARALGIS-RSTLYrKLK 622


                  ...
gi 1490467431 453 KYG 455
Cdd:COG3284   623 RYG 625
Sigma54_activat pfam00158
Sigma-54 interaction domain;
143-309 1.45e-110

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 323.20  E-value: 1.45e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 143 IVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTG 222
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 223 AVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYY 302
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160


                  ....*..
gi 1490467431 303 RLNVVQI 309
Cdd:pfam00158 161 RLNVIPI 167
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
143-453 1.19e-107

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 328.28  E-value: 1.19e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 143 IVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRGAFTG 222
Cdd:PRK05022  189 MIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTG 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 223 AVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYY 302
Cdd:PRK05022  269 AISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYH 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 303 RLNVVQINLPPLRERREDIPLLVQHFVDKYSREMekeikGV-----TPEAMELLVNYDYPGNVRELENIIERS------- 370
Cdd:PRK05022  349 RLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARL-----GLrslrlSPAAQAALLAYDWPGNVRELEHVISRAallarar 423

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 371 -----VTLETEsyitdkHIRSYMSERLLARDLPIkVEIPEEGIDLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNfR 445
Cdd:PRK05022  424 gagriVTLEAQ------HLDLPAEVALPPPEAAA-APAAVVSQNLREATEAFQRQLIRQALAQHQGNWAAAARALELD-R 495


                  ....*...
gi 1490467431 446 AIRYKLAK 453
Cdd:PRK05022  496 ANLHRLAK 503
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
 140-456 4.88e-104

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 319.06  E-value: 4.88e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 140 FWNIVGKSPRMLKVfdliekVSQAK------VNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELF 213
Cdd:COG3283   203 FDHIVASSPKMRQV------IRQAKkmamldAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELF 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 214 GYVRGAFTGAVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRK 293
Cdd:COG3283   277 GYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQE 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 294 KEFREDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTL 373
Cdd:COG3283   357 GEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSL 436

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 374 ETESYITDKHIRsymserllardLP-IKVEIPEEGIDLNRVIEEIEKAF---LLKALERTGGMKKKAAELLGMNFRAIRY 449
Cdd:COG3283   437 LEGDELTPEDLQ-----------LPeYAASAGLLDDLLEGSLDEIVKRFersLLRRLYPSYPSTRKLAKRLGVSHTAIAN 505


                  ....*..
gi 1490467431 450 KLAKYGL 456
Cdd:COG3283   506 KLREYGI 512
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
 169-456 1.31e-95

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: 291.37  E-value: 1.31e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 169 ILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESelfgyvrgaftgavtskrglleiasggtlfldeigdlp 248
Cdd:COG3604   120 ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------------- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 249 lslqvkllrvIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLLVQHF 328
Cdd:COG3604   162 ----------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHF 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 329 VDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENIIERSVTLETESYITDKHIRSYMSERLlardlpikveipeegi 408
Cdd:COG3604   232 LEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGSREAL---------------- 295

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1490467431 409 dlnrviEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:COG3604   296 ------EEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGI 337
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
 113-442 6.48e-94

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 293.55  E-value: 6.48e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 113 TIRKALERYLlweENLRLRQL----------VEQRYQFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAK 182
Cdd:PRK15424  184 TVRQAFEDAL---DMTRMTLRhnthyatrnaLRTRYVLGDLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQ 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 183 AIHYNSP--------RKNGPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKR-GLLEIASGGTLFLDEIGDLPLSLQV 253
Cdd:PRK15424  261 AIHREYFarhdarqgKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGGRaGLFEIAHGGTLFLDEIGEMPLPLQT 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 254 KLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYS 333
Cdd:PRK15424  341 RLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSL 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 334 REME----KEIKGVTPEAMELLVNYDYPGNVRELENIIER---SVTLETESYITDKHIRSYMSErlLARDLPIKVEIPEe 406
Cdd:PRK15424  421 AALSapfsAALRQGLQQCETLLLHYDWPGNVRELRNLMERlalFLSVEPTPDLTPQFLQLLLPE--LARESAKTPAPRL- 497

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1490467431 407 gidlnrvieeiEKAFLLKALERTGGMKKKAAELLGM 442
Cdd:PRK15424  498 -----------LAATLQQALERFNGDKTAAANYLGI 522
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
114-456 5.79e-91

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 290.19  E-value: 5.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 114 IRKALERylLWEENLRL-RQLVEQRYQFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKN 192
Cdd:PRK15429  350 IHRLKER--LVDENLALtEQLNNVDSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNN 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 193 GPFVPINCGAIPETLLESELFGYVRGAFTGAVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTED 272
Cdd:PRK15429  428 RRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKI 507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 273 IKVDLRIIAASNQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEIKGVTPEAMELLV 352
Cdd:PRK15429  508 IQTDVRLIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLS 587

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 353 NYDYPGNVRELENIIERSVTLETESYITdkhiRSYMSERLLARDL-PIKVEIPEEGIDlnrvieeiEKAFLLKALERTGG 431
Cdd:PRK15429  588 NMEWPGNVRELENVIERAVLLTRGNVLQ----LSLPDITLPEPETpPAATVVAQEGED--------EYQLIVRVLKETNG 655

                         330       340
                  ....*....|....*....|....*...
gi 1490467431 432 M---KKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:PRK15429  656 VvagPKGAAQRLGLKRTTLLSRMKRLGI 683
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
 131-443 2.85e-87

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: 275.97  E-value: 2.85e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 131 RQLVEQRYQFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLES 210
Cdd:TIGR02329 202 RNQLRTRYRLDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEA 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 211 ELFGYVRGAFTGAVTSKR-GLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAE 289
Cdd:TIGR02329 282 ELFGYEEGAFTGARRGGRtGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTT 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 290 KIRKKEFREDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEIKGVTPEAM----ELLVNYDYPGNVRELEN 365
Cdd:TIGR02329 362 AVQQGRFRRDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPDSEAAAQVLagvaDPLQRYPWPGNVRELRN 441

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 366 IIER---SVTLETESYITDKHIRSYMSErlLARDLPIKVEIPEEGIDLNRVIEEIEKAfllkALERTGGMKKKAAELLGM 442
Cdd:TIGR02329 442 LVERlalELSAMPAGALTPDVLRALAPE--LAEASGKGKTSALSLRERSRVEALAVRA----ALERFGGDRDAAAKALGI 515


                  .
gi 1490467431 443 N 443
Cdd:TIGR02329 516 S 516
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
 142-456 5.11e-86

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 266.54  E-value: 5.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 142 NIVGKSPRMLKVfdlIEKVSQ-AKVN--VLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVRG 218
Cdd:PRK11608    7 NLLGEANSFLEV---LEQVSRlAPLDkpVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 219 AFTGAVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFRE 298
Cdd:PRK11608   84 AFTGAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 299 DLYYRL--NVVQinLPPLRERREDIPLLVQHFVDKYSREMEKEI-KGVTPEAMELLVNYDYPGNVRELENIIERSV---- 371
Cdd:PRK11608  164 DLLDRLafDVVQ--LPPLRERQSDIMLMAEHFAIQMCRELGLPLfPGFTERARETLLNYRWPGNIRELKNVVERSVyrhg 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 372 --TLETESYITDKHIRSYMSErllARDLPIKVEIPEEGIDLNRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRY 449
Cdd:PRK11608  242 tsEYPLDNIIIDPFKRRPAEE---AIAVSETTSLPTLPLDLREWQHQQEKELLQRSLQQAKFNQKRAAELLGLTYHQLRA 318


                  ....*..
gi 1490467431 450 KLAKYGL 456
Cdd:PRK11608  319 LLKKHQI 325
PRK10820 PRK10820
transcriptional regulator TyrR;
131-456 1.83e-78

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 253.07  E-value: 1.83e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 131 RQL----VEQRYQFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPET 206
Cdd:PRK10820  190 RQLqnlaVNDDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDD 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 207 LLESELFGYVRGAFTGAVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQD 286
Cdd:PRK10820  270 VVESELFGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKN 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 287 LAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEIKGVTPEAMELLVNYDYPGNVRELENI 366
Cdd:PRK10820  350 LVELVQKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNA 429

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 367 IERSVTlETESYitdkhirsymseRLLARDlpikVEIPEEGID-------LNRVIEEIEKAF---LLKALERTGGMKKKA 436
Cdd:PRK10820  430 IYRALT-QLEGY------------ELRPQD----ILLPDYDAAvavgedaMEGSLDEITSRFersVLTRLYRNYPSTRKL 492

                         330       340
                  ....*....|....*....|
gi 1490467431 437 AELLGMNFRAIRYKLAKYGL 456
Cdd:PRK10820  493 AKRLGVSHTAIANKLREYGL 512
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
 129-456 1.86e-65

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 221.86  E-value: 1.86e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 129 RLRQLVEQ-----RYQFWNIVGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAI 203
Cdd:PRK11388  308 QMRQLMTSqlgkvSHTFDHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLY 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 204 PETLLESELFGYVRGAFTGAVTSKrglLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAAS 283
Cdd:PRK11388  388 PDEALAEEFLGSDRTDSENGRLSK---FELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATT 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 284 NQDLAEKIRKKEFREDLYYRLNVVQINLPPLRERREDIPLLVQHFVDKYSREMEKEIKgVTPEAMELLVNYDYPGNVREL 363
Cdd:PRK11388  465 TADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTRLK-IDDDALARLVSYRWPGNDFEL 543

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 364 ENIIERSVTLETESYITDKHIRSYMSERLLARDLPIKVEIPeegidlNRVIEEIEKAFLLKALERTGGMKKKAAELLGMN 443
Cdd:PRK11388  544 RSVIENLALSSDNGRIRLSDLPEHLFTEQATDDVSATRLST------SLSLAELEKEAIINAAQVCGGRIQEMAALLGIG 617

                         330
                  ....*....|...
gi 1490467431 444 FRAIRYKLAKYGL 456
Cdd:PRK11388  618 RTTLWRKMKQHGI 630
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
 157-373 9.62e-43

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: 158.07  E-value: 9.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 157 IEKV---SQAKVnvLILGESGTGKELVAKAIhYNSPRKN----GPFVPINC------GAIpetlleSELFGYVRGAFTGA 223
Cdd:COG4650   200 IERVairSRAPI--LLTGPTGAGKSQLARRI-YELKKARhqvsGRFVEVNCatlrgdGAM------SALFGHVKGAFTGA 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 224 VTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDLRIIAASNQDLAEKIRKKEFREDLYYR 303
Cdd:COG4650   271 VSDRAGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLAR 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 304 LNVVQINLPPLRERREDIPLLVQHFVDKYSRE------MEKEIK------GVTPEAMellvnydYPGNVRELENIIERSV 371
Cdd:COG4650   351 INLWTFRLPGLAERREDIEPNLDYELARFAREqgrrvrFNKEARarylafATSPEAL-------WSGNFRDLNASVTRMA 423


                  ..
gi 1490467431 372 TL 373
Cdd:COG4650   424 TL 425
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 5-132 4.33e-40

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: 140.32  E-value: 4.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQ 132
Cdd:cd17549    81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQ 128
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 5-119 8.51e-38

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: 133.39  E-value: 8.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALE 119
Cdd:cd17550    81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 5-123 2.78e-35

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: 126.93  E-value: 2.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLL 123
Cdd:cd17572    81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKL 119
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 3-121 4.32e-35

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: 129.31  E-value: 4.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTA 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERY 121
Cdd:COG0745    82 RDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRR 120
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 3-120 5.01e-35

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: 126.50  E-value: 5.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPDTLVIMI 80
Cdd:COG0784     6 KRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRriRALPRLPDIPIIAL 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:COG0784    86 TAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLAR 125
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 156-367 6.65e-34

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: 135.24  E-value: 6.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 156 LIEKVSQAK---------VNVLILGESGTGKELVAKAIH-Y----NSPRKNGPFVPINCgAI----PEtLLESELFGYVR 217
Cdd:COG1221   113 LKNAIEQAKaailyppkgLHTLILGPTGVGKSFFAELMYeYaieiGVLPEDAPFVVFNC-ADyannPQ-LLMSQLFGYVK 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 218 GAFTGAVTSKRGLLEIASGGTLFLDEIGDLPLSLQVKLLRVIQEREFKRVGGTE-DIKVDLRIIAASNQDLaEKIRKKEF 296
Cdd:COG1221   191 GAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGETEkTRKANVRIIFATTEDP-ESSLLKTF 269

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431 297 RedlyyRLNVVQINLPPLRER----REDiplLVQHFVDKYSREMEKEIKgVTPEAMELLVNYDYPGNVRELENII 367
Cdd:COG1221   270 L-----RRIPMVIKLPSLEERsleeRLE---LIKHFFKEEAKRLNKPIK-VSKEVLKALLLYDCPGNIGQLKSDI 335
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 1-136 1.05e-33

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: 126.43  E-value: 1.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNP--DTLVI 78
Cdd:COG3437     5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrDIPVI 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467431  79 MITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQLVEQ 136
Cdd:COG3437    85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKL 142
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 4-119 1.35e-33

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: 122.51  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGY 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGA-YDYITKPFQVDEVKLTIRKALE 119
Cdd:cd17569    82 ADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 3-114 3.29e-33

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: 123.48  E-value: 3.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELN--PDTLVIMI 80
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPrtADIPIIFL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTI 114
Cdd:COG3706    82 TALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 5-115 6.88e-33

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: 120.33  E-value: 6.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIR 115
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 6-104 1.33e-32

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: 119.25  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   6 LVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYGS 85
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80

                          90
                  ....*....|....*....
gi 1490467431  86 PEGAVEAMKEGAYDYITKP 104
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 4-104 1.75e-30

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: 113.33  E-value: 1.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKE-GYKVTAT-TDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMIT 81
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEaGFEVVGEaENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80

                          90       100
                  ....*....|....*....|...
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKP 104
Cdd:COG4753    81 GYSDFEYAQEAIKLGADDYLLKP 103
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 3-115 1.89e-30

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: 114.08  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGY-KVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLV--IM 79
Cdd:cd17551     1 MRILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVpiVM 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIR 115
Cdd:cd17551    81 ITADTDREVRLRALEAGATDFLTKPFDPVELLARVR 116
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
 1-119 3.48e-30

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: 113.35  E-value: 3.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMI 80
Cdd:COG5803     1 MMKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMM 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALE 119
Cdd:COG5803    81 TAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 4-118 1.07e-28

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: 109.28  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd19919    82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 6-104 1.78e-28

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: 107.88  E-value: 1.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   6 LVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYGS 85
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80

                          90
                  ....*....|....*....
gi 1490467431  86 PEGAVEAMKEGAYDYITKP 104
Cdd:cd17574    81 EEDKVLGLELGADDYITKP 99
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 5-157 2.40e-28

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: 110.96  E-value: 2.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYLLWEENLRLRQLVEQRYQfwnivGKSPRMLKVFDLI 157
Cdd:COG4566    82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRARLA-----SLTPREREVLDLV 149
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 5-120 4.16e-28

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: 107.81  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKE--GYKVTAT-TDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMIT 81
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEelGFEVVGEaENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd17536    81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 4-132 5.19e-26

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 102.74  E-value: 5.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKK-EGYKVTAT-TDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMIT 81
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERlPGFEVVGVaSSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVIT 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKPFQVDEvkltIRKALERYLLWEENLRLRQ 132
Cdd:COG4565    85 AARDPETVREALRAGVVDYLIKPFTFER----LREALERYLEYRRLLREDQ 131
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 2-121 5.74e-26

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: 103.84  E-value: 5.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   2 EARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMIT 81
Cdd:COG4567     4 DRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKPFQVDEvkltIRKALERY 121
Cdd:COG4567    84 GYASIATAVEAIKLGADDYLAKPADADD----LLAALERA 119
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 4-121 6.41e-26

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 105.28  E-value: 6.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKK-EGYKVTAT-TDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMIT 81
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKyPDLEVVGEaSNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490467431  82 AYgsPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERY 121
Cdd:COG3279    83 AY--DEYALEAFEVNAVDYLLKPIDEERLAKALEKAKERL 120
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 4-105 3.36e-25

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: 99.11  E-value: 3.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDT---LVIMI 80
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKE-DPETrhiPVIMI 79

                          90       100
                  ....*....|....*....|....*
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPF 105
Cdd:cd17538    80 TALDDREDRIRGLEAGADDFLSKPI 104
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 5-118 4.85e-25

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: 99.21  E-value: 4.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd17537    83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 5-114 5.21e-25

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: 99.08  E-value: 5.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKEL---NPDTLVIMIT 81
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeggGRRTPIIALT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTI 114
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 4-110 1.03e-24

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 97.90  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81

                          90       100
                  ....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEV 110
Cdd:cd17563    82 ASIATAVEAIKLGADDYLAKPADADEI 108
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
144-314 1.07e-24

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 98.95  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 144 VGKSPRMLKVFDLIEKVSQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESelfgyvrgaftga 223
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 224 vtskrglleiASGGTLFLDEIGDLPLSLQVKLLRVIQEREfkrvggtediKVDLRIIAASNQDLAEKIRKKEFREDLYYR 303
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127

                         170
                  ....*....|.
gi 1490467431 304 LNVVQINLPPL 314
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 3-117 1.73e-24

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: 97.68  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490467431  83 YgsPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKA 117
Cdd:cd17554    81 Y--SEYKSDFSSWAADAYVVKSSDLTELKETIKRL 113
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 4-120 2.42e-24

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: 97.42  E-value: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd17615    81 DSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLRR 117
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 3-106 2.46e-24

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: 97.27  E-value: 2.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEK----SMCDFLEimlkKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVI 78
Cdd:cd17555     1 ATILVIDDDEvvreSIAAYLE----DSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVI 76

                          90       100
                  ....*....|....*....|....*...
gi 1490467431  79 MITAYGSPEGAVEAMKEGAYDYITKPFQ 106
Cdd:cd17555    77 VVSGAGVMSDAVEALRLGAWDYLTKPIE 104
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 5-111 3.84e-24

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: 96.54  E-value: 3.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALE--KDFFHMVLTDIRMPEVDGFEILRRAKELnPDTLVIMITA 82
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79

                          90       100
                  ....*....|....*....|....*....
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEVK 111
Cdd:cd17584    80 DGSTSTVMKGLAHGACDYLLKPVSIEDLK 108
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 6-120 5.88e-24

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: 96.14  E-value: 5.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   6 LVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYGS 85
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490467431  86 PEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd17625    81 VEDRVKGLDLGADDYLPKPFSLAELLARIRALLRR 115
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 5-105 2.68e-23

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: 93.73  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTL---VIMIT 81
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKA-DPATRhipVIFLT 79

                          90       100
                  ....*....|....*....|....
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKPF 105
Cdd:cd19920    80 ALTDTEDKVKGFELGAVDYITKPF 103
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 161-313 6.01e-23

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: 94.52  E-value: 6.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 161 SQAKVNVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYVrgaftgAVTSKRGLLEIASGGTLF 240
Cdd:cd00009    16 LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLLFELAEKAKPGVLF 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490467431 241 LDEIGDLPLSLQVKLLRVIQEREFKRVggtedIKVDLRIIAASNQDLAEKirkkeFREDLYYRLNVVqINLPP 313
Cdd:cd00009    90 IDEIDSLSRGAQNALLRVLETLNDLRI-----DRENVRVIGATNRPLLGD-----LDRALYDRLDIR-IVIPL 151
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
 4-130 1.67e-22

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: 92.81  E-value: 1.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKkEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1490467431  84 GSPEGAVEAMKE-GAYDYITKPFQVDEVKLTIRKALERYLLWEENLRL 130
Cdd:cd17596    81 TDSEDIIAGINEaGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERL 128
fixJ PRK09390
response regulator FixJ; Provisional
 2-120 2.16e-22

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 94.68  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   2 EARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMIT 81
Cdd:PRK09390    3 KGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMT 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK09390   83 GHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQ 121
pleD PRK09581
response regulator PleD; Reviewed
 1-131 5.35e-22

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 98.05  E-value: 5.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTL---V 77
Cdd:PRK09581    1 MTARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKS-DPATThipV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431  78 IMITAYGSPEGAVEAMKEGAYDYITKPfqVDEVKLTIR-KALERYLLWEENLRLR 131
Cdd:PRK09581   80 VMVTALDDPEDRVRGLEAGADDFLTKP--INDVALFARvKSLTRLKMVIDELRLR 132
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
 5-104 8.98e-22

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: 89.52  E-value: 8.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80

                          90       100
                  ....*....|....*....|
gi 1490467431  85 SPEGAVEAMKEGAYDYITKP 104
Cdd:cd19926    81 SLDTAIEALKAGAFDFLTKP 100
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 4-118 4.61e-21

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 88.10  E-value: 4.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTAT-TDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYEVVGEaANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSA 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd17542    82 MGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 6-120 5.22e-21

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: 88.10  E-value: 5.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   6 LVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPDTLVIMITAY 83
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRilRSDPKTSSIPIIMLTAK 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIrKALER 120
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKPFSPRELLARV-KAVLR 116
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 5-109 6.05e-21

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: 87.51  E-value: 6.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPDTLVIMITA 82
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARrlRELPWLANTPAIALTG 80

                          90       100
                  ....*....|....*....|....*..
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDE 109
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDE 107
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 3-118 6.10e-21

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: 87.74  E-value: 6.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELnP---DTLVIM 79
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKL-PaykFTPILM 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd17562    80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 4-118 9.67e-21

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: 87.22  E-value: 9.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:cd17553     2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd17553    82 GELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 5-120 3.99e-20

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: 85.23  E-value: 3.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRkALER 120
Cdd:cd17624    81 GVDDRVAGLDAGADDYLVKPFALEELLARLR-ALLR 115
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 4-118 4.51e-20

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: 85.47  E-value: 4.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYK-VTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPDTLVIMI 80
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKtiRADGALSHLPVLMV 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd19923    82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 4-105 9.80e-19

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: 81.01  E-value: 9.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDF-FHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80

                          90       100
                  ....*....|....*....|...
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPF 105
Cdd:cd18160    81 GAAAAPELLSDAVGDNATLKKPF 103
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 5-120 1.41e-18

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 80.93  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNpDTLVIMITAYG 84
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd17614    80 SEVDKVLGLELGADDYVTKPFSNRELLARVKANLRR 115
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
 5-120 2.13e-18

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: 80.79  E-value: 2.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd19934    81 SWQDKVEGLDAGADDYLTKPFHIEELLARLRALIRR 116
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 4-109 2.79e-18

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: 80.64  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDF-FHMVLTDIRMPEVDGFEILRRA-KELNPDTLVIM-I 80
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIrKKYSRDQLAIIgI 81

                          90       100
                  ....*....|....*....|....*....
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDE 109
Cdd:cd17544    82 SASGDNALSARFIKAGANDFLTKPFLPEE 110
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 5-104 6.24e-18

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: 78.64  E-value: 6.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80

                          90       100
                  ....*....|....*....|
gi 1490467431  85 SPEGAVEAMKEGAYDYITKP 104
Cdd:cd19935    81 SVEDRVKGLDLGADDYLVKP 100
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 1-137 7.33e-18

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: 81.54  E-value: 7.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTAT-TDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTlVIM 79
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAEaADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPAP-VIL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYL----LWEENLRLRQLVEQR 137
Cdd:COG3707    81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRelraLRRELAKLREALEER 142
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 5-119 1.26e-17

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: 78.32  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKE-GYKVTATT-DPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEpDIEVVGEAaDGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALE 119
Cdd:cd17535    81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
 1-120 1.74e-17

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


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 81.22  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAK--ELNPDTLVI 78
Cdd:TIGR02154   1 MTRRILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRrrPETRAIPII 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1490467431  79 MITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:TIGR02154  81 MLTARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLRR 122
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 5-120 1.89e-17

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: 77.73  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMITAYG 84
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTARG 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd17623    80 DDIDRILGLELGADDYLPKPFNPRELVARIRAILRR 115
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 5-123 2.42e-17

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: 77.75  E-value: 2.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTL---VIMIT 81
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKS-DPDLKdipVILLT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKPFqvDEVKLTIRKaleRYLL 123
Cdd:cd17598    80 TLSDPRDVIRGLECGADNFITKPY--DEKYLLSRI---KYIL 116
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 5-120 4.56e-17

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: 77.04  E-value: 4.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd17627    81 SVSDRVAGLDAGADDYLVKPFALEELLARVRALLRR 116
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 3-118 5.28e-17

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: 76.90  E-value: 5.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAK--ELNPDTLVIMI 80
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKrdEMTRDIPIIML 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd17618    81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 4-104 9.68e-17

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: 76.28  E-value: 9.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKE-GYKVTAT-TDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPdTLVIMIT 81
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILESDpDIEVVGTaRDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVS 80

                          90       100
                  ....*....|....*....|....*
gi 1490467431  82 AYGSPEGAV--EAMKEGAYDYITKP 104
Cdd:cd17541    81 SLTEEGAEItlEALELGAVDFIAKP 105
orf27 CHL00148
Ycf27; Reviewed
 4-120 1.27e-16

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 78.99  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEI---LRRAKelnpDTLVIMI 80
Cdd:CHL00148    8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVcqeIRKES----DVPIIML 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:CHL00148   84 TALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRR 123
ompR PRK09468
osmolarity response regulator; Provisional
 4-120 1.83e-16

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 78.48  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK09468    7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAK 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK09468   87 GEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRR 123
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 3-118 2.61e-16

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: 74.81  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMITA 82
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd17626    80 KSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 1-120 1.12e-15

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 76.15  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMI 80
Cdd:PRK11083    2 QQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK11083   82 TARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTILRR 121
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 5-104 1.25e-15

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: 72.23  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPdtlVIMITA 82
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRqlRARSNVP---VIMVTA 77

                          90       100
                  ....*....|....*....|..
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKP 104
Cdd:cd17621    78 KDSEIDKVVGLELGADDYVTKP 99
PRK15347 PRK15347
two component system sensor kinase;
4-104 2.07e-15

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 78.92  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRR----AKELNPDTLVIM 79
Cdd:PRK15347  692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLwrddPNNLDPDCMIVA 771

                          90       100
                  ....*....|....*....|....*
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKP 104
Cdd:PRK15347  772 LTANAAPEEIHRCKKAGMNHYLTKP 796
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 3-118 3.09e-15

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: 71.67  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTAT-TDPKEALTALEKDFFHMVLTDIRMP-EVDGFEILRRAKElNPDTLVIMI 80
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLGYEVVGIaDSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE-KFDIPVIFL 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd17534    80 TAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
4-120 3.85e-15

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 74.45  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEkDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMITAY 83
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQ-THQTPVIMLTAR 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK10955   81 GSELDRVLGLELGADDYLPKPFNDRELVARIRAILRR 117
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 4-116 6.89e-15

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: 70.65  E-value: 6.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDE----KSMCDFLEImlkkEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTL--- 76
Cdd:cd17548     1 KILIVEDNplnmKLARDLLES----AGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKE-DPATRdip 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490467431  77 VIMITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRK 116
Cdd:cd17548    76 VIALTAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 5-120 4.84e-14

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: 68.33  E-value: 4.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTA--TTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIVgeAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490467431  83 YgsPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd17532    81 Y--DEYAVEAFELNAVDYLLKPFSEERLAEALAKLRKR 116
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 5-104 5.39e-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: 67.53  E-value: 5.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80

                          90       100
                  ....*....|....*....|
gi 1490467431  85 SPEGAVEAMKEGAYDYITKP 104
Cdd:cd19928    81 TLMTAVKAAERGAFEYLPKP 100
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 5-104 7.92e-14

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 67.19  E-value: 7.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMITAYG 84
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLRE-WSAVPVIVLSARD 79

                          90       100
                  ....*....|....*....|
gi 1490467431  85 SPEGAVEAMKEGAYDYITKP 104
Cdd:cd17620    80 EESDKIAALDAGADDYLTKP 99
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 5-104 1.08e-13

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: 66.70  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNpDTLVIMITAYG 84
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79

                          90       100
                  ....*....|....*....|
gi 1490467431  85 SPEGAVEAMKEGAYDYITKP 104
Cdd:cd19936    80 DEIDEVFGLRMGADDYITKP 99
PRK15479 PRK15479
transcriptional regulator TctD;
4-153 1.25e-13

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 69.75  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTAR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERYL-LWEENLRLRQLVEQRYQFWNIVGK----SPRMLKV 153
Cdd:PRK15479   82 SAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSAgQVQEVQQLGELIFHDEGYFLLQGQplalTPREQAL 156
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 4-121 1.42e-13

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: 66.88  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKK-EGYKVTATTDP-KEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMIT 81
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQvPGFTVIGTAGTgEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKPFQVDevklTIRKALERY 121
Cdd:cd19925    82 AANDVETVREALRLGVVDYLIKPFTFE----RLRQRLERY 117
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
 5-115 5.26e-13

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: 65.12  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIR 115
Cdd:cd17616    81 DIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 5-104 6.31e-13

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 64.71  E-value: 6.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPD--TL-VIMIT 81
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRK-NADfdTIpVIFLT 79

                          90       100
                  ....*....|....*....|...
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKP 104
Cdd:cd19927    80 AKGMTSDRIKGYNAGCDGYLSKP 102
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 4-118 7.64e-13

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 64.88  E-value: 7.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKE-GYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDT---LVIM 79
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQA-NPETqsiPVIL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPFqvDEVKLT--IRKAL 118
Cdd:cd17552    82 LTAKAQPSDRQRFASLGVAGVIAKPF--DPLTLAeqIAKLL 120
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 3-115 1.04e-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: 64.33  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMITA 82
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE-QSEVGIILVTG 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEvkLTIR 115
Cdd:cd17619    80 RDDEVDRIVGLEIGADDYVTKPFNPRE--LLVR 110
PRK10336 PRK10336
two-component system response regulator QseB;
4-120 1.06e-12

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 67.23  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTAR 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK10336   82 DALAERVEGLRLGADDYLCKPFALIEVAARLEALMRR 118
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 4-57 1.44e-12

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: 62.20  E-value: 1.44e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1490467431    4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMP 57
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10610 PRK10610
chemotaxis protein CheY;
2-120 1.53e-12

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 64.61  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   2 EARILVVDDEKSMCDFLEIMLKKEGY-KVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPDTLVI 78
Cdd:PRK10610    5 ELKFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKtiRADGAMSALPVL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1490467431  79 MITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK10610   85 MVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
PRK10643 PRK10643
two-component system response regulator PmrA;
4-130 1.78e-12

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 66.60  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERY------LLWEENLRL 130
Cdd:PRK10643   82 DTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHqgqgenELQVGNLTL 134
PRK11517 PRK11517
DNA-binding response regulator HprR;
4-121 1.85e-12

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 66.46  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNpDTLVIMITAY 83
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAK-QTPVICLTAR 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERY 121
Cdd:PRK11517   81 DSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQH 118
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 5-116 4.05e-12

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: 62.85  E-value: 4.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPdtlVIMITA 82
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRtiRARSDVP---IIIISG 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490467431  83 YGSPEGA-VEAMKEGAYDYITKPFQVDEVKLTIRK 116
Cdd:cd17594    79 DRRDEIDrVVGLELGADDYLAKPFGLRELLARVRA 113
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1-120 5.01e-12

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 65.51  E-value: 5.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKE--LNPDTLVI 78
Cdd:PRK10161    1 MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKResMTRDIPVV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1490467431  79 MITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK10161   81 MLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRR 122
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 4-121 6.01e-12

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: 62.82  E-value: 6.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEG--YKVTATTDPKEALtalekDFFH------------MVLTDIRMPEVDGFEILRRAK 69
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEAL-----DFLRgegeyadaprpdLILLDLNMPRMDGFEVLREIK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431  70 ElNPDTL---VIMITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRkALERY 121
Cdd:cd17557    76 A-DPDLRripVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIR-SLGEY 128
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 5-104 8.90e-12

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: 61.23  E-value: 8.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEI---LRRAKELNpDTLVIMIT 81
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELcslLRKSSALK-DTPIIMLT 79

                          90       100
                  ....*....|....*....|...
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKP 104
Cdd:cd17602    80 GKDGLVDRIRAKMAGASGYLTKP 102
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
 5-108 1.21e-11

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 61.29  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80

                          90       100
                  ....*....|....*....|....
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVD 108
Cdd:cd17573    81 KTEQEIEAFKEGADDYIAKPFDFK 104
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 4-105 1.45e-11

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: 61.09  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFL-EIMLKKEGYKVTATT-DPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPDTLVIM 79
Cdd:cd17561     3 KVLIADDNREFVQLLeEYLNSQPDMEVVGVAhNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEklRRMRLEKRPKIIM 82

                          90       100
                  ....*....|....*....|....*.
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPF 105
Cdd:cd17561    83 LTAFGQEDITQRAVELGASYYILKPF 108
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 166-304 1.75e-11

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: 62.01  E-value: 1.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  166 NVLILGESGTGKELVAKAIHYNSPRKNGPFVPINCGAIPETLLESELFGYV--RGAFTGAVTSKRGLLEIA---SGGTLF 240
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVggKKASGSGELRLRLALALArklKPDVLI 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467431  241 LDEIGDLPLSLQVKLLRVIQERefkRVGGTEDIKVDLRIIAASN--QDLAEKIRKKEFREDLYYRL 304
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEEL---RLLLLLKSEKNLTVILTTNdeKDLGPALLRRRFDRRIVLLL 146
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 4-120 2.22e-11

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 60.89  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTA-TTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTlVIMITA 82
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIAP-IVLLTA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd19932    81 YSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 5-104 3.26e-11

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: 60.08  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEK---------DFFHMVLTDIRMPEVDGFEILRRAKElNP-- 73
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELRD-DPrl 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1490467431  74 -DTLVIMITAYGSPEGAVEAMKEGAYDYITKP 104
Cdd:cd19924    80 aNIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
 5-112 3.29e-11

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 60.81  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLK---KEGYKVTATTDPKEALTALEK-----DFFHMVLTDIRMPEVDGFEILRRAKELNPDTL 76
Cdd:cd17595     3 ILTVDDDPQVLRAVARDLRrqyGKDYRVLRADSGAEALDALKElklrgEAVALFLVDQRMPEMDGVEFLEKAMELFPEAK 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  77 VIMITAYGSPEGAVEAMKEGAYD-YITKPFQVDEVKL 112
Cdd:cd17595    83 RVLLTAYADTDAAIRAINDVQLDyYLLKPWDPPEEKL 119
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 4-121 3.31e-11

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: 60.24  E-value: 3.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDD----EKSMCDFLEimlKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIM 79
Cdd:cd17593     2 KVLICDDssmaRKQLARALP---ADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1490467431  80 ITAYGSPEgAVEAMKE-GAYDYITKPFQVDEVkltiRKALERY 121
Cdd:cd17593    79 VSGDVQPE-AKERVLElGALAFLKKPFDPEKL----AQLLEEL 116
PRK10816 PRK10816
two-component system response regulator PhoP;
4-120 3.34e-11

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 62.83  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK10816   82 ESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRR 118
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 5-111 7.77e-11

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: 59.30  E-value: 7.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDekSMCD--FLEIMLKKEGYKVTATTDPKEALTALEKDF-----------FHMVLTDIRMPEVDGFEILRRAKE- 70
Cdd:cd17581     1 VLAVDD--SLVDrkVIERLLRISSCRVTAVDSGKRALEFLGLEDeedssnfnepkVNMIITDYCMPGMTGYDLLKKVKEs 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1490467431  71 --LNPDTLVIMiTAYGSPEGAVEAMKEGAYDYITKPFQVDEVK 111
Cdd:cd17581    79 saLKEIPVVIM-SSENIPTRISRCLEEGAEDFLLKPVKLADVK 120
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 4-105 1.45e-10

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: 58.61  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYK-VTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1490467431  83 YGSpeGAVEAMKEGAYDY-------ITKPF 105
Cdd:cd17530    82 LDG--GILESAETLAGANglnllgtLSKPF 109
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 4-118 1.45e-10

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: 58.16  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELnPDTLVIMITAY 83
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRF-SDVPIIMVTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd19938    80 VEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 4-120 1.70e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 60.71  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:PRK09836   82 GTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRR 118
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
 5-111 6.10e-10

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: 56.50  E-value: 6.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGY-KVTATTDPKEALTALEKDFFHMVLTDIRMPE-VDG---FEILRRAKELNPDTLVIM 79
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGqqlLEELRHKKLISPSTVFIM 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPFQVDEVK 111
Cdd:cd17589    81 VTGESSRAMVLSALELEPDDYLLKPFTVSELR 112
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 5-118 6.32e-10

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: 56.52  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPdTLVIMITAYG 84
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSRD 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd18159    80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 4-120 6.82e-10

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: 56.61  E-value: 6.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMITAY 83
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE-HSHVPILMLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALER 120
Cdd:cd19939    80 TEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR 116
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-105 8.01e-10

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 60.16  E-value: 8.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDD----EKSMCDFLEimlKKEGYKVTAT-TDPKEALTALEK---DffhmVLT-DIRMPEVDGFEILRRAKEL 71
Cdd:PRK00742    2 MKIRVLVVDDsafmRRLISEILN---SDPDIEVVGTaPDGLEAREKIKKlnpD----VITlDVEMPVMDGLDALEKIMRL 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  72 NPdTLVIMI---TAYGSpEGAVEAMKEGAYDYITKPF 105
Cdd:PRK00742   75 RP-TPVVMVsslTERGA-EITLRALELGAVDFVTKPF 109
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
414-453 8.02e-10

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 53.94  E-value: 8.02e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1490467431 414 IEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAK 453
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 5-104 8.98e-10

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: 55.87  E-value: 8.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFH--MVLTDIRMPEVDGFEILR---RAKELNpDTLVIM 79
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEidLILTEVDLPVSSGFKLLSyimRHKICK-NIPVIM 79

                          90       100
                  ....*....|....*....|....*
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKP 104
Cdd:cd17582    80 MSSQDSVGVVFKCLSKGAADYLVKP 104
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 5-121 9.29e-10

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 58.66  E-value: 9.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPdTLVIMITAYG 84
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA-IPVIVLSARS 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  85 SPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERY 121
Cdd:PRK10529   83 EESDKIAALDAGADDYLSKPFGIGELQARLRVALRRH 119
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
 4-108 2.52e-09

Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 57.89  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFL-EIMLKKEGYKVTATT-DPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDT--LVIM 79
Cdd:COG5801     6 KVLIADDNREFCELLeEYLSSQPDMEVVGVAyNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLREMNLEKrpKVIM 85

                          90       100
                  ....*....|....*....|....*....
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKPFQVD 108
Cdd:COG5801    86 LTAFGQEDITQRAVELGADYYILKPFDLD 114
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 5-105 3.17e-09

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 54.27  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDF-FHMVLTDIRMP-EVDGFEILRRAKELNPDTLVIMITA 82
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80

                          90       100
                  ....*....|....*....|...
gi 1490467431  83 YGSPEGAVEAMKEGaYDYITKPF 105
Cdd:cd18161    81 YAENAIEGGDLAPG-VDVLSKPF 102
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 166-317 4.69e-09

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 54.61  E-value: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 166 NVLILGESGTGK----ELVAKAIhynsprKNGPFVPINCgaiPETLLESELFGYVRGAFTGAVTSKRGLLEIA-SGGTLF 240
Cdd:pfam07728   1 GVLLVGPPGTGKtelaERLAAAL------SNRPVFYVQL---TRDTTEEDLFGRRNIDPGGASWVDGPLVRAArEGEIAV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431 241 LDEIGDLPLSLQVKLLRVIQEREFKRVGGTEDIKVDL---RIIAASNqdlaekirkkefreDLYYRLNVVqinLPPLRER 317
Cdd:pfam07728  72 LDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAAPdgfRLIATMN--------------PLDRGLNEL---SPALRSR 134
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 5-119 5.69e-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: 5.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEG--YKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITA 82
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490467431  83 YGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALE 119
Cdd:cd19930    81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 5-104 9.15e-09

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: 52.66  E-value: 9.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKE--GYKVTATTDPKEA---LTALEKDffhMVLTDIRMPEVDGFEILRRAKELNPDTLVIM 79
Cdd:cd17565     1 FYIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAydeILFLQPD---IVLIDLLMPGMDGIQLVRKLKDTGSNGKFIM 77

                          90       100
                  ....*....|....*....|....*
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITKP 104
Cdd:cd17565    78 ISQVSDKEMIGKAYQAGIEFFINKP 102
PRK11173 PRK11173
two-component response regulator; Provisional
 4-140 9.79e-09

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 55.79  E-value: 9.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMITAY 83
Cdd:PRK11173    5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELRE-QANVALMFLTGR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEvkLTI--RKALERYLLWEENLRLRQLVEqRYQF 140
Cdd:PRK11173   84 DNEVDKILGLEIGADDYITKPFNPRE--LTIraRNLLSRTMNLGTVSEERRSVE-SYKF 139
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 4-67 1.54e-08

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 52.97  E-value: 1.54e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKE-GYKVTAT-TDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRR 67
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEpDIEVVGEaADGEEALELLEELRPDVVLLDIRMPGMDGLEALRR 68
PRK13856 PRK13856
two-component response regulator VirG; Provisional
 5-136 1.66e-08

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 55.21  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMITAYG 84
Cdd:PRK13856    4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLAT-KSDVPIIIISGDR 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467431  85 SPEG-AVEAMKEGAYDYITKPFQVDEVKLTIRKALE--------------RYLLWEENLRLRQLVEQ 136
Cdd:PRK13856   83 LEEAdKVVALELGATDFIAKPFGTREFLARIRVALRvrpnvvrtkdrrsfCFADWTLNLRQRRLISE 149
PRK13557 PRK13557
histidine kinase; Provisional
 4-119 2.41e-08

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 56.22  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKD-FFHMVLTDIRMP-EVDGFEILRRAKELNPDTLVIMIT 81
Cdd:PRK13557  417 TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVLLTT 496

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490467431  82 AYGspEGAVEAMKEGA--YDYITKPFQVDEVKLTIRKALE 119
Cdd:PRK13557  497 GYA--EASIERTDAGGseFDILNKPYRRAELARRVRMVLD 534
PRK10766 PRK10766
two-component system response regulator TorR;
1-124 5.30e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 53.50  E-value: 5.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKElNPDTLVIMI 80
Cdd:PRK10766    1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS-RSTVGIILV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEvkLTIRKaleRYLLW 124
Cdd:PRK10766   80 TGRTDSIDRIVGLEMGADDYVTKPLELRE--LLVRV---KNLLW 118
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
5-111 7.27e-08

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 55.13  E-value: 7.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431    5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYG 84
Cdd:PRK09959   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040

                           90       100
                   ....*....|....*....|....*..
gi 1490467431   85 SPEGAVEAMKEGAYDYITKPFQVDEVK 111
Cdd:PRK09959  1041 QANEREKGLSCGMNLCLFKPLTLDVLK 1067
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 4-104 7.31e-08

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: 50.84  E-value: 7.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPdtlVIMIT 81
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRdlRPKYQGP---ILLLT 78

                          90       100
                  ....*....|....*....|...
gi 1490467431  82 AYGSPEGAVEAMKEGAYDYITKP 104
Cdd:cd17622    79 ALDSDIDHILGLELGADDYVVKP 101
PRK11697 PRK11697
two-component system response regulator BtsR;
4-120 9.12e-08

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 52.93  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEG--YKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILrraKELNPDTL--VIM 79
Cdd:PRK11697    3 KVLIVDDEPLAREELRELLQEEGdiEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELV---GMLDPEHMpyIVF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1490467431  80 ITAYGspEGAVEAMKEGAYDYITKPfqVDEVKLtiRKALER 120
Cdd:PRK11697   80 VTAFD--EYAIKAFEEHAFDYLLKP--IDPARL--AKTLAR 114
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
4-121 9.62e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 53.73  E-value: 9.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFL-EIMLKKEGYKV--TATtDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPdTLVIMI 80
Cdd:PRK12555    2 RIGIVNDSPLAVEALrRALARDPDHEVvwVAT-DGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERP-CPILIV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1490467431  81 TAygSPEGAV----EAMKEGAYDYITKPfqvdevKLTIRKALERY 121
Cdd:PRK12555   80 TS--LTERNAsrvfEAMGAGALDAVDTP------TLGIGAGLEEY 116
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 4-104 1.05e-07

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 50.09  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTAL--EKDFFHMVLTDIRMPEVDGFEILRRAKELNPDT---LVI 78
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLasAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRerpLIV 81

                          90       100
                  ....*....|....*....|....*.
gi 1490467431  79 MITAYGSPEGAVEAMKEGAYDYITKP 104
Cdd:cd19933    82 ALTANTDDSTREKCLSLGMNGVITKP 107
Fis COG2901
DNA-binding protein Fis (factor for inversion stimulation) [Transcription];
413-456 2.94e-07

DNA-binding protein Fis (factor for inversion stimulation) [Transcription];


Pssm-ID: 442146 [Multi-domain]  Cd Length: 83  Bit Score: 47.89  E-value: 2.94e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1490467431 413 VIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:COG2901    39 VLAEVEKPLLETVLEHTRGNQSRAAEMLGINRNTLRKKLKQYGL 82
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
4-121 8.17e-07

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 51.51  E-value: 8.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:PRK10841  803 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTAN 882

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDevklTIRKALERY 121
Cdd:PRK10841  883 ALAEEKQRCLEAGMDSCLSKPVTLD----VLKQTLTVY 916
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
 3-118 1.39e-06

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: 46.86  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEGYKVT--ATTDpKEALTALEKDFFHMVLTDIRMPE-VDGFEILRRAKELNpDTLVIM 79
Cdd:cd17540     1 TRVLIIEDEPLIAMDLEQIVEDLGHQVVgiARTR-DEAVALARRERPDLILADIQLADgSSGIDAVNEILTTH-DVPVIF 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490467431  80 ITAYgsPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd17540    79 VTAY--PERLLTGERPEPTFLITKPFDPEMVKAAISQAL 115
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
 1-139 1.86e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 48.91  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNpDTLVIMI 80
Cdd:PRK10710    9 NTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS-DIPIVMV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKALERY-----LLWEENLRLRQLVEQRYQ 139
Cdd:PRK10710   88 TAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCkpqreLQQQDAESPLIIDESRFQ 151
PRK09191 PRK09191
two-component response regulator; Provisional
 1-118 3.54e-06

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 48.31  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEK--SMcDfLEIMLKKEGYKVT--ATTDpKEALTALEKDFFHMVLTDIRMpeVDGF-------EILRRAk 69
Cdd:PRK09191  136 VATRVLIIEDEPiiAM-D-LEQLVESLGHRVTgiARTR-AEAVALAKKTRPGLILADIQL--ADGSsgidavnDILKTF- 209

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490467431  70 elnpDTLVIMITAYgsPE----GavEAMkEGAYdYITKPFQVDEVKLTIRKAL 118
Cdd:PRK09191  210 ----DVPVIFITAF--PErlltG--ERP-EPAF-LITKPFQPDTVKAAISQAL 252
PRK15369 PRK15369
two component system response regulator;
1-103 4.09e-06

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 47.38  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   1 MEARILVVDDEKSMCDFLEIMLKK-EGYKVTATTDPK----EALTALEKDffhMVLTDIRMPEVDGFEILRRAKELNPDT 75
Cdd:PRK15369    2 KNYKILLVDDHELIINGIKNMLAPyPRYKIVGQVDNGlevyNACRQLEPD---IVILDLGLPGMNGLDVIPQLHQRWPAM 78

                          90       100
                  ....*....|....*....|....*...
gi 1490467431  76 LVIMITAYGSPEGAVEAMKEGAYDYITK 103
Cdd:PRK15369   79 NILVLTARQEEHMASRTLAAGALGYVLK 106
PLN03029 PLN03029
type-a response regulator protein; Provisional
 5-110 7.22e-06

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 46.95  E-value: 7.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDekSMCD--FLEIMLKKEGYKVTATTDPKEALTAL---EKDF-----------------FHMVLTDIRMPEVDGF 62
Cdd:PLN03029   11 VLAVDD--SLIDrkLIEKLLKTSSYQVTTVDSGSKALKFLglhEDDRsnpdtpsvspnshqeveVNLIITDYCMPGMTGY 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1490467431  63 EILRRAKELNP--DTLVIMITAYGSPEGAVEAMKEGAYDYITKPFQVDEV 110
Cdd:PLN03029   89 DLLKKIKESSSlrNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
 5-110 9.30e-06

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


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 44.39  E-value: 9.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALT-ALEKDfFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAY 83
Cdd:cd19922     1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSlALETD-YDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDHW 79

                          90       100
                  ....*....|....*....|....*..
gi 1490467431  84 GSPEGAVEAMKEGAYDYITKPFQVDEV 110
Cdd:cd19922    80 EDLQEELEEVQRFAVSYVVKPVLISNL 106
PRK09483 PRK09483
response regulator; Provisional
 50-122 1.41e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 45.87  E-value: 1.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431  50 VLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRK--ALERYL 122
Cdd:PRK09483   51 VLMDMNMPGIGGLEATRKILRYTPDVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRSvhSGQRYI 125
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
 3-103 2.71e-05

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 45.02  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKsmcdfleiMLKKeGYKVTATTDP-----------KEALT---ALEKDffhMVLTDIRMPEVDGFEILRRA 68
Cdd:PRK10651    7 ATILLIDDHP--------MLRT-GVKQLISMAPditvvgeasngEQGIElaeSLDPD---LILLDLNMPGMNGLETLDKL 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490467431  69 KELNPDTLVIMITAYGSPEGAVEAMKEGAYDYITK 103
Cdd:PRK10651   75 REKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLK 109
PRK01905 PRK01905
Fis family transcriptional regulator;
411-456 8.60e-05

Fis family transcriptional regulator;


Pssm-ID: 179348 [Multi-domain]  Cd Length: 77  Bit Score: 40.94  E-value: 8.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1490467431 411 NRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:PRK01905   31 DMVLSCVEKPLLEVVMEQAGGNQSLAAEYLGINRNTLRKKLQQHGL 76
PRK10360 PRK10360
transcriptional regulator UhpA;
36-117 9.18e-05

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 43.43  E-value: 9.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  36 KEALTALEKDFFHMVLTDIRMPEVDGFEILrraKELNPDTLVIMITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIR 115
Cdd:PRK10360   37 REALAGLPGRGVQVCICDISMPDISGLELL---SQLPKGMATIMLSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVH 113


                  ..
gi 1490467431 116 KA 117
Cdd:PRK10360  114 TV 115
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
 3-103 9.60e-05

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 42.01  E-value: 9.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKE-GYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILR--RAKELNPDTLVIM 79
Cdd:cd17575     1 IMVLLVDDQAIIGEAVRRALADEeDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRffRANPATRDIPIIV 80

                          90       100
                  ....*....|....*....|....
gi 1490467431  80 ITAYGSPEGAVEAMKEGAYDYITK 103
Cdd:cd17575    81 LSTKEEPEVKSEAFALGANDYLVK 104
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
3-103 1.24e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 42.94  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKK--EGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMI 80
Cdd:PRK09935    4 ASVIIMDTHPIIRMSIEVLLQKnsELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFL 83

                          90       100
                  ....*....|....*....|...
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITK 103
Cdd:PRK09935   84 SSKSECFYAGRAIQAGANGFVSK 106
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
 4-119 1.78e-04

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: 41.45  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLE-----IMLKKEGYKVTATT----DPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPD 74
Cdd:cd17533     2 NIFILEDDKIQRVRLEeiienILKIENIEYVIELTgkteELLEKIKERGKNGIYFLDIDIKMEEKNGLEVAQKIRKYDPY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1490467431  75 TLVIMITAYG--SPEGAVeaMKEGAYDYITKPFQVDEVKLTIRKALE 119
Cdd:cd17533    82 AIIIFVTTHSefAPLTFE--YKVAALDFILKPLKLEEFKKRIEECIK 126
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
 4-121 2.07e-04

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 43.68  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGF---EILRRAkELNPDTLVIMI 80
Cdd:PRK11107  669 TVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIracELIRQL-PHNQNTPIIAV 747

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPfqVDEVKLtiRKALERY 121
Cdd:PRK11107  748 TAHAMAGERERLLSAGMDDYLAKP--IDEAML--KQVLLRY 784
pleD PRK09581
response regulator PleD; Reviewed
 3-137 4.11e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 42.58  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   3 ARILVVDDEKSMCDFLEIMLKKEgYKVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGfeiLR-----RAKELNPDTLV 77
Cdd:PRK09581  156 GRILLVDDDVSQAERIANILKEE-FRVVVVSDPSEALFNAAETNYDLVIVSANFENYDP---LRlcsqlRSKERTRYVPI 231

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467431  78 IMITAYGSPEGAVEAMKEGAYDYITKPfqVDE------VKLTIRKalERYllweeNLRLRQLVEQR 137
Cdd:PRK09581  232 LLLVDEDDDPRLVKALELGVNDYLMRP--IDKnellarVRTQIRR--KRY-----QDALRNNLEQS 288
fis PRK00430
DNA-binding transcriptional regulator Fis;
411-456 5.88e-04

DNA-binding transcriptional regulator Fis;


Pssm-ID: 179020 [Multi-domain]  Cd Length: 95  Bit Score: 38.89  E-value: 5.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1490467431 411 NRVIEEIEKAFLLKALERTGGMKKKAAELLGMNFRAIRYKLAKYGL 456
Cdd:PRK00430   49 ELVLAEVEAPLLDMVMQYTRGNQTRAALMLGINRGTLRKKLKKYGM 94
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 49-118 9.27e-04

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 38.87  E-value: 9.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431  49 MVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYGSPEGAVEAMKEGAYDYITKPFQVDEVKLTIRKAL 118
Cdd:cd19931    47 LILLDLNMKGMSGLDTLKALREEGVSARIVILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAA 116
PRK14084 PRK14084
DNA-binding response regulator;
4-117 9.32e-04

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 40.89  E-value: 9.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   4 RILVVDDEKSMCDFLEIMLKKEGY--KVTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMIT 81
Cdd:PRK14084    2 KALIVDDEPLARNELTYLLNEIGGfeEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIFAT 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490467431  82 AYGSpeGAVEAMKEGAYDYITKPFQVDEVKLTIRKA 117
Cdd:PRK14084   82 AHDQ--FAVKAFELNATDYILKPFEQKRIEQAVNKV 115
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
 5-115 3.73e-03

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-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 the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 37.29  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKKEgYKVTATTDPKEAL-TALEKDF-FHMVLTDIrmpevDGFEILR-----RAKELNPDTLV 77
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLSSE-HEVVVEADPDEALfRAAEGPFdLVIVSLAL-----EDFDGLRlcsqlRSLERTRQLPI 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490467431  78 IMITAYGSPEGAVEAMKEGAYDYITKPfqVDEVKLTIR 115
Cdd:cd17539    75 LAVADPGDRGRLIRALEIGVNDYLVRP--IDPNELLAR 110
PRK10693 PRK10693
two-component system response regulator RssB;
30-104 5.27e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 38.82  E-value: 5.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490467431  30 TATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMITAYGSPEGAVEAMKEGAYDYITKP 104
Cdd:PRK10693    1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75
PRK10430 PRK10430
two-component system response regulator DcuR;
5-136 6.10e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 38.17  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467431   5 ILVVDDEKSMCDFLEIMLKK-EGYK---VTATTDPKEALTALEKDFFHMVLTDIRMPEVDGFEILRRAKELNPDTLVIMI 80
Cdd:PRK10430    4 VLIVDDDAMVAELNRRYVAQiPGFQccgTASTLEQAKEIIFNSDTPIDLILLDIYMQQENGLDLLPVLHEAGCKSDVIVI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467431  81 TAYGSPEGAVEAMKEGAYDYITKPFQVDEVKltirKALERYLLWEENLRLRQLVEQ 136
Cdd:PRK10430   84 SSAADAATIKDSLHYGVVDYLIKPFQASRFE----EALTGWRQKKMALEKHQYYDQ 135
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH