NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|520869243|ref|WP_020309162|]
View 

sigma-54 dependent transcriptional regulator [Stutzerimonas stutzeri]

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, ...
 9-449 3.91e-178

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: 505.27  E-value: 3.91e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   9 TQAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILI 88
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRlaladrqqlsaRLLGQSRAMLRLREQIGA 168
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS-----------GLIGRSPAMQEVRRLIEK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 169 LAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTL 248
Cdd:COG2204  150 VAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 249 FLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSE 328
Cdd:COG2204  230 FLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 329 DILLLFQHFAEAAAQRHGLPVReLQPGQRAMLLQHTWPGNVRELQNTAERFALGLGLGLERPGSEPsaglagggslgEQV 408
Cdd:COG2204  310 DIPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP-----------EAL 377

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 520869243 409 EAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHG 449
Cdd:COG2204  378 EEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 9-449 3.91e-178

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: 505.27  E-value: 3.91e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   9 TQAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILI 88
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRlaladrqqlsaRLLGQSRAMLRLREQIGA 168
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS-----------GLIGRSPAMQEVRRLIEK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 169 LAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTL 248
Cdd:COG2204  150 VAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 249 FLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSE 328
Cdd:COG2204  230 FLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 329 DILLLFQHFAEAAAQRHGLPVReLQPGQRAMLLQHTWPGNVRELQNTAERFALGLGLGLERPGSEPsaglagggslgEQV 408
Cdd:COG2204  310 DIPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP-----------EAL 377

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 520869243 409 EAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHG 449
Cdd:COG2204  378 EEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
9-450 2.92e-125

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 372.26  E-value: 2.92e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   9 TQAQVVLI-DDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVIL 87
Cdd:PRK11361   2 TAINRILIvDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLALADRQQlSARLLGQSRAMLRLREQIG 167
Cdd:PRK11361  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQ-WGHILTNSPAMMDICKDTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 168 ALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGT 247
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 248 LFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERS 327
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 328 EDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAER----------FALGLGLGL---ERPGSEP 394
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERavvmnsgpiiFSEDLPPQIrqpVCNAGEV 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 520869243 395 SAGLAGGGSLGEQVEAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHGL 450
Cdd:PRK11361 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
 13-446 1.90e-124

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


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 370.22  E-value: 1.90e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQlvlDNRSLRLAlADRQQLSARLLGQSRAMLRLREQIGALAGT 172
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQ---EQVALPAD-AGEAEDSAELIGEAPAMQEVFRAIGRLSRS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  173 QADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTLFLDE 252
Cdd:TIGR01818 157 DITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  253 IESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDILL 332
Cdd:TIGR01818 237 IGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  333 LFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAERFAL--------------GLGLGlERPGSEPSAGL 398
Cdd:TIGR01818 317 LARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVmasgdevlvsdlpaELALT-GRPASAPDSDG 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520869243  399 AGGGSLG------------------EQVEAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLR 446
Cdd:TIGR01818 396 QDSWDEAleawakqalsrgeqglldRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLK 461
Sigma54_activat pfam00158
Sigma-54 interaction domain;
152-319 7.25e-100

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 296.62  E-value: 7.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  152 LLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTG 231
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  232 AQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYY 311
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160


                  ....*...
gi 520869243  312 RLNVAPLR 319
Cdd:pfam00158 161 RLNVIPIE 168
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 13-142 1.91e-70

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 219.67  E-value: 1.91e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLAL 142
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
tetrathio_RR NF040749
tetrathionate respiration response regulator TtrR;
15-155 3.40e-25

tetrathionate respiration response regulator TtrR;


Pssm-ID: 468713 [Multi-domain]  Cd Length: 191  Bit Score: 102.05  E-value: 3.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  15 LIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHGDI 94
Cdd:NF040749   4 LVDDDVAVTDACRFLLESLGYEVQCWNDSEAFLAQADLYQEGVVLLDMRMPGLDGHQVHQALREQGSTLAVVFLTGHGDV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520869243  95 QLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRL---ALADRQQLSARLLGQ 155
Cdd:NF040749  84 PMAVEQMKLGAVDFLQKPVSAAPLQAALERALAVSAAAFERHQIRQryqSLTPKEREIAGLVVQ 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 176-313 1.57e-10

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: 59.31  E-value: 1.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   176 VLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVES---ELFGHEPGAFTGAQKRRIGkFEFA---NGGTLF 249
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLA-LALArklKPDVLI 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520869243   250 LDEIESMSLDLQVKLLRLLQErvvERLGGNQSIALDIRVIAAT--KEDLRVAADQGRFRADLYYRL 313
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTndEKDLGPALLRRRFDRRIVLLL 146
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 9-449 3.91e-178

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: 505.27  E-value: 3.91e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   9 TQAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILI 88
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRlaladrqqlsaRLLGQSRAMLRLREQIGA 168
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS-----------GLIGRSPAMQEVRRLIEK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 169 LAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTL 248
Cdd:COG2204  150 VAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 249 FLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSE 328
Cdd:COG2204  230 FLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 329 DILLLFQHFAEAAAQRHGLPVReLQPGQRAMLLQHTWPGNVRELQNTAERFALGLGLGLERPGSEPsaglagggslgEQV 408
Cdd:COG2204  310 DIPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP-----------EAL 377

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 520869243 409 EAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHG 449
Cdd:COG2204  378 EEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 128-451 1.07e-137

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: 403.38  E-value: 1.07e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 128 LRQLVLDNRSLRLALADRQQLS-ARLLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVA 206
Cdd:COG3829  115 LKRLERKLREEELERGLSAKYTfDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 207 INAGALAESVVESELFGHEPGAFTGAQKR-RIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALD 285
Cdd:COG3829  195 VNCAAIPENLLESELFGYEKGAFTGAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVD 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 286 IRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTW 365
Cdd:COG3829  275 VRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDW 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 366 PGNVRELQNTAER-FALGLG-------LGLERPGSEPSAGLAGGGSLGEQVEAFERALIAAELNRPHGSLRSVAEALGLP 437
Cdd:COG3829  355 PGNVRELENVIERaVVLSEGdvitpehLPEYLLEEAEAASAAEEGSLKEALEEVEKELIEEALEKTGGNKSKAAKALGIS 434

                        330
                 ....*....|....
gi 520869243 438 RKTLHDKLRKHGLS 451
Cdd:COG3829  435 RSTLYRKLKKYGIK 448
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
9-450 2.92e-125

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 372.26  E-value: 2.92e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   9 TQAQVVLI-DDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVIL 87
Cdd:PRK11361   2 TAINRILIvDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLALADRQQlSARLLGQSRAMLRLREQIG 167
Cdd:PRK11361  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQ-WGHILTNSPAMMDICKDTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 168 ALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGT 247
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 248 LFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERS 327
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 328 EDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAER----------FALGLGLGL---ERPGSEP 394
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERavvmnsgpiiFSEDLPPQIrqpVCNAGEV 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 520869243 395 SAGLAGGGSLGEQVEAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHGL 450
Cdd:PRK11361 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
 13-446 1.90e-124

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


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 370.22  E-value: 1.90e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQlvlDNRSLRLAlADRQQLSARLLGQSRAMLRLREQIGALAGT 172
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQ---EQVALPAD-AGEAEDSAELIGEAPAMQEVFRAIGRLSRS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  173 QADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTLFLDE 252
Cdd:TIGR01818 157 DITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  253 IESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDILL 332
Cdd:TIGR01818 237 IGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  333 LFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAERFAL--------------GLGLGlERPGSEPSAGL 398
Cdd:TIGR01818 317 LARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVmasgdevlvsdlpaELALT-GRPASAPDSDG 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520869243  399 AGGGSLG------------------EQVEAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLR 446
Cdd:TIGR01818 396 QDSWDEAleawakqalsrgeqglldRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLK 461
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 13-451 7.62e-115

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: 345.19  E-value: 7.62e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   13 VVLIDDDPHLRQALSQTLDlaGLEVASLGDARDLAARLPAEWQGVIVSDIRMP-----GIDGLELLQQLRARDSELPVIL 87
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLALaDRQQLSArLLGQSRAMLRLREQIG 167
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSAL-GGTALRG-LITSSPGMQKICRTIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  168 ALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGT 247
Cdd:TIGR02915 157 KIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  248 LFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERS 327
Cdd:TIGR02915 237 LFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  328 EDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAERFAL--------GLGLGLERPGSEPSAGLA 399
Cdd:TIGR02915 317 GDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVImaegnqitAEDLGLDARERAETPLEV 396

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 520869243  400 GGGSLGEQVeafERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHGLS 451
Cdd:TIGR02915 397 NLREVRERA---EREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGIK 445
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
7-447 6.20e-104

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 316.97  E-value: 6.20e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   7 ISTQAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVI 86
Cdd:PRK10365   2 THDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  87 LITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVldnrSLRLALADRQQLSarLLGQSRAMLRLREQI 166
Cdd:PRK10365  82 IMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSI----DAETPAVTASQFG--MVGKSPAMQHLLSEI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 167 GALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGG 246
Cdd:PRK10365 156 ALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 247 TLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRER 326
Cdd:PRK10365 236 TLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQR 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 327 SEDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAERfALGLGLG---LERPGSEPSAGLAGGGS 403
Cdd:PRK10365 316 REDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVER-AVVLLTGeyiSERELPLAIASTPIPLG 394

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 520869243 404 LGEQVEAF---ERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRK 447
Cdd:PRK10365 395 QSQDIQPLvevEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
121-442 1.89e-101

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 312.88  E-value: 1.89e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 121 SVRRALALRQLVLDN-RSLRLALADRQQLSAR--LLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLS 197
Cdd:PRK05022 155 TLRNALLIEQLESQAeLPQDVAEFLRQEALKEgeMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAAS 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 198 SRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLG 277
Cdd:PRK05022 235 PRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVG 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 278 GNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRHGLPVRELQPGQR 357
Cdd:PRK05022 315 SDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQ 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 358 AMLLQHTWPGNVRELQNT--------------------AERFALGLGLGLERPGSEPSAGLAGGGSLGEQVEAFERALIA 417
Cdd:PRK05022 395 AALLAYDWPGNVRELEHVisraallarargagrivtleAQHLDLPAEVALPPPEAAAAPAAVVSQNLREATEAFQRQLIR 474

                        330       340
                 ....*....|....*....|....*
gi 520869243 418 AELNRPHGSLRSVAEALGLPRKTLH 442
Cdd:PRK05022 475 QALAQHQGNWAAAARALELDRANLH 499
PRK15115 PRK15115
response regulator GlrR; Provisional
 11-378 2.06e-100

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 307.92  E-value: 2.06e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:PRK15115   6 AHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSlrlaladRQQLSARllgqSRAMLRLREQIGALA 170
Cdd:PRK15115  86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDERW-------REAIVTR----SPLMLRLLEQARMVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 171 GTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTLFL 250
Cdd:PRK15115 155 QSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 251 DEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDI 330
Cdd:PRK15115 235 DEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDI 314

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 520869243 331 LLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAER 378
Cdd:PRK15115 315 PLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQ 362
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 10-375 3.14e-100

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 308.34  E-value: 3.14e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  10 QAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILIT 89
Cdd:PRK10923   3 RGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLAladrqQLSARLLGQSRAMLRLREQIGAL 169
Cdd:PRK10923  83 AHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVN-----GPTTDIIGEAPAMQDVFRIIGRL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 170 AGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTLF 249
Cdd:PRK10923 158 SRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLF 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 250 LDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSED 329
Cdd:PRK10923 238 LDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERRED 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 520869243 330 ILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNT 375
Cdd:PRK10923 318 IPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENT 363
Sigma54_activat pfam00158
Sigma-54 interaction domain;
152-319 7.25e-100

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 296.62  E-value: 7.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  152 LLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTG 231
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  232 AQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYY 311
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160


                  ....*...
gi 520869243  312 RLNVAPLR 319
Cdd:pfam00158 161 RLNVIPIE 168
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
123-449 1.43e-96

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 303.75  E-value: 1.43e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 123 RRALALRQLVLDNRSLRLALADRQQLSA--RLLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRR 200
Cdd:COG3284  292 RRLGALLRLRPARRAARAAPAGAPAPAAlaALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRA 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 201 NGPFVAINAGALAESVVESELFGHEPGAFTGAQKR-RIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGN 279
Cdd:COG3284  372 DGPFVAVNCAAIPEELIESELFGYEPGAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGT 451

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 280 QSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERsEDILLLFQHFAEAAAQRHGLPvrELQPGQRAM 359
Cdd:COG3284  452 KPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRER-EDLPALIEHLLRELAAGRGPL--RLSPEALAL 528

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 360 LLQHTWPGNVRELQNTAER-FALGLGLGLERP------GSEPSAGLAGGGSLGEQVEAFERALIAAELNRPHGSLRSVAE 432
Cdd:COG3284  529 LAAYPWPGNVRELRNVLRTaLALADGGVITVEdlpdelRAELAAAAPAAAAPLTSLEEAERDAILRALRACGGNVSAAAR 608

                        330
                 ....*....|....*..
gi 520869243 433 ALGLPRKTLHDKLRKHG 449
Cdd:COG3284  609 ALGISRSTLYRKLKRYG 625
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
 151-451 7.56e-87

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 275.14  E-value: 7.56e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 151 RLLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFT 230
Cdd:COG3283  205 HIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFG 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 231 GAQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLY 310
Cdd:COG3283  285 NAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLY 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 311 YRLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAERfALGLGLG---- 386
Cdd:COG3283  365 YRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYR-AVSLLEGdelt 443

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520869243 387 ---LERPGSEPSAGLAGGGSL---GEQVEAFERALIaAELNRPHGSLRSVAEALGLPRKTLHDKLRKHGLS 451
Cdd:COG3283  444 pedLQLPEYAASAGLLDDLLEgslDEIVKRFERSLL-RRLYPSYPSTRKLAKRLGVSHTAIANKLREYGIG 513
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
 122-380 2.13e-85

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: 271.97  E-value: 2.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  122 VRRALALRQLVLDNRSLRLALADRQQLSAR----------------LLGQSRAMLRLREQIGALAGTQADVLILGETGAG 185
Cdd:TIGR01817 152 IGQTVRLHRLVAQRRERLIAEAVQLSKQLRdkapeiarrrsgkedgIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTG 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  186 KEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLL 265
Cdd:TIGR01817 232 KELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLL 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  266 RLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRH 345
Cdd:TIGR01817 312 RVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNREN 391

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 520869243  346 GLPVReLQPGQRAMLLQHTWPGNVRELQNTAERFA 380
Cdd:TIGR01817 392 GRPLT-ITPSAIRVLMSCKWPGNVRELENCLERTA 425
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
 120-450 1.48e-82

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 264.66  E-value: 1.48e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 120 DSVRR----ALALRQLVLDNR---SLRLALADRQQLSArLLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARA 192
Cdd:PRK15424 183 ATVRQafedALDMTRMTLRHNthyATRNALRTRYVLGD-LLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQA 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 193 LH--------DLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKR-RIGKFEFANGGTLFLDEIESMSLDLQVK 263
Cdd:PRK15424 262 IHreyfarhdARQGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGgRAGLFEIAHGGTLFLDEIGEMPLPLQTR 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 264 LLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDILLLFQHFAEAAAQ 343
Cdd:PRK15424 342 LLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLA 421

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 344 RHGLPV-----RELQPGQRAMLLQHtWPGNVRELQNTAERFALGLGLGLERPGSEPSAGLAGGGSLGEQVEA----FERA 414
Cdd:PRK15424 422 ALSAPFsaalrQGLQQCETLLLHYD-WPGNVRELRNLMERLALFLSVEPTPDLTPQFLQLLLPELARESAKTpaprLLAA 500

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 520869243 415 LIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHGL 450
Cdd:PRK15424 501 TLQQALERFNGDKTAAANYLGISRTTLWRRLKAEAK 536
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
 120-447 5.47e-82

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


Pssm-ID: 274079 [Multi-domain]  Cd Length: 526  Bit Score: 262.87  E-value: 5.47e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  120 DSVRRA----LALRQLVLDNRSLRLALADRQQLSAR-----LLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVA 190
Cdd:TIGR02329 173 DSVRQAfddaLDVARATRLRQAATLRSATRNQLRTRyrlddLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVA 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  191 RALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTGAQKR-RIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQ 269
Cdd:TIGR02329 253 QAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTGARRGgRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLE 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  270 ERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRHGLP- 348
Cdd:TIGR02329 333 EREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPd 412

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  349 ----VRELQPGQRAmLLQHTWPGNVRELQNTAERFALGLG------------LGLERPGSEPSAGLAGGGSLGEQVEAFE 412
Cdd:TIGR02329 413 seaaAQVLAGVADP-LQRYPWPGNVRELRNLVERLALELSampagaltpdvlRALAPELAEASGKGKTSALSLRERSRVE 491

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 520869243  413 RALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRK 447
Cdd:TIGR02329 492 ALAVRAALERFGGDRDAAAKALGISRTTLWRRLKA 526
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
 152-450 6.30e-78

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 246.12  E-value: 6.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 152 LLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTG 231
Cdd:PRK11608   8 LLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 232 AQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYY 311
Cdd:PRK11608  88 AQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 312 RLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRHGLPvreLQPG----QRAMLLQHTWPGNVRELQNTAER--------- 378
Cdd:PRK11608 168 RLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLP---LFPGfterARETLLNYRWPGNIRELKNVVERsvyrhgtse 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 379 -------------FALGLGLGLERPGSEPSAGLAGGGSLGEQveafERALIAAELNRPHGSLRSVAEALGLPRKTLHDKL 445
Cdd:PRK11608 245 ypldniiidpfkrRPAEEAIAVSETTSLPTLPLDLREWQHQQ----EKELLQRSLQQAKFNQKRAAELLGLTYHQLRALL 320


                 ....*
gi 520869243 446 RKHGL 450
Cdd:PRK11608 321 KKHQI 325
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
130-450 1.46e-74

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 247.44  E-value: 1.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 130 QLVLDNRSLRLALADRQQLSARLLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINA 209
Cdd:PRK15429 356 RLVDENLALTEQLNNVDSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNC 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 210 GALAESVVESELFGHEPGAFTGAQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVI 289
Cdd:PRK15429 436 AAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLI 515

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 290 AATKEDLRVAADQGRFRADLYYRLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNV 369
Cdd:PRK15429 516 AATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNV 595

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 370 RELQNTAERFAL---GLGLGLERPGSEPSAGLAGGGSLGEQVEAF-ERALIAAELNRPHGSL---RSVAEALGLPRKTLH 442
Cdd:PRK15429 596 RELENVIERAVLltrGNVLQLSLPDITLPEPETPPAATVVAQEGEdEYQLIVRVLKETNGVVagpKGAAQRLGLKRTTLL 675


                 ....*...
gi 520869243 443 DKLRKHGL 450
Cdd:PRK15429 676 SRMKRLGI 683
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 13-142 1.91e-70

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 219.67  E-value: 1.91e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLAL 142
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
 160-451 2.57e-66

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


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 216.25  E-value: 2.57e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 160 LRLREQIGALAGtqadVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESelfghepgaftgaqkrrigk 239
Cdd:COG3604  106 LRLLETLASLAA----VAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 240 fefanggtlfldeiesmsldlqvkllrlLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVAPLR 319
Cdd:COG3604  162 ----------------------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIR 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 320 IPSLRERSEDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAERFALglglgleRPGSEPSAGLA 399
Cdd:COG3604  214 LPPLRERREDIPLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVI-------LAEGGVLDADD 286

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 520869243 400 GGGSLGEQVEAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHGLS 451
Cdd:COG3604  287 LAPGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
PRK10820 PRK10820
transcriptional regulator TyrR;
152-451 2.74e-66

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 221.48  E-value: 2.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 152 LLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPGAFTG 231
Cdd:PRK10820 206 IVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPN 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 232 AQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYY 311
Cdd:PRK10820 286 ALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYY 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 312 RLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRHGLPVRELQPGQRAMLLQHTWPGNVRELQNTAERfALGLGLGLE-RP 390
Cdd:PRK10820 366 RLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYR-ALTQLEGYElRP 444

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 391 GSEPSAGLAGGGSLGEQV---------EAFERAlIAAELNRPHGSLRSVAEALGLPRKTLHDKLRKHGLS 451
Cdd:PRK10820 445 QDILLPDYDAAVAVGEDAmegsldeitSRFERS-VLTRLYRNYPSTRKLAKRLGVSHTAIANKLREYGLS 513
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
 152-450 7.86e-53

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 187.96  E-value: 7.86e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 152 LLGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEPgafTG 231
Cdd:PRK11388 327 MPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLGSDR---TD 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 232 AQKRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYY 311
Cdd:PRK11388 404 SENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYY 483

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 312 RLNVAPLRIPSLRERSEDILLLFQHFAEAAAQRHGlpvRELQPGQRAM--LLQHTWPGNVRELQNTAERFALGLGLGLER 389
Cdd:PRK11388 484 ALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFS---TRLKIDDDALarLVSYRWPGNDFELRSVIENLALSSDNGRIR 560

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 390 PGSEPSAGLAGGGSLGEQVEAFERALIAAELNRP---------HGSLRSVAEALGLPRKTLHDKLRKHGL 450
Cdd:PRK11388 561 LSDLPEHLFTEQATDDVSATRLSTSLSLAELEKEaiinaaqvcGGRIQEMAALLGIGRTTLWRKMKQHGI 630
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 13-151 2.78e-47

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: 161.81  E-value: 2.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLALADR-QQLSAR 151
Cdd:COG4566   82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRARlASLTPR 141
fixJ PRK09390
response regulator FixJ; Provisional
 8-151 1.46e-41

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 147.07  E-value: 1.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   8 STQAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVIL 87
Cdd:PRK09390   1 SDKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLALADR-QQLSAR 151
Cdd:PRK09390  81 MTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEAAKSEAVAADIRARiASLSER 145
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 11-126 1.41e-40

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: 141.19  E-value: 1.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:cd17537    1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITG 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17537   81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
 161-372 1.37e-37

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: 144.20  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 161 RLREQIGALAG-TQADVLILGETGAGKEVVARALHDLSSRRN---GPFVAINAGALAESVVESELFGHEPGAFTGAQKRR 236
Cdd:COG4650  195 RLIEQIERVAIrSRAPILLTGPTGAGKSQLARRIYELKKARHqvsGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDR 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 237 IGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNQSIALDIRVIAATKEDLRVAADQGRFRADLYYRLNVA 316
Cdd:COG4650  275 AGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLW 354

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520869243 317 PLRIPSLRERSEDILLLFQHFAEAAAQRHGLPVRELQPGQRAML-----LQHTWPGNVREL 372
Cdd:COG4650  355 TFRLPGLAERREDIEPNLDYELARFAREQGRRVRFNKEARARYLafatsPEALWSGNFRDL 415
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 13-123 1.73e-35

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: 127.65  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 520869243   93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 12-126 1.92e-31

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: 116.99  E-value: 1.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd19919   82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 13-127 6.83e-31

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: 115.29  E-value: 6.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALA 127
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 13-127 5.12e-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: 107.42  E-value: 5.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARD------LAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSELPVI 86
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGFEVVGEAENgeealeLIEEHKPD---IVITDIRMPGMDGLELIEKIRELYPDIKII 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 520869243  87 LITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALA 127
Cdd:cd17536   78 ILSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 8-143 7.40e-28

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: 110.64  E-value: 7.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   8 STQAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDS--ELPV 85
Cdd:COG3437    4 GQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrDIPV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 520869243  86 ILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLALA 143
Cdd:COG3437   84 IFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLK 141
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 15-112 1.08e-27

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 106.16  E-value: 1.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  15 LIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHGDI 94
Cdd:cd00156    2 IVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKADE 81

                         90
                 ....*....|....*...
gi 520869243  95 QLAVQAMRAGAYDFLEKP 112
Cdd:cd00156   82 EDAVRALELGADDYLVKP 99
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 10-130 1.81e-26

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: 106.19  E-value: 1.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  10 QAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILIT 89
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQ 130
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRA 121
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 13-131 1.57e-25

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: 100.74  E-value: 1.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQL 131
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKL 119
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 11-125 1.83e-25

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: 100.35  E-value: 1.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPS-EALLDSVRRA 125
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKPIEDlAVLEHAVRRA 116
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 13-112 2.29e-25

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: 99.85  E-value: 2.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLD-LAGLEV----ASLGDARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSELPVIL 87
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEwEAGFEVvgeaENGEEALELLEEHKPD---LVITDINMPGMDGLELLEAIRELDPDTKIII 78

                         90       100
                 ....*....|....*....|....*
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:COG4753   79 LSGYSDFEYAQEAIKLGADDYLLKP 103
tetrathio_RR NF040749
tetrathionate respiration response regulator TtrR;
15-155 3.40e-25

tetrathionate respiration response regulator TtrR;


Pssm-ID: 468713 [Multi-domain]  Cd Length: 191  Bit Score: 102.05  E-value: 3.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  15 LIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHGDI 94
Cdd:NF040749   4 LVDDDVAVTDACRFLLESLGYEVQCWNDSEAFLAQADLYQEGVVLLDMRMPGLDGHQVHQALREQGSTLAVVFLTGHGDV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520869243  95 QLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRL---ALADRQQLSARLLGQ 155
Cdd:NF040749  84 PMAVEQMKLGAVDFLQKPVSAAPLQAALERALAVSAAAFERHQIRQryqSLTPKEREIAGLVVQ 147
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 13-140 4.00e-25

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 100.43  E-value: 4.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLD-LAGLEV----ASLGDARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSELPVIL 87
Cdd:COG4565    6 VLIVEDDPMVAELLRRYLErLPGFEVvgvaSSGEEALALLAEHRPD---LILLDIYLPDGDGLELLRELRARGPDVDVIV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRL 140
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDL 135
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 13-130 4.61e-25

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 99.92  E-value: 4.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARD--SELPVILITG 90
Cdd:COG0784    8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPrlPDIPIIALTA 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQ 130
Cdd:COG0784   88 YADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 10-122 1.03e-23

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 97.67  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  10 QAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARD----LAARLPAewqgVIVSDIRMPGIDGLELLQQLRA--RDSEL 83
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEalelLQEHRPD----LILLDLEMPDMDGLELCRRLRAdpRTADI 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 520869243  84 PVILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSV 122
Cdd:COG3706   77 PIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 13-127 1.59e-22

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: 94.21  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEV---ASLGDARDLAARLPAEWqgvIVSDIRMPGIDGLELLQQLRARDSELPVILIT 89
Cdd:COG4567    7 LLLVDDDEAFARVLARALERRGFEVttaASVEEALALLEQAPPDY---AVLDLRLGDGSGLDLIEALRERDPDARIVVLT 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALA 127
Cdd:COG4567   84 GYASIATAVEAIKLGADDYLAKPADADDLLAALERAEG 121
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 13-127 5.24e-22

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: 91.03  E-value: 5.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLA-GLE-VASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALA 127
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 13-131 2.82e-21

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 92.19  E-value: 2.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTL-DLAGLE-VASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:COG3279    4 ILIVDDEPLARERLERLLeKYPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 520869243  91 HgdIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQL 131
Cdd:COG3279   84 Y--DEYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEA 122
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 154-314 8.04e-21

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 88.74  E-value: 8.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 154 GQSRAMLRLREqiGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVESELFGHEpgaftgAQ 233
Cdd:cd00009    2 GQEEAIEALRE--ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 234 KRRIGKFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLGGNqsialDIRVIAATKEDlrvaaDQGRFRADLYYRL 313
Cdd:cd00009   74 RLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRP-----LLGDLDRALYDRL 143


                 .
gi 520869243 314 N 314
Cdd:cd00009  144 D 144
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 13-127 4.44e-20

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: 85.53  E-value: 4.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17569    3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGYA 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520869243  93 DIQLAVQAMRAGA-YDFLEKPFPSEALLDSVRRALA 127
Cdd:cd17569   83 DLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
153-323 6.97e-20

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 85.47  E-value: 6.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  153 LGQSRAMLRLREQIGALAGTQADVLILGETGAGKEVVARALHDLSSRRNGPFVAINagalaesvveselFGHEPGAFtga 232
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEY-------------LAHAPLEL--- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  233 qkrrigkFEFANGGTLFLDEIESMSLDLQVKLLRLLQERVVERLggnqsialdiRVIAATKEDLRVAADQGRFRADLYYR 312
Cdd:pfam14532  65 -------LEQAKGGTLYLKDIADLSKALQKGLLLLLAKAEGYRV----------RLVCTSSKDLPQLAAAGLFDEQLYFE 127

                         170
                  ....*....|.
gi 520869243  313 LNVAPLRIPSL 323
Cdd:pfam14532 128 LSALRLHVPPL 138
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 176-374 8.68e-20

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: 92.48  E-value: 8.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 176 VLILGETGAGKEVVARALHD--LSSRR---NGPFVAINAGALAES--VVESELFGHEPGAFTGAQKRRIGKFEFANGGTL 248
Cdd:COG1221  133 TLILGPTGVGKSFFAELMYEyaIEIGVlpeDAPFVVFNCADYANNpqLLMSQLFGYVKGAFTGADKDKEGLIEKADGGIL 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243 249 FLDEIESMSLDLQVKLLRLLQERVVERLG-GNQSIALDIRVIAATKED---------LRvaadqgrfradlyyrlnvapl 318
Cdd:COG1221  213 FLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDpessllktfLR--------------------- 271

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520869243 319 RI------PSLRERSED-----ILLLFQHfaEaaAQRHGLPVReLQPgqRAM--LLQHTWPGNVRELQN 374
Cdd:COG1221  272 RIpmviklPSLEERSLEerlelIKHFFKE--E--AKRLNKPIK-VSK--EVLkaLLLYDCPGNIGQLKS 333
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 11-119 9.60e-20

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: 84.42  E-value: 9.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTL-DLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRAR--DSELPVIL 87
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLrSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIVM 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPF-PSEALL 119
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPFdPVELLA 113
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 15-112 1.54e-19

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: 83.23  E-value: 1.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  15 LIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHGDI 94
Cdd:cd17574    2 VVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDEE 81

                         90
                 ....*....|....*...
gi 520869243  95 QLAVQAMRAGAYDFLEKP 112
Cdd:cd17574   82 EDKVLGLELGADDYITKP 99
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
 13-142 4.24e-19

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: 83.18  E-value: 4.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDlAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520869243  93 DIQLAVQAMR-AGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLAL 142
Cdd:cd17596   82 DSEDIIAGINeAGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERLSLEL 132
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 13-146 2.17e-17

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: 80.00  E-value: 2.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEV-ASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLrARDSELPVILITGH 91
Cdd:COG3707    6 VLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQI-SEERPAPVILLTAY 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALA----LRQLVLDNRSLRLALADRQ 146
Cdd:COG3707   85 SDPELIERALEAGVSAYLVKPLDPEDLLPALELALArfreLRALRRELAKLREALEERK 143
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 15-112 3.74e-17

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: 77.10  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  15 LIDDDPHLRQALSQTLDLAGLEV---ASLGDARDLAARLPAEWqgvIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:cd17563    5 LVDDDEVFAERLARALERRGFEVetaHSVEEALALAREEKPDY---AVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81

                         90       100
                 ....*....|....*....|.
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd17563   82 ASIATAVEAIKLGADDYLAKP 102
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 11-125 4.38e-17

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: 76.88  E-value: 4.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520869243  91 HGDIQLAVQAMRAGAYdfLEKPFPSEALLDSVRRA 125
Cdd:cd17554   81 YSEYKSDFSSWAADAY--VVKSSDLTELKETIKRL 113
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 13-126 4.60e-17

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: 76.96  E-value: 4.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDS--ELPVILITG 90
Cdd:cd17562    3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAykFTPILMLTT 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17562   83 ESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 13-112 4.72e-17

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: 76.26  E-value: 4.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEV--ASLGD-ARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLR--ARDSELPVIL 87
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTViaASNGLeALDLLNQYIPD---LIISDIIMPGVDGYSLLGKLRknADFDTIPVIF 77

                         90       100
                 ....*....|....*....|....*
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd19927   78 LTAKGMTSDRIKGYNAGCDGYLSKP 102
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
 13-112 7.49e-17

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: 75.65  E-value: 7.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80

                         90       100
                 ....*....|....*....|
gi 520869243  93 DIQLAVQAMRAGAYDFLEKP 112
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 15-123 1.37e-16

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 75.72  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  15 LIDDDPHLRQALSQTLDLAGLEVASLGDARD-LAARLPAEWQgVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHGD 93
Cdd:cd17625    2 VVEDEKDLSEAITKHLKKEGYTVDVCFDGEEgLEYALSGIYD-LIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 520869243  94 IQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELLARIR 110
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 12-126 1.75e-16

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: 75.39  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVAslGDARDL--AARLPAEWQGVIVS-DIRMPGIDGLELLQQLRARDSELPVILI 88
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAGYEVV--GEAANGeeAVEKYKELKPDLVTmDITMPEMDGIEALKEIKKIDPNAKVIMC 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17542   80 SAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 13-122 2.09e-16

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: 74.80  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARD--SELPVILITG 90
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPwlANTPAIALTG 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSV 122
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 13-123 2.52e-16

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: 74.83  E-value: 2.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEELLARLR 111
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 13-126 5.16e-16

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: 73.96  E-value: 5.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 13-113 1.45e-15

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 72.16  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRA--RDSELPVILITG 90
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKAdpATRHIPVIFLTA 80

                         90       100
                 ....*....|....*....|...
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPF 113
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 13-123 1.49e-15

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 72.77  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 14-126 1.50e-15

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: 72.81  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  14 VLI-DDDPHLRQALSQTL-DLAGLEV---ASLG-DARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARdSELPVIL 87
Cdd:cd17541    3 VLIvDDSAVMRKLLSRILeSDPDIEVvgtARDGeEALEKIKELKPD---VITLDIEMPVMDGLEALRRIMAE-RPTPVVM 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 520869243  88 ITGH--GDIQLAVQAMRAGAYDFLEKPF-PSEALLDSVRRAL 126
Cdd:cd17541   79 VSSLteEGAEITLEALELGAVDFIAKPSgGISLDLEEIAEEL 120
orf27 CHL00148
Ycf27; Reviewed
 5-116 5.56e-15

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 74.37  E-value: 5.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   5 TPISTQAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRaRDSELP 84
Cdd:CHL00148   1 TMENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR-KESDVP 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520869243  85 VILITGHGDIQLAVQAMRAGAYDFLEKPF-PSE 116
Cdd:CHL00148  80 IIMLTALGDVSDRITGLELGADDYVVKPFsPKE 112
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
 13-123 5.61e-15

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 71.16  E-value: 5.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 13-118 6.21e-15

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: 70.73  E-value: 6.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQG--VIVSDIRMPGIDGLELLQQLRArDSELPVILITG 90
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEfdLVITDVHMPDMDGFEFLELIRL-EMDLPVIMMSA 79

                         90       100
                 ....*....|....*....|....*...
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEAL 118
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 13-118 1.39e-14

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: 70.06  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTL-DLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARD--SELPVILIT 89
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLkELGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGalSHLPVLMVT 82

                         90       100
                 ....*....|....*....|....*....
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKPFPSEAL 118
Cdd:cd19923   83 AEAKKENVIAAAQAGVNNYIVKPFTAATL 111
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 13-123 1.44e-14

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: 69.78  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGHG 92
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR-SDVPIIIISGDR 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 520869243  93 DIQLA-VQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd17594   81 RDEIDrVVGLELGADDYLAKPFGLRELLARVR 112
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 11-123 1.62e-14

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 69.59  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLR--ARDSELPVILI 88
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKrdEMTRDIPIIML 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 13-112 3.19e-14

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 68.30  E-value: 3.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAaRLPAEWQG-VIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLW-RWVEEGEGdLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQ 79

                         90       100
                 ....*....|....*....|.
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd19928   80 NTLMTAVKAAERGAFEYLPKP 100
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 13-126 3.27e-14

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: 68.87  E-value: 3.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGHG 92
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT-SQVPVLMLTARG 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFNPRELVARIRAIL 113
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 13-112 5.05e-14

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 67.85  E-value: 5.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAG--LEVASLG-DARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSELPVILIT 89
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGyaVDVAYDGeDGLHLALTNEYD---LIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLT 77

                         90       100
                 ....*....|....*....|...
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd19935   78 ARDSVEDRVKGLDLGADDYLVKP 100
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 14-113 6.55e-14

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 67.52  E-value: 6.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  14 VLI-DDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDS--ELPVILITG 90
Cdd:cd17538    2 ILVvDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPEtrHIPVIMITA 81

                         90       100
                 ....*....|....*....|...
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPF 113
Cdd:cd17538   82 LDDREDRIRGLEAGADDFLSKPI 104
PRK10360 PRK10360
transcriptional regulator UhpA;
13-167 1.43e-13

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 69.24  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLdlaGLE-----VASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLrarDSELPVIL 87
Cdd:PRK10360   4 VALIDDHLIVRSGFAQLL---GLEpdlqvVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQL---PKGMATIM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLA------LADRQQLSARLLGQSRAMLR 161
Cdd:PRK10360  78 LSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTVATGGCYLTPDIAIKLAsgrqdpLTKRERQVAEKLAQGMAVKE 157


                 ....*.
gi 520869243 162 LREQIG 167
Cdd:PRK10360 158 IAAELG 163
PRK15479 PRK15479
transcriptional regulator TctD;
12-129 1.64e-13

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 69.75  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTAR 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPFPSEAlLDSVRRALALR 129
Cdd:PRK15479  82 SAVADRVKGLNVGADDYLPKPFELEE-LDARLRALLRR 118
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 11-123 3.24e-13

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 65.87  E-value: 3.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITG 90
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ-SEVGIILVTG 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 13-127 3.70e-13

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: 65.76  E-value: 3.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAG-LE-VASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDdLEvVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALA 127
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 13-113 7.23e-13

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: 64.45  E-value: 7.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQ-GVIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81

                         90       100
                 ....*....|....*....|..
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPF 113
Cdd:cd18160   82 AAAAPELLSDAVGDNATLKKPF 103
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 16-126 7.92e-13

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: 64.99  E-value: 7.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  16 IDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLR--ARDSELPVILITGHGD 93
Cdd:cd19937    3 VDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRsdPKTSSIPIIMLTAKGE 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520869243  94 IQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd19937   83 EFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 13-126 8.94e-13

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 64.65  E-value: 8.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDS--ELPVILITG 90
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDlkDIPVILLTT 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 14-122 1.08e-12

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: 64.41  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  14 VLI-DDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSE---LPVILIT 89
Cdd:cd17546    1 VLVvDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGgrrTPIIALT 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSV 122
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
ompR PRK09468
osmolarity response regulator; Provisional
 13-126 1.36e-12

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 67.31  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:PRK09468   8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAKG 87

                         90       100       110
                 ....*....|....*....|....*....|....
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:PRK09468  88 EEVDRIVGLEIGADDYLPKPFNPRELLARIRAVL 121
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 13-112 1.44e-12

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: 63.62  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARD----LAARLPaewqGVIVSDIRMPGIDGLELLQQLRARdSELPVILI 88
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASaldgLNARPP----DLAILDIKMPRMDGMELLQRLRQK-STLPVIFL 75

                         90       100
                 ....*....|....*....|....
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd19936   76 TSKDDEIDEVFGLRMGADDYITKP 99
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 13-116 3.58e-12

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 63.31  E-value: 3.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQ-GVIVSDIRMPGIDGLELLQQLRARDS--ELPVILIT 89
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDiKLVITDYNMPEMDGFELVREIRKKYSrdQLAIIGIS 82

                         90       100
                 ....*....|....*....|....*..
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKPFPSE 116
Cdd:cd17544   83 ASGDNALSARFIKAGANDFLTKPFLPE 109
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 13-126 8.47e-12

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 62.01  E-value: 8.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGHG 92
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH-SHVPILMLTART 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd19939   81 EEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
PRK11517 PRK11517
DNA-binding response regulator HprR;
12-141 1.41e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 64.15  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGH 91
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTA-KQTPVICLTAR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRalALRQLVLDNRSLRLA 141
Cdd:PRK11517  81 DSVDDRVRGLDSGANDYLVKPFSFSELLARVRA--QLRQHHALNSTLEIS 128
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 12-127 1.97e-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: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVasLGDARD------LAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSeLPV 85
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEV--VGEASDgeeaveLAKKHKPD---LVIMDVKMPRLDGIEAAKIITSENI-API 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 520869243  86 ILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALA 127
Cdd:cd19932   76 VLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIA 117
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 13-112 2.39e-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: 60.47  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARD---------LAARLPAEWQGVIVSDIRMPGIDGLELLQQLRA--RDS 81
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEalnklenlaKEGNDLSKELDLIITDIEMPKMDGYELTFELRDdpRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 520869243  82 ELPVILITGHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
 1-193 2.62e-11

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 63.12  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   1 MSSDTPistqAQVVLIDDDPHLRQALSQTLDLA-GLEV----ASLGDARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQ 75
Cdd:PRK10651   1 MSNQEP----ATILLIDDHPMLRTGVKQLISMApDITVvgeaSNGEQGIELAESLDPD---LILLDLNMPGMNGLETLDK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  76 LRARDSELPVILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNRSLRLALADRQQLSArllgQ 155
Cdd:PRK10651  74 LREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGEMVLSEALTPVLAASLRANRAT----T 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 520869243 156 SRAMLRLREQigalagtQADVLILGETGAGKEVVARAL 193
Cdd:PRK10651 150 ERDVNQLTPR-------ERDILKLIAQGLPNKMIARRL 180
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 13-112 2.80e-11

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: 59.87  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDA----RDLAARLPaewqGVIVSDIRMPGIDGLELLQQLRARdSELPVILI 88
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGqeglLEAATRKP----DLIILDLGLPDMDGLEVIRRLREW-SAVPVIVL 75

                         90       100
                 ....*....|....*....|....
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd17620   76 SARDEESDKIAALDAGADDYLTKP 99
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 12-126 3.21e-11

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: 60.26  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTL-DLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDS--ELPVILI 88
Cdd:cd17552    3 RILVIDDEEDIREVVQACLeKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPEtqSIPVILL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 520869243  89 TGHG---DIQLAVQAMRAGAydfLEKPFPSEALLDSVRRAL 126
Cdd:cd17552   83 TAKAqpsDRQRFASLGVAGV---IAKPFDPLTLAEQIAKLL 120
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 11-126 3.80e-11

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 60.18  E-value: 3.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRArDSELPVILITG 90
Cdd:cd17626    1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLTA 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17626   80 KSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
 13-123 3.91e-11

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 60.12  E-value: 3.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEV--ASLG-DARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSELPVILIT 89
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVytTDLGeEGLDLGKLYDYD---IILLDLNLPDMSGYEVLRTLRLAKVKTPILILS 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd17616   78 GLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 13-124 5.42e-11

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 59.57  E-value: 5.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLD-LAGLEV----ASLGDARDLAARLPAewqGVIVSDIRMPGIDGLELLQQLRARDSELPVIL 87
Cdd:cd19925    3 VLIVEDDPMVAEIHRAYVEqVPGFTVigtaGTGEEALKLLKERQP---DLILLDIYLPDGNGLDLLRELRAAGHDVDVIV 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRR 124
Cdd:cd19925   80 VTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 13-130 6.25e-11

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 59.47  E-value: 6.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTL-DLAGLE-VASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:cd17532    1 ALIVDDEPLAREELRYLLeEHPDIEiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 520869243  91 HGdiQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQ 130
Cdd:cd17532   81 YD--EYAVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 176-313 1.57e-10

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: 59.31  E-value: 1.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   176 VLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESVVES---ELFGHEPGAFTGAQKRRIGkFEFA---NGGTLF 249
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLA-LALArklKPDVLI 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520869243   250 LDEIESMSLDLQVKLLRLLQErvvERLGGNQSIALDIRVIAAT--KEDLRVAADQGRFRADLYYRL 313
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTndEKDLGPALLRRRFDRRIVLLL 146
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 13-127 1.58e-10

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 58.51  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGL-----EVASLGDARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSELPVIL 87
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDftvvgEASSGEEGIELAERLDPD---LILLDLNMKGMSGLDTLKALREEGVSARIVI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALA 127
Cdd:cd19931   78 LTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
PRK10643 PRK10643
two-component system response regulator PmrA;
12-146 1.86e-10

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 60.82  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVLDNR----SLRLALADRQ 146
Cdd:PRK10643  82 DTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQGQGENElqvgNLTLNLGRQQ 140
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 13-126 5.06e-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: 56.91  E-value: 5.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGHG 92
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI-SNVPIIFISSRD 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 14-120 5.58e-10

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 56.78  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  14 VLI-DDDPHLRQALSQTL-DLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITgh 91
Cdd:cd17593    3 VLIcDDSSMARKQLARALpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS-- 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 520869243  92 GDIQ-LAVQ-AMRAGAYDFLEKPFPSEALLD 120
Cdd:cd17593   81 GDVQpEAKErVLELGALAFLKKPFDPEKLAQ 111
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 13-112 6.58e-10

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: 56.22  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDA-RDLAARLPAEWQgVIVSDIRMPGIDGLELLQQLRARDS--ELPVILIT 89
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPlRALTTLLNSKPD-LILIDIDMPDLDGYELCSLLRKSSAlkDTPIIMLT 79

                         90       100
                 ....*....|....*....|...
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd17602   80 GKDGLVDRIRAKMAGASGYLTKP 102
PRK13856 PRK13856
two-component response regulator VirG; Provisional
 13-162 8.08e-10

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 59.06  E-value: 8.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGHG 92
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATK-SDVPIIIISGDR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520869243  93 -DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLVL---DNRSLRLA---LADRQQlsaRLLGQSRAMLRL 162
Cdd:PRK13856  83 lEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVVrtkDRRSFCFAdwtLNLRQR---RLISEAGGEVKL 156
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 12-126 2.03e-09

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: 55.25  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEV--ASLG-DARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSELPVILI 88
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTfqAANGlQALDIVTKERPD---LVLLDMKIPGMDGIEILKRMKVIDENIRVIIM 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17553   79 TAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
PRK10610 PRK10610
chemotaxis protein CheY;
14-118 2.70e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 55.37  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  14 VLIDDDPHLRQALSQTLDLAGLE-VASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARD--SELPVILITG 90
Cdd:PRK10610   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALPVLMVTA 88

                         90       100
                 ....*....|....*....|....*...
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEAL 118
Cdd:PRK10610  89 EAKKENIIAAAQAGASGYVVKPFTAATL 116
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
12-127 6.92e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 57.47  E-value: 6.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDL-AGLEV-ASLGD---ARDLAARLpaeWQGVIVSDIRMPGIDGLELLQQLRARdSELPVI 86
Cdd:PRK00742   5 RVLVVDDSAFMRRLISEILNSdPDIEVvGTAPDgleAREKIKKL---NPDVITLDVEMPVMDGLDALEKIMRL-RPTPVV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 520869243  87 LI---TGHG-DIQLavQAMRAGAYDFLEKPFPSEAL-LDSVRRALA 127
Cdd:PRK00742  81 MVsslTERGaEITL--RALELGAVDFVTKPFLGISLgMDEYKEELA 124
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 13-126 8.65e-09

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: 53.54  E-value: 8.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGHG 92
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLLTALD 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17622   82 SDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 13-124 1.03e-08

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 52.93  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARD--SELPVILITG 90
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPatRDIPVIALTA 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 520869243  91 H---GDIQlavQAMRAGAYDFLEKPFPSEALLDSVRR 124
Cdd:cd17548   82 YamkGDRE---KILEAGCDGYISKPIDTREFLETVAK 115
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
12-126 1.70e-08

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 55.11  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLR--ARDSELPVILIT 89
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKreSMTRDIPVVMLT 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 520869243  90 GHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:PRK10161  84 ARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 13-112 1.70e-08

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 52.20  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGHG 92
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR-SNVPVIMVTAKD 79

                         90       100
                 ....*....|....*....|
gi 520869243  93 DIQLAVQAMRAGAYDFLEKP 112
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 12-126 1.74e-08

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 52.38  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRaRDSELPVILITGH 91
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR-RFSDVPIIMVTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd19938   80 VEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
PRK10816 PRK10816
two-component system response regulator PhoP;
12-113 3.19e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 53.97  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81

                         90       100
                 ....*....|....*....|..
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPF 113
Cdd:PRK10816  82 ESWQDKVEVLSAGADDYVTKPF 103
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
12-126 3.68e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 54.04  E-value: 3.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQgVIVSDIRMPGIDGLELLQQLRaRDSELPVILITGH 91
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSID-LLLLDVMMPKKNGIDTLKELR-QTHQTPVIMLTAR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:PRK10955  81 GSELDRVLGLELGADDYLPKPFNDRELVARIRAIL 115
PRK10336 PRK10336
two-component system response regulator QseB;
12-128 4.81e-08

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 53.36  E-value: 4.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:PRK10336   2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTAR 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 520869243  92 GDIQLAVQAMRAGAYDFLEKPFpseALLDSVRRALAL 128
Cdd:PRK10336  82 DALAERVEGLRLGADDYLCKPF---ALIEVAARLEAL 115
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 12-124 5.28e-08

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: 51.26  E-value: 5.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPH----LRQALSQTLDLAGLEVASLGDA-----RDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRArDSE 82
Cdd:cd17557    1 TILLVEDNPGdaelIQEAFKEAGVPNELHVVRDGEEaldflRGEGEYADAPRPDLILLDLNMPRMDGFEVLREIKA-DPD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 520869243  83 L---PVILIT---GHGDIQlavQAMRAGAYDFLEKPFPSEALLDSVRR 124
Cdd:cd17557   80 LrriPVVVLTtsdAEEDIE---RAYELGANSYIVKPVDFEEFVEAIRS 124
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
3-153 6.09e-08

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 55.51  E-value: 6.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243    3 SDTPIS--TQAQVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARD 80
Cdd:PRK09959  949 AEQPITlpEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN 1028

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520869243   81 SELPVILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLV-----LDNRSLRLALADRQQLSARLL 153
Cdd:PRK09959 1029 SSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIApqyrhLDIEALKNNTANDLQLMQEIL 1106
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 12-126 8.01e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 53.00  E-value: 8.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLeVASLGD----ARDLAarLPAEWQGVIVsDIRMPGIDGLELLQQLRARDSELPVIL 87
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGF-VVDLADnglnGYHLA--MTGDYDLIIL-DIMLPDVNGWDIVRMLRSANKGMPILL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:PRK09836  78 LTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL 116
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 14-126 9.58e-08

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: 50.48  E-value: 9.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  14 VLI-DDDPHLRQALSQTLDLAGLEV----ASLGDARDLAARLPAEwqgVIVSDIRMPG-IDGLELLQQLRARdSELPVIL 87
Cdd:cd17534    3 ILIvEDEAIIALDLKEILESLGYEVvgiaDSGEEAIELAEENKPD---LILMDINLKGdMDGIEAAREIREK-FDIPVIF 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17534   79 LTAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 13-76 1.14e-07

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: 50.66  E-value: 1.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAG-----LEVASLGDARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQL 76
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEPdievvGEAADGEEALELLEELRPD---VVLLDIRMPGMDGLEALRRL 69
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
14-111 1.48e-07

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 51.82  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  14 VLIDDDPHLRQALSQTLDLAGLEV-ASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEIlAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKN 83

                         90
                 ....*....|....*....
gi 520869243  93 DIQLAVQAMRAGAYDFLEK 111
Cdd:PRK09958  84 DHFYGKHCADAGANGFVSK 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 13-112 2.97e-07

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: 48.55  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGV--IVSDIRMPGIDGLELLQQLrARDSEL---PVIL 87
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIdlILTEVDLPVSSGFKLLSYI-MRHKICkniPVIM 79

                         90       100
                 ....*....|....*....|....*
gi 520869243  88 ITGHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:cd17582   80 MSSQDSVGVVFKCLSKGAADYLVKP 104
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 10-126 3.12e-07

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 51.34  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  10 QAQVVLIDDDPHLRQALSQTLDLAGLEVAslgDARDL-------AARLPaewqGVIVSDIRMPGIDGLELLQQLRaRDSE 82
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMRVF---EAETLqrglleaATRKP----DLIILDLGLPDGDGIEFIRDLR-QWSA 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 520869243  83 LPVILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:PRK10529  73 IPVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVAL 116
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 9-116 4.18e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 50.73  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   9 TQAQVVLIDDDPHLRQALSQTLDLAG--LEVASLG-DARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDSELPV 85
Cdd:PRK11083   2 QQPTILLVEDEQAIADTLVYALQSEGftVEWFERGlPALDKLRQQPPD---LVILDVGLPDISGFELCRQLLAFHPALPV 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 520869243  86 ILITGHGDIQLAVQAMRAGAYDFLEKPF-PSE 116
Cdd:PRK11083  79 IFLTARSDEVDRLVGLEIGADDYVAKPFsPRE 110
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 13-119 6.55e-07

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 48.21  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTL-DLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGH 91
Cdd:cd17530    3 VLVLDDDPFQCMMAATILeDLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSGL 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520869243  92 GDIQLAVQAMRAGAYDF-----LEKPFPSEALL 119
Cdd:cd17530   83 DGGILESAETLAGANGLnllgtLSKPFSPEELT 115
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
6-123 8.57e-07

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 49.85  E-value: 8.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   6 PISTQAQVVLIDDDPHLRQALSQTLDL-AGLEV-ASLGD---ARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRaRD 80
Cdd:PRK10403   2 PEATPFQVLIVDDHPLMRRGVRQLLELdPGFEVvAEAGDgasAIDLANRLDPD---VILLDLNMKGMSGLDTLNALR-RD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 520869243  81 SELPVILITGHGDIQLAVQAM-RAGAYDFLEKPFPSEALLDSVR 123
Cdd:PRK10403  78 GVTAQIIILTVSDASSDVFALiDAGADGYLLKDSDPEVLLEAIR 121
PRK15369 PRK15369
two component system response regulator;
57-162 1.13e-06

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 49.31  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  57 VIVSDIRMPGIDGLELLQQLRARDSELPVILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRALALRQLV---L 133
Cdd:PRK15369  52 IVILDLGLPGMNGLDVIPQLHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKRYIdpaL 131

                         90       100
                 ....*....|....*....|....*....
gi 520869243 134 DNRSLRLALADRQQLSARLLGQSRAMLRL 162
Cdd:PRK15369 132 NREAILALLNADDTNPPLLTPRERQILKL 160
PRK10766 PRK10766
two-component system response regulator TorR;
13-126 1.30e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 49.27  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARdSELPVILITGHG 92
Cdd:PRK10766   5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSR-STVGIILVTGRT 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:PRK10766  84 DSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
pleD PRK09581
response regulator PleD; Reviewed
 57-123 2.32e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 49.90  E-value: 2.32e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520869243  57 VIVSDIRMPGIDGLELLQQLRA--RDSELPVILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:PRK09581  49 IILLDVMMPGMDGFEVCRRLKSdpATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVK 117
PRK10693 PRK10693
two-component system response regulator RssB;
58-112 4.31e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 48.45  E-value: 4.31e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 520869243  58 IVSDIRMPGIDGLELLQQLRARDSELPVILITGHGDIQLAVQAMRAGAYDFLEKP 112
Cdd:PRK10693  21 IICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
14-153 8.73e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 47.57  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  14 VLI-DDDPHLRQALSQTLDL-AGLEV---ASLG-DARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARdSELPVIL 87
Cdd:PRK12555   3 IGIvNDSPLAVEALRRALARdPDHEVvwvATDGaQAVERCAAQPPD---VILMDLEMPRMDGVEATRRIMAE-RPCPILI 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520869243  88 ITghGDIQLAV----QAMRAGAYDFLEKPF---------PSEALLDSVRRALALRQLVLDNRSLRLALADRQQLSARLL 153
Cdd:PRK12555  79 VT--SLTERNAsrvfEAMGAGALDAVDTPTlgigagleeYAAELLAKIDQIGRLLGRRLAPAAAPAAASAAPFRTTPRL 155
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
 2-116 1.01e-05

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 46.60  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   2 SSDTPISTQAQVVLI-DDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRaRD 80
Cdd:PRK10710   1 MTELPIDENTPRILIvEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR-RF 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 520869243  81 SELPVILITGHGDIQLAVQAMRAGAYDFLEKPF-PSE 116
Cdd:PRK10710  80 SDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYsPRE 116
FleQ pfam06490
Flagellar regulatory protein FleQ; This domain is found at the N terminus of a subset of ...
 12-127 1.59e-05

Flagellar regulatory protein FleQ; This domain is found at the N terminus of a subset of sigma54-dependent transcriptional activators that are involved in regulation of flagellar motility e.g. FleQ in Pseudomonas aeruginosa. It is clearly related to pfam00072, but lacks the conserved aspartate residue that undergoes phosphorylation in the classic two-component system response regulator (pfam00072).


Pssm-ID: 428975 [Multi-domain]  Cd Length: 108  Bit Score: 43.72  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMpgiDGLELLQQLRARDSELPVILITGH 91
Cdd:pfam06490   1 KILVIDDDAERRHDLSTILEFLGEQCEAISSEDLSAALWSSRWEALAVILGSV---SAAELLKALAKWDPHLPVLLLGET 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 520869243   92 GDIqlavqAMRAGAYDFLEKPFPSEALLDSVRRALA 127
Cdd:pfam06490  78 DDA-----LELANVIGTLEEPLNYPQLTDLLHRCQV 108
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 13-113 1.67e-05

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: 43.49  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAG---LEVASLGDARDLAARLPAewQGVIVSDIRMPG-IDGLELLQQLRARDSELPVILI 88
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGytvLEAASGDEALDLLESGPD--IDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLT 78

                         90       100
                 ....*....|....*....|....*
gi 520869243  89 TGHGDIQLAVQAMRAGaYDFLEKPF 113
Cdd:cd18161   79 SGYAENAIEGGDLAPG-VDVLSKPF 102
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
 13-119 2.39e-05

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: 43.19  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80

                         90       100
                 ....*....|....*....|....*..
gi 520869243  93 DIQLAVQAMRAGAYDFLEKPFPSEALL 119
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVLV 107
HTH_50 pfam18024
Helix-turn-helix domain; The TyrR protein of Haemophilus influenzae is a 36-kD transcription ...
 406-451 2.99e-05

Helix-turn-helix domain; The TyrR protein of Haemophilus influenzae is a 36-kD transcription factor whose major function is to control the expression of genes important in the biosynthesis and transport of aromatic amino acids. This entry represents the C-terminal helix-turn-helix DNA-binding domain of TyrR and related proteins.


Pssm-ID: 407862 [Multi-domain]  Cd Length: 50  Bit Score: 41.25  E-value: 2.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 520869243  406 EQVEAFERALIAAELNRpHGSLRSVAEALGLPRKTLHDKLRKHGLS 451
Cdd:pfam18024   6 EYVSYIERELIGAAYEN-YKSARKVAKALGLSHTTIANKMKRYGIS 50
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 175-292 3.36e-05

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: 43.44  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  175 DVLILGETGAGKEVVARALHDLSSRRNGPFVAINAGALAESV-----VESELFGHEPGAFTGAQKRrigkfefanGGTLF 249
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLfgrrnIDPGGASWVDGPLVRAARE---------GEIAV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 520869243  250 LDEIESMSLDLQVKLLRLLQERV--VERLGGNQSIALD-IRVIAAT 292
Cdd:pfam07728  72 LDEINRANPDVLNSLLSLLDERRllLPDGGELVKAAPDgFRLIATM 117
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 15-112 3.69e-05

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: 42.65  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  15 LIDDDPHLRQALSQTL--DLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITghg 92
Cdd:cd17565    3 IVDDDKNIIKILSDIIedDDLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMIS--- 79

                         90       100
                 ....*....|....*....|....*
gi 520869243  93 diQLAVQAMRAGAYD-----FLEKP 112
Cdd:cd17565   80 --QVSDKEMIGKAYQagiefFINKP 102
dpiA PRK10046
two-component response regulator DpiA; Provisional
 32-137 4.60e-05

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 44.62  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  32 LAGlevaSLGDARDLAARLPAewqGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHGDIQLAVQAMRAGAYDFLEK 111
Cdd:PRK10046  35 LAG----NLAQARMMIERFKP---GLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIK 107

                         90       100
                 ....*....|....*....|....*.
gi 520869243 112 PFPSEALLDSVRRALALRQLVLDNRS 137
Cdd:PRK10046 108 PIAYERLGQTLTRFRQRKHMLESIDS 133
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 13-108 8.24e-05

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 45.21  E-value: 8.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:PRK13558  10 VLFVGDDPEAGPVDCDLDEDGRLDVTQIRDFVAARDRVEAGEIDCVVADHEPDGFDGLALLEAVRQTTAVPPVVVVPTAG 89

                         90
                 ....*....|....*.
gi 520869243  93 DIQLAVQAMRAGAYDF 108
Cdd:PRK13558  90 DEAVARRAVDADAAAY 105
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
 61-126 1.04e-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: 41.84  E-value: 1.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520869243  61 DIRMPGIDGLELLQQLRARDSELPVILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL 126
Cdd:cd17533   60 DIKMEEKNGLEVAQKIRKYDPYAIIIFVTTHSEFAPLTFEYKVAALDFILKPLKLEEFKKRIEECI 125
PRK09483 PRK09483
response regulator; Provisional
 13-123 1.14e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 43.17  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTL-DLAGLEVA-SLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITG 90
Cdd:PRK09483   4 VLLVDDHELVRAGIRRILeDIKGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLTV 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:PRK09483  84 HTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIR 116
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
 13-123 1.15e-04

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: 41.92  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLD-LAGLEVASLGD-ARDLAARLPAEWqgVIVSdIRMPGIDGLELLQQLRA--RDSELPVILI 88
Cdd:cd17539    1 VLLVDDRPSSAERIAAMLSsEHEVVVEADPDeALFRAAEGPFDL--VIVS-LALEDFDGLRLCSQLRSleRTRQLPILAV 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVR 123
Cdd:cd17539   78 ADPGDRGRLIRALEIGVNDYLVRPIDPNELLARVR 112
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
11-111 2.31e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 42.56  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDPHLRQALSQTLDL-AGLEVA-SLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILI 88
Cdd:PRK09935   4 ASVIIMDTHPIIRMSIEVLLQKnSELQIVlKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFL 83

                         90       100
                 ....*....|....*....|...
gi 520869243  89 TGHGDIQLAVQAMRAGAYDFLEK 111
Cdd:PRK09935  84 SSKSECFYAGRAIQAGANGFVSK 106
PRK11697 PRK11697
two-component system response regulator BtsR;
13-127 2.40e-04

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 42.53  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGlEVASLGDARDLAARLPA---EWQGVIVSDIRMPGIDGLELLQQLrarDSE-LP-VIL 87
Cdd:PRK11697   4 VLIVDDEPLAREELRELLQEEG-DIEIVGECSNAIEAIGAihrLKPDVVFLDIQMPRISGLELVGML---DPEhMPyIVF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 520869243  88 ITGHGdiQLAVQAMRAGAYDFLEKPFPSEAL---LDSVRRALA 127
Cdd:PRK11697  80 VTAFD--EYAIKAFEEHAFDYLLKPIDPARLaktLARLRQERS 120
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
 15-118 2.52e-04

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: 41.17  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  15 LIDDDPHLRQALSQTL------DLAGLEVASLGDARDLAA--RLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVI 86
Cdd:cd17595    5 TVDDDPQVLRAVARDLrrqygkDYRVLRADSGAEALDALKelKLRGEAVALFLVDQRMPEMDGVEFLEKAMELFPEAKRV 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520869243  87 LITGHGDIQLAVQAMRAGAYDF-LEKPF--PSEAL 118
Cdd:cd17595   85 LLTAYADTDAAIRAINDVQLDYyLLKPWdpPEEKL 119
PRK10430 PRK10430
two-component system response regulator DcuR;
13-113 2.87e-04

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 42.40  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHL----RQALSQtldLAGLE----VASLGDARDLAARlPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELP 84
Cdd:PRK10430   4 VLIVDDDAMVaelnRRYVAQ---IPGFQccgtASTLEQAKEIIFN-SDTPIDLILLDIYMQQENGLDLLPVLHEAGCKSD 79

                         90       100
                 ....*....|....*....|....*....
gi 520869243  85 VILITGHGDIQLAVQAMRAGAYDFLEKPF 113
Cdd:PRK10430  80 VIVISSAADAATIKDSLHYGVVDYLIKPF 108
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
13-127 4.02e-04

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 43.04  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSELPVILITGHG 92
Cdd:PRK10841 804 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANA 883

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 520869243  93 diqLAVQAMR---AGAYDFLEKPfpseALLDSVRRALA 127
Cdd:PRK10841 884 ---LAEEKQRcleAGMDSCLSKP----VTLDVLKQTLT 914
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 13-113 4.64e-04

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: 39.51  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDL-AGLEVasLGDARD--LAARLPAEWQ-GVIVSDIRMPGIDGLELLQQLRARD--SELPVI 86
Cdd:cd17561    4 VLIADDNREFVQLLEEYLNSqPDMEV--VGVAHNgqEALELIEEKEpDVLLLDIIMPHLDGIGVLEKLRRMRleKRPKII 81

                         90       100
                 ....*....|....*....|....*..
gi 520869243  87 LITGHGDIQLAVQAMRAGAYDFLEKPF 113
Cdd:cd17561   82 MLTAFGQEDITQRAVELGASYYILKPF 108
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
 13-164 5.08e-04

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: 40.08  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDP----HLRQALSQTLDLAGLEVASLGDARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLRARDS--ELPVI 86
Cdd:cd17575    3 VLLVDDQAiigeAVRRALADEEDIDFHYCSDPTEAIEVASQIKPT---VILQDLVMPGVDGLTLVRFFRANPAtrDIPII 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520869243  87 LITGHGDIQLAVQAMRAGAYDFLEKpfpsealldsvrralalrqlvldnrslrlaLADRQQLSARLLGQSRAMLRLRE 164
Cdd:cd17575   80 VLSTKEEPEVKSEAFALGANDYLVK------------------------------LPDKIELVARIRYHSRSYINLLQ 127
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
408-447 6.57e-04

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 37.37  E-value: 6.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 520869243  408 VEAFERALIAAELNRPHGSLRSVAEALGLPRKTLHDKLRK 447
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 12-118 1.04e-03

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: 38.92  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  12 QVVLIDDDPHLRQALSQTLDLAGLEVASLGDARDLAARLPAEWQG--VIVSDIRMPGIDGLELLQQLRAR--DSELPVIL 87
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLfgRRERPLIV 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 520869243  88 I-TGHGDIQLAVQAMRAGAYDFLEKPFPSEAL 118
Cdd:cd19933   82 AlTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 27-112 1.84e-03

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 38.12  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  27 SQTLDLAGLEvaslGDARDLAARLPAewQGVIVSDIRMPGIDGLELLQQLRARDS--ELPVILITGHGDIQLAVQAMRAG 104
Cdd:cd17581   32 KRALEFLGLE----DEEDSSNFNEPK--VNMIITDYCMPGMTGYDLLKKVKESSAlkEIPVVIMSSENIPTRISRCLEEG 105


                 ....*...
gi 520869243 105 AYDFLEKP 112
Cdd:cd17581  106 AEDFLLKP 113
pleD PRK09581
response regulator PleD; Reviewed
 11-144 2.78e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 39.88  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  11 AQVVLIDDDP----HLRQALSQTLDLAglEVASLGDARDLAARLPAEwqgVIVSDIRMPGIDGLELLQQLR--ARDSELP 84
Cdd:PRK09581 156 GRILLVDDDVsqaeRIANILKEEFRVV--VVSDPSEALFNAAETNYD---LVIVSANFENYDPLRLCSQLRskERTRYVP 230

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520869243  85 VILITGHGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRRAL-------ALRQLVldNRSLRLALAD 144
Cdd:PRK09581 231 ILLLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIrrkryqdALRNNL--EQSIEMAVTD 295
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
5-127 3.84e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 39.66  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243   5 TPISTQAQVVLIDDDPHLRQALSQTLDLAGLE---VASLGDARDLAARLPAEWQGVIVSDirmPGIDGLELLQQLRARDS 81
Cdd:PRK13837 692 LPRGRGETVLLVEPDDATLERYEEKLAALGYEpvgFSTLAAAIAWISKGPERFDLVLVDD---RLLDEEQAAAALHAAAP 768

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 520869243  82 ELPVILITGHGDIQLAVQAMRAGAyDFLEKPFPSEALLDSVRRALA 127
Cdd:PRK13837 769 TLPIILGGNSKTMALSPDLLASVA-EILAKPISSRTLAYALRTALA 813
PRK15347 PRK15347
two component system sensor kinase;
61-112 4.90e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 39.63  E-value: 4.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 520869243  61 DIRMPGIDGLELLQQLR----ARDSELPVILITGH---GDIQLAVQamrAGAYDFLEKP 112
Cdd:PRK15347 741 DIRMPGLDGLETTQLWRddpnNLDPDCMIVALTANaapEEIHRCKK---AGMNHYLTKP 796
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
 13-130 5.49e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 38.46  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520869243  13 VVLIDDDPHLRQALSQTLDLAGLEVasLGDAR-DLA-ARLPAEWQGVIVSDIRMPGIDGLELLQQLRARDSElPVILITG 90
Cdd:PRK10701   4 IVFVEDDAEVGSLIAAYLAKHDIDV--TVEPRgDRAeATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG-PIVLLTS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 520869243  91 HGDIQLAVQAMRAGAYDFLEKPFPSEALLDSVRraLALRQ 130
Cdd:PRK10701  81 LDSDMNHILALEMGACDYILKTTPPAVLLARLR--LHLRQ 118
 
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