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Conserved domains on  [gi|815678357|ref|WP_046415654|]
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sigma-54 dependent transcriptional regulator [Barnesiella intestinihominis]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-443 0e+00

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


:

Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 533.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLrEEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNgVKNRPEKEtfqqysfnsILGQSKPLLEAIALARKVA 159
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLR-RENAEDSG---------LIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 160 STDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFL 239
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 240 DEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDI 319
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 320 RLLTEAFVQSLSEKMTHSSKtVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPieiqnaafkekscnns 399
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP---------------- 374
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 815678357 400 gFELSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEY 443
Cdd:COG2204  375 -EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-443 0e+00

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 533.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLrEEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNgVKNRPEKEtfqqysfnsILGQSKPLLEAIALARKVA 159
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLR-RENAEDSG---------LIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 160 STDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFL 239
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 240 DEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDI 319
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 320 RLLTEAFVQSLSEKMTHSSKtVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPieiqnaafkekscnns 399
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP---------------- 374
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 815678357 400 gFELSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEY 443
Cdd:COG2204  375 -EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
2-443 5.59e-125

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 370.33  E-value: 5.59e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   2 NKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:PRK11361   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFaDIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  81 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEkARTNGVKNRP-EKETFQQYSFNSILGQSKPLLEAIALARKVA 159
Cdd:PRK11361  85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ-LQSMKKEIRHlHQALSTSWQWGHILTNSPAMMDICKDTAKIA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 160 STDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFL 239
Cdd:PRK11361 164 LSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 240 DEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDI 319
Cdd:PRK11361 244 DEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 320 RLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPIEIQ---NAAFKEKSC 396
Cdd:PRK11361 324 SLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRqpvCNAGEVKTA 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 815678357 397 ----NNSGFELSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEY 443
Cdd:PRK11361 404 pvgeRNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEY 454
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-442 6.10e-123

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


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 365.60  E-value: 6.10e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357    4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEY-SPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARgQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNGvknRPEKETFQQYSFNSILGQSkPLLEAI--ALARkVAS 160
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQV---ALPADAGEAEDSAELIGEA-PAMQEVfrAIGR-LSR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  161 TDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFLD 240
Cdd:TIGR01818 156 SDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  241 EIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDIR 320
Cdd:TIGR01818 236 EIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIP 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  321 LLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPIEI-----QNAAFKEKS 395
Cdd:TIGR01818 316 RLARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELaltgrPASAPDSDG 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815678357  396 CNNSGFELSAMEKRHIAR--------------------VLDYTNGNKTEAAKLLKIGLTTLYRKIEE 442
Cdd:TIGR01818 396 QDSWDEALEAWAKQALSRgeqglldralpeferplleaALQHTRGHKQEAAALLGWGRNTLTRKLKE 462
Sigma54_activat pfam00158
Sigma-54 interaction domain;
141-308 4.81e-105

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 308.56  E-value: 4.81e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  141 ILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTG 220
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  221 ALKDKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFY 300
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 815678357  301 RLSVFQIH 308
Cdd:pfam00158 161 RLNVIPIE 168
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
4-121 5.38e-32

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: 118.36  E-value: 5.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYS-PNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDfPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKART 121
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRL 119
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
164-283 2.28e-12

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 64.32  E-value: 2.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   164 PVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLES---EIFGHKAGSFTGAlKDKKGLFEEAHN---GTI 237
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGE-LRLRLALALARKlkpDVL 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 815678357   238 FLDEIGEMAIELQAKLLRVLETGEYIKIgetKPTSVNVRIIAATNR 283
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLLEELRLLLL---LKSEKNLTVILTTND 125
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-443 0e+00

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 533.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLrEEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNgVKNRPEKEtfqqysfnsILGQSKPLLEAIALARKVA 159
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLR-RENAEDSG---------LIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 160 STDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFL 239
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 240 DEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDI 319
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 320 RLLTEAFVQSLSEKMTHSSKtVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPieiqnaafkekscnns 399
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP---------------- 374
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 815678357 400 gFELSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEY 443
Cdd:COG2204  375 -EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
64-445 1.92e-170

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: 485.82  E-value: 1.92e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  64 KTIKKISPESEIILLTAHGN-IPDGVQAIKNGAFDYITKG---DDNNKIIPLIS-----RAMEKARTNGVKNRPEKETFQ 134
Cdd:COG3829   54 KNVTELIPNSPLLEVLKTGKpVTGVIQKTGGKGKTVIVTAipiFEDGEVIGAVEtfrdiTELKRLERKLREEELERGLSA 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 135 QYSFNSILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHK 214
Cdd:COG3829  134 KYTFDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYE 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 215 AGSFTGALK-DKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGH 293
Cdd:COG3829  214 KGAFTGAKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGR 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 294 FREDLFYRLSVFQIHLPPLRERPGDIRLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCE 373
Cdd:COG3829  294 FREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSE 373
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815678357 374 SDELHPEDLPIEIQNAAFKEKSCNNSGFE--LSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEYKL 445
Cdd:COG3829  374 GDVITPEHLPEYLLEEAEAASAAEEGSLKeaLEEVEKELIEEALEKTGGNKSKAAKALGISRSTLYRKLKKYGI 447
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
136-444 1.79e-135

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 403.13  E-value: 1.79e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 136 YSFNSILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKA 215
Cdd:COG3284  318 AALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEP 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 216 GSFTGALKD-KKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHF 294
Cdd:COG3284  398 GAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRF 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 295 REDLFYRLSVFQIHLPPLRERpGDIRLLTEAFVQSLSEKmtHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCES 374
Cdd:COG3284  478 REDLYYRLNGLTLTLPPLRER-EDLPALIEHLLRELAAG--RGPLRLSPEALALLAAYPWPGNVRELRNVLRTALALADG 554
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815678357 375 DELHPEDLPIEIQNAAF-KEKSCNNSGFELSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEYK 444
Cdd:COG3284  555 GVITVEDLPDELRAELAaAAPAAAAPLTSLEEAERDAILRALRACGGNVSAAARALGISRSTLYRKLKRYG 625
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
2-443 5.59e-125

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 370.33  E-value: 5.59e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   2 NKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:PRK11361   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFaDIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  81 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEkARTNGVKNRP-EKETFQQYSFNSILGQSKPLLEAIALARKVA 159
Cdd:PRK11361  85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ-LQSMKKEIRHlHQALSTSWQWGHILTNSPAMMDICKDTAKIA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 160 STDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFL 239
Cdd:PRK11361 164 LSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 240 DEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDI 319
Cdd:PRK11361 244 DEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 320 RLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPIEIQ---NAAFKEKSC 396
Cdd:PRK11361 324 SLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRqpvCNAGEVKTA 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 815678357 397 ----NNSGFELSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEY 443
Cdd:PRK11361 404 pvgeRNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEY 454
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-442 6.10e-123

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


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 365.60  E-value: 6.10e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357    4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEY-SPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARgQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNGvknRPEKETFQQYSFNSILGQSkPLLEAI--ALARkVAS 160
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQV---ALPADAGEAEDSAELIGEA-PAMQEVfrAIGR-LSR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  161 TDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFLD 240
Cdd:TIGR01818 156 SDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  241 EIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDIR 320
Cdd:TIGR01818 236 EIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIP 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  321 LLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPIEI-----QNAAFKEKS 395
Cdd:TIGR01818 316 RLARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELaltgrPASAPDSDG 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815678357  396 CNNSGFELSAMEKRHIAR--------------------VLDYTNGNKTEAAKLLKIGLTTLYRKIEE 442
Cdd:TIGR01818 396 QDSWDEALEAWAKQALSRgeqglldralpeferplleaALQHTRGHKQEAAALLGWGRNTLTRKLKE 462
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
4-445 2.89e-110

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: 332.48  E-value: 2.89e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357    4 VLIIDDEPQIRQLLAriLGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLP---DG--NGVDFIKTIKKISPESEIIL 77
Cdd:TIGR02915   1 LLIVEDDLGLQKQLK--WSFADYELAVAADRESAIALVrRHEPAVVTLDLGLPpdaDGasEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   78 LTAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNgVKNRPEKETFQQYSFNSILGQSKPLLEAIALARK 157
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLE-TENRRLQSALGGTALRGLITSSPGMQKICRTIEK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  158 VASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTI 237
Cdd:TIGR02915 158 IAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  238 FLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPG 317
Cdd:TIGR02915 238 FLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  318 DIRLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPIEIQNAAFKEKSCN 397
Cdd:TIGR02915 318 DAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLGLDARERAETPLEVN 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 815678357  398 NSGFELSAmEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEYKL 445
Cdd:TIGR02915 398 LREVRERA-EREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
Sigma54_activat pfam00158
Sigma-54 interaction domain;
141-308 4.81e-105

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 308.56  E-value: 4.81e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  141 ILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTG 220
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  221 ALKDKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFY 300
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 815678357  301 RLSVFQIH 308
Cdd:pfam00158 161 RLNVIPIE 168
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
3-442 2.05e-103

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 315.66  E-value: 2.05e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAH 81
Cdd:PRK10923   5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALaSKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTngvKNRPEKETFQQySFNSILGQSKPLLEAIALARKVAST 161
Cdd:PRK10923  85 SDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQE---QQQPRNIQVNG-PTTDIIGEAPAMQDVFRIIGRLSRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 162 DVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFLDE 241
Cdd:PRK10923 161 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 242 IGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDIRL 321
Cdd:PRK10923 241 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 322 LTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPIEIQNAAFKEKSCN---- 397
Cdd:PRK10923 321 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSQmqpd 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815678357 398 --------------NSGFE------LSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEE 442
Cdd:PRK10923 401 swatllaqwadralRSGHQnllseaQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKE 465
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-440 4.74e-103

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 313.89  E-value: 4.74e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVrEQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMekARTNGVKNRPEKETFQQYSfnsILGQS---KPLLEAIALarkVA 159
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAL--AHTHSIDAETPAVTASQFG---MVGKSpamQHLLSEIAL---VA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 160 STDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFL 239
Cdd:PRK10365 160 PSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 240 DEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDI 319
Cdd:PRK10365 240 DEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 320 RLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPIEIQNAAFKEKSCNNS 399
Cdd:PRK10365 320 PLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDI 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 815678357 400 GfELSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKI 440
Cdd:PRK10365 400 Q-PLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
137-382 9.30e-103

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 315.21  E-value: 9.30e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 137 SFNSILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAG 216
Cdd:COG3283  202 GFDHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPG 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 217 SFTGALKDKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFRE 296
Cdd:COG3283  282 AFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFRE 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 297 DLFYRLSVFQIHLPPLRERPGDIRLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDE 376
Cdd:COG3283  362 DLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGDE 441

                 ....*.
gi 815678357 377 LHPEDL 382
Cdd:COG3283  442 LTPEDL 447
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
141-438 5.74e-100

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 307.87  E-value: 5.74e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 141 ILGQSKP---LLEAIALarkVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGS 217
Cdd:PRK05022 189 MIGQSPAmqqLKKEIEV---VAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGA 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 218 FTGALKDKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFRED 297
Cdd:PRK05022 266 FTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRAD 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 298 LFYRLSVFQIHLPPLRERPGDIRLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVC--ESD 375
Cdd:PRK05022 346 LYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVISRAALLAraRGA 425
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815678357 376 E----LHPEDLPIEIQNAAFKEKSCNNSGFELS--------AMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYR 438
Cdd:PRK05022 426 GrivtLEAQHLDLPAEVALPPPEAAAAPAAVVSqnlreateAFQRQLIRQALAQHQGNWAAAARALELDRANLHR 500
PRK15115 PRK15115
response regulator GlrR; Provisional
4-445 9.77e-100

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 305.22  E-value: 9.77e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:PRK15115   8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLnREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNGvknrpeKETFQQysfnSILGQSKPLLEAIALARKVASTD 162
Cdd:PRK15115  88 SIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPAT------DERWRE----AIVTRSPLMLRLLEQARMVAQSD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 163 VPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFLDEI 242
Cdd:PRK15115 158 VSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 243 GEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDIRLL 322
Cdd:PRK15115 238 GDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 323 TEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCE----SDELHPEDLpiEIQNAAFKEKSCNN 398
Cdd:PRK15115 318 ANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSspviSDALVEQAL--EGENTALPTFVEAR 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 815678357 399 SGFELSAMEKrhiarVLDYTNGNKTEAAKLLKIGLTTLYRKIEEYKL 445
Cdd:PRK15115 396 NQFELNYLRK-----LLQITKGNVTHAARMAGRNRTEFYKLLSRHEL 437
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
120-381 3.32e-99

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: 307.03  E-value: 3.32e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  120 RTNGVKNRPEKETFQQYSFNSILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCS 199
Cdd:TIGR01817 177 SKQLRDKAPEIARRRSGKEDGIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCA 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  200 AFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIA 279
Cdd:TIGR01817 257 ALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVA 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  280 ATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDIRLLTEAFVQSLSEKmTHSSKTVSKAFIDMLEQQEWKGNVR 359
Cdd:TIGR01817 337 ATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRE-NGRPLTITPSAIRVLMSCKWPGNVR 415
                         250       260
                  ....*....|....*....|..
gi 815678357  360 ELRNVIERSLIVCESDELHPED 381
Cdd:TIGR01817 416 ELENCLERTATLSRSGTITRSD 437
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
116-441 3.94e-92

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: 288.30  E-value: 3.94e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  116 MEKARTNGVKNRPEKETFQ-QYSFNSILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFV 194
Cdd:TIGR02329 188 ATRLRQAATLRSATRNQLRtRYRLDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFV 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  195 AINCSAFSKELLESEIFGHKAGSFTGALKD-KKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSV 273
Cdd:TIGR02329 268 AINCGAIAESLLEAELFGYEEGAFTGARRGgRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPV 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  274 NVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDIRLLTEAFVQ----SLSEKMTHSSKTVSKAFIDML 349
Cdd:TIGR02329 348 DVRVVAATHCALTTAVQQGRFRRDLFYRLSILRIALPPLRERPGDILPLAAEYLVqaaaALRLPDSEAAAQVLAGVADPL 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  350 EQQEWKGNVRELRNVIER---SLIVCESDELHPEDLPI---EIQNAAFKEKSCNNSGFELSAMEKRHIARVLDYTNGNKT 423
Cdd:TIGR02329 428 QRYPWPGNVRELRNLVERlalELSAMPAGALTPDVLRAlapELAEASGKGKTSALSLRERSRVEALAVRAALERFGGDRD 507
                         330
                  ....*....|....*...
gi 815678357  424 EAAKLLKIGLTTLYRKIE 441
Cdd:TIGR02329 508 AAAKALGISRTTLWRRLK 525
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
115-442 1.71e-90

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 284.30  E-value: 1.71e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 115 AMEKAR---TNGVKNRPEKETFQQYSFNSILGQSKPLL---EAIALARKVASTdvpVLLTGETGTGKEVFAQAIHHE--- 185
Cdd:PRK15424 192 ALDMTRmtlRHNTHYATRNALRTRYVLGDLLGQSPQMEqvrQTILLYARSSAA---VLIQGETGTGKELAAQAIHREyfa 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 186 -----SKRNKGNFVAINCSAFSKELLESEIFGHKAGSFTGALKD-KKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLET 259
Cdd:PRK15424 269 rhdarQGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGgRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEE 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 260 GEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDIRLLTEAFVQ----SLSEKMT 335
Cdd:PRK15424 349 KEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKqslaALSAPFS 428
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 336 HSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDlPIEIQNAAfKEKSCNNSGFELSAMEKRHIARVL 415
Cdd:PRK15424 429 AALRQGLQQCETLLLHYDWPGNVRELRNLMERLALFLSVEPTPDLT-PQFLQLLL-PELARESAKTPAPRLLAATLQQAL 506
                        330       340
                 ....*....|....*....|....*..
gi 815678357 416 DYTNGNKTEAAKLLKIGLTTLYRKIEE 442
Cdd:PRK15424 507 ERFNGDKTAAANYLGISRTTLWRRLKA 533
PRK10820 PRK10820
transcriptional regulator TyrR;
138-445 1.14e-84

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 268.86  E-value: 1.14e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 138 FNSILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGS 217
Cdd:PRK10820 203 FSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGA 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 218 FTGALKDKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFRED 297
Cdd:PRK10820 283 YPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFRED 362
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 298 LFYRLSVFQIHLPPLRERPGDIRLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDEL 377
Cdd:PRK10820 363 LYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLEGYEL 442
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815678357 378 HPED--LPIEIQNAAFKEKSCNNSgfeLSAMEKRHIARVL-----DYTNGNKTeaAKLLKIGLTTLYRKIEEYKL 445
Cdd:PRK10820 443 RPQDilLPDYDAAVAVGEDAMEGS---LDEITSRFERSVLtrlyrNYPSTRKL--AKRLGVSHTAIANKLREYGL 512
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
167-445 3.44e-81

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: 254.00  E-value: 3.44e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 167 LTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESeifghkagsftgalkdkkglfeeahngtifldeigema 246
Cdd:COG3604  120 ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 247 ielqakllrvLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPLRERPGDIRLLTEAF 326
Cdd:COG3604  162 ----------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHF 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 327 VQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDELHPEDLPIEIQNAafkekscnnsgfeLSAM 406
Cdd:COG3604  232 LEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGSREA-------------LEEV 298
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 815678357 407 EKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEYKL 445
Cdd:COG3604  299 EREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGI 337
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
138-436 9.58e-77

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 252.44  E-value: 9.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 138 FNSILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGS 217
Cdd:PRK15429 375 FGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGA 454
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 218 FTGALKDKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFRED 297
Cdd:PRK15429 455 FTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSD 534
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 298 LFYRLSVFQIHLPPLRERPGDIRLLTEAFVQSLSEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESDEL 377
Cdd:PRK15429 535 LYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVL 614
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815678357 378 H---PEDLPIEIQNAAFKEKSCNNsgfelSAMEKRHIARVLDYTNG---NKTEAAKLLKIGLTTL 436
Cdd:PRK15429 615 QlslPDITLPEPETPPAATVVAQE-----GEDEYQLIVRVLKETNGvvaGPKGAAQRLGLKRTTL 674
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
136-445 9.58e-73

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 240.74  E-value: 9.58e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 136 YSFNSILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKA 215
Cdd:PRK11388 322 HTFDHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLGSDR 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 216 GSFTGALKDKkglFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFR 295
Cdd:PRK11388 402 TDSENGRLSK---FELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFS 478
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 296 EDLFYRLSVFQIHLPPLRERPGDIRLLTEAFVQSLsEKMTHSSKTVSKAFIDMLEQQEWKGNVRELRNVIERSLIVCESD 375
Cdd:PRK11388 479 RQLYYALHAFEITIPPLRMRREDIPALVNNKLRSL-EKRFSTRLKIDDDALARLVSYRWPGNDFELRSVIENLALSSDNG 557
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815678357 376 ELHPEDLPIEIqnaaFKEKSCNNSG-------FELSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEEYKL 445
Cdd:PRK11388 558 RIRLSDLPEHL----FTEQATDDVSatrlstsLSLAELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGI 630
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
140-369 9.92e-70

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 224.16  E-value: 9.92e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 140 SILGQSKPLLEAIALARKVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHKAGSFT 219
Cdd:PRK11608   7 NLLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 220 GALKDKKGLFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLF 299
Cdd:PRK11608  87 GAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLL 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815678357 300 YRLSVFQIHLPPLRERPGDIRLLTEAFVQSLSEKMthsSKTVSKAFIDMLEQQ----EWKGNVRELRNVIERSL 369
Cdd:PRK11608 167 DRLAFDVVQLPPLRERQSDIMLMAEHFAIQMCREL---GLPLFPGFTERARETllnyRWPGNIRELKNVVERSV 237
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
157-367 4.36e-43

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


Pssm-ID: 443688 [Multi-domain]  Cd Length: 534  Bit Score: 158.84  E-value: 4.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 157 KVAS-TDVPVLLTGETGTGKEVFAQAIHhESKRN----KGNFVAINCSAFSKELLESEIFGHKAGSFTGALKDKKGLFEE 231
Cdd:COG4650  202 RVAIrSRAPILLTGPTGAGKSQLARRIY-ELKKArhqvSGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGLLRS 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 232 AHNGTIFLDEIGEMAIELQAKLLRVLETGEYIKIGETKPTSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPP 311
Cdd:COG4650  281 ADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPG 360
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815678357 312 LRERPGDIR-----LLtEAFVQSLSEKMTHsSKTVSKAFIDMLEQQE--WKGNVRELRNVIER 367
Cdd:COG4650  361 LAERREDIEpnldyEL-ARFAREQGRRVRF-NKEARARYLAFATSPEalWSGNFRDLNASVTR 421
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
98-395 1.05e-35

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: 140.24  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  98 YITKGDDNNKIIPLISRAMEKARTNGVKNRPEKEtfqQYSFNSILGQSKPLLEAIALArKVA----STDVPVLLTGETGT 173
Cdd:COG1221   66 FLDKEAFEEQFGTKLKSEYSFVELLAEKENNEEE---EDPFDNLIGANGSLKNAIEQA-KAAilypPKGLHTLILGPTGV 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 174 GKEVFAQAIHH---ESKR--NKGNFVAINCS--AFSKELLESEIFGHKAGSFTGALKDKKGLFEEAHNGTIFLDEIGEMA 246
Cdd:COG1221  142 GKSFFAELMYEyaiEIGVlpEDAPFVVFNCAdyANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLP 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 247 IELQAKLLRVLETGEYIKIGETKPT-SVNVRIIAATNrnlpEEINaghfredlfyrlSVF----------QIHLPPLRER 315
Cdd:COG1221  222 PEGQEMLFTFMDKGIYRRLGETEKTrKANVRIIFATT----EDPE------------SSLlktflrripmVIKLPSLEER 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 316 PGDIRL-LTEAFVQSLSEKMTHS---SKTVSKAFIdmleQQEWKGNVRELRNVIErslIVC------------ESDELHP 379
Cdd:COG1221  286 SLEERLeLIKHFFKEEAKRLNKPikvSKEVLKALL----LYDCPGNIGQLKSDIQ---LACakaflnyitnkkEEIEITL 358
                        330
                 ....*....|....*.
gi 815678357 380 EDLPIEIQNAAFKEKS 395
Cdd:COG1221  359 SDLPENVKKGLLKLKE 374
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
4-121 5.38e-32

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: 118.36  E-value: 5.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYS-PNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDfPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKART 121
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRL 119
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
4-117 7.17e-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: 114.90  E-value: 7.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIkERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAME 117
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
4-101 6.13e-29

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 109.55  E-value: 6.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357    4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLkEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90
                  ....*....|....*....
gi 815678357   83 NIPDGVQAIKNGAFDYITK 101
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSK 99
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
5-101 2.24e-28

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 107.70  E-value: 2.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   5 LIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHGN 83
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLrEERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*...
gi 815678357  84 IPDGVQAIKNGAFDYITK 101
Cdd:cd00156   81 EEDAVRALELGADDYLVK 98
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1-101 1.55e-27

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 108.89  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLeEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100
                 ....*....|....*....|..
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITK 101
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTK 102
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
150-303 6.66e-27

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 105.31  E-value: 6.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 150 EAIALARKVA--STDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFGHkagsftGALKDKKG 227
Cdd:cd00009    5 EAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGH------FLVRLLFE 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815678357 228 LFEEAHNGTIFLDEIGEMAIELQAKLLRVLETGEyikigETKPTSVNVRIIAATNRNLPeeinaGHFREDLFYRLS 303
Cdd:cd00009   79 LAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLN-----DLRIDRENVRVIGATNRPLL-----GDLDRALYDRLD 144
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
3-101 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: 99.46  E-value: 2.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARIL-GLEGYE-VLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILeWEAGFEvVGEAENGEEALELLeEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                         90       100
                 ....*....|....*....|..
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITK 101
Cdd:COG4753   81 GYSDFEYAQEAIKLGADDYLLK 102
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-101 2.58e-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: 2.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILG-LEGYEVL-QAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESEIIL 77
Cdd:COG4565    3 MIRVLIVEDDPMVAELLRRYLErLPGFEVVgVASSGEEALALLAeHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIV 82
                         90       100
                 ....*....|....*....|....
gi 815678357  78 LTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIK 106
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
2-101 3.11e-25

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: 99.44  E-value: 3.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   2 NKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALArEEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTG 80
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17563   81 YASIATAVEAIKLGADDYLAK 101
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
3-135 5.22e-25

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 100.76  E-value: 5.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAH 81
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEqAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGY 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 815678357  82 GNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNGVK----NRPEKETFQQ 135
Cdd:COG4567   86 ASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENpmslDRLEWEHIQR 143
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
3-121 3.42e-24

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 97.23  E-value: 3.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESE--IILLT 79
Cdd:COG0784    7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRaGPPDLILLDINMPGMDGLELLRRIRALPRLPDipIIALT 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKART 121
Cdd:COG0784   87 AYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1-101 7.25e-24

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: 7.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESE--IIL 77
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLqEHRPDLILLDLEMPDMDGLELCRRLRADPRTADipIIF 80
                         90       100
                 ....*....|....*....|....
gi 815678357  78 LTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTK 104
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
3-101 1.62e-23

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: 94.96  E-value: 1.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAH 81
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRsEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGA 81
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:cd17555   82 GVMSDAVEALRLGAWDYLTK 101
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
3-120 3.85e-23

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 97.16  E-value: 3.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEI--ILLT 79
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLlEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIpvIFLT 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKAR 120
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRR 128
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
5-101 8.67e-23

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: 92.09  E-value: 8.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   5 LIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQ-MEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHGN 83
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELaREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*...
gi 815678357  84 IPDGVQAIKNGAFDYITK 101
Cdd:cd17574   81 EEDKVLGLELGADDYITK 98
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
2-101 2.33e-21

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: 88.85  E-value: 2.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   2 NKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEI--ILL 78
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIvEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIpiIML 80
                         90       100
                 ....*....|....*....|...
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITK 103
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
4-101 1.12e-20

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: 86.45  E-value: 1.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQ-MEYSPNVILCDVFLPDGNGVDFIKTIKKIS--PeseIILLTA 80
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEaATRKPDLIILDLGLPDMDGLEVIRRLREWSavP---VIVLSA 77
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17620   78 RDEESDKIAALDAGADDYLTK 98
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
2-116 2.06e-20

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: 86.18  E-value: 2.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   2 NKVLIIDDEPQIRQLLARILGLEGYEVL-QAGDCKAAV-KQMEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVeKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAM 116
Cdd:cd17542   81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
4-117 4.26e-20

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 85.26  E-value: 4.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLE-GYEVL-QAGDCKAAVKQ-MEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpDIEVVgEAADGEEALALlRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 815678357  81 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAME 117
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
2-115 7.36e-20

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: 84.63  E-value: 7.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   2 NKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYS-PNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSqPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 815678357  81 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRA 115
Cdd:cd19919   81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERA 115
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
4-137 7.46e-20

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: 87.08  E-value: 7.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEV---------LQAGDckaavkqmEYSPNVILCDVFLPDGNGVDFIKTIKKISPESE 74
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVetfasaeafLAALD--------PDRPGCLLLDVRMPGMSGLELQEELAARGSPLP 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815678357  75 IILLTAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKARTNGVKNRPEKETFQQYS 137
Cdd:COG4566   74 VIFLTGHGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRARLA 136
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
4-118 9.91e-20

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: 84.31  E-value: 9.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGY---EVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELgfeVVGEAENGEEALELIeEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEK 118
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
3-101 1.22e-19

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: 83.70  E-value: 1.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKiSPESE---IILL 78
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEeELPDLILLDVMMPGMDGFEVCRRLKE-DPETRhipVIMI 79
                         90       100
                 ....*....|....*....|...
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17538   80 TALDDREDRIRGLEAGADDFLSK 102
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1-120 1.63e-19

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 87.18  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILG-LEGYEVL-QAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIIL 77
Cdd:COG3279    1 MMKILIVDDEPLARERLERLLEkYPDLEVVgEASNGEEALELLeEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 815678357  78 LTAHGNipDGVQAIKNGAFDYITKGDDNNKIIplisRAMEKAR 120
Cdd:COG3279   81 TTAYDE--YALEAFEVNAVDYLLKPIDEERLA----KALEKAK 117
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
4-117 1.86e-19

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: 83.79  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYS-PNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQpPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAME 117
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALK 115
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
157-312 2.59e-19

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 83.93  E-value: 2.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  157 KVASTDVPVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESeifghkagsftgalkdkkglfeeAHNGT 236
Cdd:pfam14532  16 QAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ-----------------------AKGGT 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815678357  237 IFLDEIGEMAIELQAKLLRVLETGEyikigetkptSVNVRIIAATNRNLPEEINAGHFREDLFYRLSVFQIHLPPL 312
Cdd:pfam14532  73 LYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFELSALRLHVPPL 138
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
3-117 1.94e-18

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: 80.53  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAH 81
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPvDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGY 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 815678357  82 GNIPDGVQAIKNGA-FDYITKGDDNNKIIPLISRAME 117
Cdd:cd17569   82 ADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1-222 3.84e-18

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 83.31  E-value: 3.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSPNVILCDVFLPDGNGVDFIKTIKKiSPESEIILLTA 80
Cdd:PRK10955   1 MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDVMMPKKNGIDTLKELRQ-THQTPVIMLTA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  81 HGNIPDGVQAIKNGAFDYITKGDDNNKIIplisramekARTNGVKNRPEKETFQQYSFNsilgqSKPLLEAIAL----AR 156
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDRELV---------ARIRAILRRSHWSEQQQNNDN-----GSPTLEVDALslnpGR 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815678357 157 KVASTDVPVL-LTGETGTGKEVFAQaihheskrNKGNFVaincsafSKELLESEIFGHKAGSFTGAL 222
Cdd:PRK10955 146 QEASFDGQTLeLTGTEFTLLYLLAQ--------HLGQVV-------SREHLSQEVLGKRLTPFDRAI 197
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
4-101 1.26e-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: 77.96  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPyDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTK 99
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
4-101 2.33e-17

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: 77.17  E-value: 2.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKiSPESE---IILLT 79
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQaEPPDLILLDVMMPGMDGFEVCRRLKA-DPATRhipVIFLT 79
                         90       100
                 ....*....|....*....|..
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd19920   80 ALTDTEDKVKGFELGAVDYITK 101
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
3-101 3.00e-17

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: 77.39  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAH 81
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAArEFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:cd17615   81 DSVEDRIAGLTAGGDDYVTK 100
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
4-101 2.71e-16

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: 74.08  E-value: 2.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEgDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPK 99
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-120 7.06e-16

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 75.76  E-value: 7.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVL-QAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESeIILL 78
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVrELKPDLVIVDIDMPDRDGLEAARQISEERPAP-VILL 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 815678357  79 TAHGNiPDGVQ-AIKNGAFDYITKGDDNNKIIPLISRAMEKAR 120
Cdd:COG3707   82 TAYSD-PELIErALEAGVSAYLVKPLDPEDLLPALELALARFR 123
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
4-116 7.67e-16

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: 73.40  E-value: 7.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQ-MEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAaPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAM 116
Cdd:cd17537   83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
fixJ PRK09390
response regulator FixJ; Provisional
4-120 1.70e-15

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 74.65  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:PRK09390   6 VHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALpGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHG 85
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKAR 120
Cdd:PRK09390  86 DVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAP 123
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
3-118 1.78e-15

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 75.53  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKK--ISPESEIILLT 79
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLnEPWPDLILLDWMLPGGSGIQFIKHLKResMTRDIPVVMLT 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEK 118
Cdd:PRK10161  84 ARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRR 122
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
5-101 1.95e-15

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: 72.31  E-value: 1.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   5 LIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESE--IILLTAH 81
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKdEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSipIIMLTAK 80
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:cd19937   81 GEEFDKVLGLELGADDYITK 100
orf27 CHL00148
Ycf27; Reviewed
3-140 4.63e-15

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 74.37  E-value: 4.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLP--DGNGVdfiktIKKISPESE--IIL 77
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRkEQPDLVILDVMMPklDGYGV-----CQEIRKESDvpIIM 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815678357  78 LTAHGNIPDGVQAIKNGAFDYITKgddnnkiiPLISRAMEkARTNGVKNRPEKETFQQYSFNS 140
Cdd:CHL00148  83 LTALGDVSDRITGLELGADDYVVK--------PFSPKELE-ARIRSVLRRTNKKSFSSKIPNS 136
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
4-101 6.65e-15

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: 70.59  E-value: 6.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPyDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVK 99
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
4-101 6.68e-15

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 70.87  E-value: 6.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVIsGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVK 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
4-101 9.30e-15

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: 70.41  E-value: 9.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKiSPESEIILLTAHG 82
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALlEGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTARG 79
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd17623   80 DDIDRILGLELGADDYLPK 98
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
3-104 1.51e-14

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 69.56  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYS-PNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAH 81
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEdPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81
                         90       100
                 ....*....|....*....|...
gi 815678357  82 GNIPDGVQAIKNGAfdYITKGDD 104
Cdd:cd17554   82 SEYKSDFSSWAADA--YVVKSSD 102
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
4-101 1.70e-14

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 69.41  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESEIIL--LTA 80
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQrFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAiaLTG 80
                         90       100
                 ....*....|....*....|..
gi 815678357  81 HGNIPDGVQAIKNGaFD-YITK 101
Cdd:cd17580   81 YGQPEDRERALEAG-FDaHLVK 101
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
5-101 1.79e-14

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: 69.56  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   5 LIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHGN 83
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIyDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90
                 ....*....|....*...
gi 815678357  84 IPDGVQAIKNGAFDYITK 101
Cdd:cd17625   81 VEDRVKGLDLGADDYLPK 98
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
4-101 2.21e-14

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 69.37  E-value: 2.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQ-MEYSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAHG 82
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKvEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd17614   80 SEVDKVLGLELGADDYVTK 98
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
4-101 2.39e-14

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: 68.95  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAHG 82
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILaRQDIDLVLLDINLPGKDGLSLTRELREQS-EVGIILVTGRD 81
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd17619   82 DEVDRIVGLEIGADDYVTK 100
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
3-101 1.09e-13

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 67.27  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILG-LEGYEVL-QAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEqVPGFTVIgTAGTGEEALKLLkERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVT 81
                         90       100
                 ....*....|....*....|...
gi 815678357  80 AhGNIPDGVQ-AIKNGAFDYITK 101
Cdd:cd19925   82 A-ANDVETVReALRLGVVDYLIK 103
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1-101 1.10e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 70.22  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGY-----EVLQAGDCKAAVKQmeysPNVILCDVFLPDGNGVDFIKTIKKISPeSEI 75
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMrvfeaETLQRGLLEAATRK----PDLIILDLGLPDGDGIEFIRDLRQWSA-IPV 75
                         90       100
                 ....*....|....*....|....*.
gi 815678357  76 ILLTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10529  76 IVLSARSEESDKIAALDAGADDYLSK 101
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
3-101 1.19e-13

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


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 67.18  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKIsPESE---IILL 78
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIArKEKPDLILMDIQLPGMDGLEATRLLKED-PATRdipVIAL 79
                         90       100
                 ....*....|....*....|...
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17548   80 TAYAMKGDREKILEAGCDGYISK 102
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
4-101 2.62e-13

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: 65.95  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESE---IILLT 79
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPfDLVLMDLQMPVMDGLEATRRIRELEGGGRrtpIIALT 80
                         90       100
                 ....*....|....*....|..
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSK 102
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1-82 8.21e-13

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: 65.30  E-value: 8.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLE-GYEVL-QAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIkkISP-ESEII 76
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEpDIEVVgEAADGEEALELLEeLRPDVVLLDIRMPGMDGLEALRRL--LTPrEREVL 78

                 ....*.
gi 815678357  77 LLTAHG 82
Cdd:COG2197   79 RLLAEG 84
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-101 1.21e-12

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 64.46  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSPNV--ILCDVFLPDGNGVDFIKTIKKISPESE--IILL 78
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIklVITDYNMPEMDGFELVREIRKKYSRDQlaIIGI 81
                         90       100
                 ....*....|....*....|...
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTK 104
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
3-108 2.08e-12

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 63.73  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAH 81
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVtKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81
                         90       100
                 ....*....|....*....|....*...
gi 815678357  82 GNIpDGVQAIKN-GAFDYITKGDDNNKI 108
Cdd:cd17553   82 GEL-DMIQESKElGALTHFAKPFDIDEI 108
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
4-101 2.09e-12

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 63.16  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGD-CKAAVKQMEYSPNVILCDVFLPDGNGVDFIKTIKKIS--PESEIILLTA 80
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDpLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSalKDTPIIMLTG 80
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTK 101
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
164-283 2.28e-12

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 64.32  E-value: 2.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   164 PVLLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLES---EIFGHKAGSFTGAlKDKKGLFEEAHN---GTI 237
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGE-LRLRLALALARKlkpDVL 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 815678357   238 FLDEIGEMAIELQAKLLRVLETGEYIKIgetKPTSVNVRIIAATNR 283
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLLEELRLLLL---LKSEKNLTVILTTND 125
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
3-55 2.63e-12

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.43  E-value: 2.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 815678357     3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLP 55
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLkEEKPDLILLDIMMP 55
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
4-101 2.64e-12

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: 62.84  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQ-MEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLaLTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVK 99
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
4-120 3.10e-12

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: 62.94  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGY--EVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDieIVGEAENGEEALEAIeELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 815678357  81 HGNIpdGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKAR 120
Cdd:cd17532   81 YDEY--AVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
3-101 3.55e-12

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: 63.18  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLE-GYEVL-QAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESeIILLT 79
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDpDIEVVgTARDGEEALEKIkELKPDVITLDIEMPVMDGLEALRRIMAERPTP-VVMVS 80
                         90       100
                 ....*....|....*....|....
gi 815678357  80 AH--GNIPDGVQAIKNGAFDYITK 101
Cdd:cd17541   81 SLteEGAEITLEALELGAVDFIAK 104
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
4-101 4.85e-12

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 62.30  E-value: 4.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAaVKQ--MEYSPNVILCDVFLPDGNGVDFIKTIKKISPeSEIILLTAH 81
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFED-VLEefLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSR 78
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:cd18159   79 DDNMDQVMAINMGGDDYITK 98
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
4-101 1.35e-11

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: 61.61  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGlEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWvQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81
                         90       100
                 ....*....|....*....|
gi 815678357  83 NIPDGVQAIKN-GAFDYITK 101
Cdd:cd17596   82 DSEDIIAGINEaGIYQYLTK 101
ompR PRK09468
osmolarity response regulator; Provisional
1-139 1.99e-11

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 63.84  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:PRK09468   5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESfHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLT 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLIsRAMEKARTNGVKNRPEKE----TFQQYSFN 139
Cdd:PRK09468  85 AKGEEVDRIVGLEIGADDYLPKPFNPRELLARI-RAVLRRQAPELPGAPSQEeeviAFGKFKLN 147
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
4-101 2.56e-11

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 60.08  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEI--ILLTA 80
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLnQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIpvIFLTA 80
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSK 101
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
3-118 5.01e-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: 59.73  E-value: 5.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVL-QAGDCKAAV-KQMEYSPNVILCDVFLPDGNGVDFIKTI--KKISPeseIILL 78
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVeLAKKHKPDLVIMDVKMPRLDGIEAAKIItsENIAP---IVLL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEK 118
Cdd:cd19932   79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
3-101 7.35e-11

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: 59.38  E-value: 7.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGY-EVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESE--IILL 78
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCrENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDvpIVMI 81
                         90       100
                 ....*....|....*....|...
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17551   82 TADTDREVRLRALEAGATDFLTK 104
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
4-101 7.60e-11

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 59.22  E-value: 7.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCK-AAVKQMEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEeALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTK 99
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
3-116 9.06e-11

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: 58.85  E-value: 9.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAV-KQMEYSPNVILCDVFLPDGNGVDFIKTIKKIsPESE---IILL 78
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALsKAQSKKFDLIITDQNMPNMDGIELIKELRKL-PAYKftpILML 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAM 116
Cdd:cd17562   81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
3-101 1.02e-10

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: 58.64  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAH 81
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFrEVRPDLVLLDLMLPGIDGIEVCRQIRAES-GVPIVMLTAK 80
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:cd17626   81 SDTVDVVLGLESGADDYVAK 100
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
3-120 2.13e-10

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 61.70  E-value: 2.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLE-GYEVL-QAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISP-------- 71
Cdd:PRK00742   5 RVLVVDDSAFMRRLISEILNSDpDIEVVgTAPDGLEAREKIkKLNPDVITLDVEMPVMDGLDALEKIMRLRPtpvvmvss 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 815678357  72 ----ESEIILltahgnipdgvQAIKNGAFDYITK--GDdnnkiiplISRAMEKAR 120
Cdd:PRK00742  85 lterGAEITL-----------RALELGAVDFVTKpfLG--------ISLGMDEYK 120
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1-116 4.54e-10

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: 57.18  E-value: 4.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLAriLGLE---GYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKiSPESE-- 74
Cdd:cd17552    1 SKRILVIDDEEDIREVVQ--ACLEklaGWEVLTASSGQEGLEKAAtEQPDAILLDVMMPDMDGLATLKKLQA-NPETQsi 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 815678357  75 -IILLTAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAM 116
Cdd:cd17552   78 pVILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
4-101 6.49e-10

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 56.48  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSPN---VILCDVFLPDGNGVDFIKTIKKIsPESEIILLTA 80
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDefdLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLK 100
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
4-112 7.25e-10

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 56.28  E-value: 7.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVlqagDCKAAVKQMEYSPNV-----ILCDVFLPDGNGVDFIKTIKKISPESEIILL 78
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQA----DVAESLKDGEYYIDIrnydlVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVL 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLI 112
Cdd:cd17573   77 SDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
2-101 8.50e-10

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: 56.23  E-value: 8.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   2 NKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTA 80
Cdd:cd17622    1 TRILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIArEKPDAVLLDIMLPGIDGLTLCRDLRPKY-QGPILLLTA 79
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVK 100
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
4-101 1.13e-09

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: 55.79  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIK-----KISPeseIIL 77
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLaEHRPTLVISDIVMPEMDGYELCRKIKsdpdlKDIP---VIL 77
                         90       100
                 ....*....|....*....|....
gi 815678357  78 LTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17598   78 LTTLSDPRDVIRGLECGADNFITK 101
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
4-79 1.19e-09

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 55.43  E-value: 1.19e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSPNV--ILCDVFLPDG-NGVDFIKTIKKISPESEIILLT 79
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIdlLVTDVIMPGGmNGSQLAEEARRRRPDLKVLLTS 79
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
4-101 1.26e-09

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 55.28  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYS-PNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAHG 82
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAgADIVLLDLMLPGLSGTEVCRQLRARS-NVPVIMVTAKD 79
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd17621   80 SEIDKVVGLELGADDYVTK 98
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
3-101 2.10e-09

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: 55.04  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYE-VLQAGDCKAAVKQMEY-SPNVILCDVFLPDGNGVDFIKTIKKISPESE--IILL 78
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAgGFDFVITDWNMPNMDGLELLKTIRADGALSHlpVLMV 81
                         90       100
                 ....*....|....*....|...
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVK 104
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
3-101 2.57e-09

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: 54.72  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVL-QAGDCKAAVKQ-MEYSPNVILCDVFLPDG-NGVDFIKTIKKIS--PeseIIL 77
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELaEENKPDLILMDINLKGDmDGIEAAREIREKFdiP---VIF 78
                         90       100
                 ....*....|....*....|....*
gi 815678357  78 LTAHGNiPDGVQ-AIKNGAFDYITK 101
Cdd:cd17534   79 LTAYSD-EETLErAKETNPYGYLVK 102
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
4-101 2.69e-09

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 56.96  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLE-GYEVL-QAGDCKAAVK-QMEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:PRK10651   9 ILLIDDHPMLRTGVKQLISMApDITVVgEASNGEQGIElAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSV 88
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10651  89 SNHEEDVVTALKRGADGYLLK 109
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
403-442 2.93e-09

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 52.40  E-value: 2.93e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 815678357  403 LSAMEKRHIARVLDYTNGNKTEAAKLLKIGLTTLYRKIEE 442
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
3-112 4.65e-09

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 53.99  E-value: 4.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAH 81
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMlHRRVDLVLLDLRLGQESGLDLLRTIRARS-DVPIIIISGD 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 815678357  82 -GNIPDGVQAIKNGAFDYITKGDDNNKIIPLI 112
Cdd:cd17594   80 rRDEIDRVVGLELGADDYLAKPFGLRELLARV 111
dpiA PRK10046
two-component response regulator DpiA; Provisional
4-216 6.11e-09

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 56.18  E-value: 6.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLAR-ILGLEGY-EVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:PRK10046   7 LLIVEDETPLAEMHAEyIRHIPGFsQILLAGNLAQARMMIErFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  81 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAMEKAR----TNGVKNRPEKETFQQYSFNSILGQSKPLLEAIAL-A 155
Cdd:PRK10046  87 ASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHmlesIDSASQKQIDEMFNAYARGEPKDELPTGIDPLTLnA 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815678357 156 RKVASTDVPVLLTGETgtgkevFAQA--IHHESKRNKGNFVAincsafSKELLESEIFGHKAG 216
Cdd:PRK10046 167 VRKLFKEPGVQHTAET------VAQAltISRTTARRYLEYCA------SRHLIIAEIVHGKVG 217
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
3-101 2.22e-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: 52.00  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKiSPESEIILLTAH 81
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVrHTPPDLILLDLMLPGTDGLTLCREIRR-FSDVPIIMVTAR 79
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:cd19938   80 VEEIDRLLGLELGADDYICK 99
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
4-101 2.35e-08

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: 51.89  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEG--YEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVlKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLK 101
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
4-101 4.41e-08

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 53.92  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYE---VLQAGDCKAAVKQmeYSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTA 80
Cdd:PRK10710  13 ILIVEDEPKLGQLLIDYLQAASYAttlLSHGDEVLPYVRQ--TPPDLILLDLMLPGTDGLTLCREIRRFS-DIPIVMVTA 89
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10710  90 KIEEIDRLLGLEIGADDYICK 110
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-101 7.11e-08

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 53.04  E-value: 7.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEV---LQAGDCKAAVKQMeySPNVILCDVFLPDGNGVDFIKTIKKISPESEIIL 77
Cdd:PRK11083   3 QPTILLVEDEQAIADTLVYALQSEGFTVewfERGLPALDKLRQQ--PPDLVILDVGLPDISGFELCRQLLAFHPALPVIF 80
                         90       100
                 ....*....|....*....|....
gi 815678357  78 LTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK11083  81 LTARSDEVDRLVGLEIGADDYVAK 104
PRK10643 PRK10643
two-component system response regulator PmrA;
3-101 7.47e-08

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 52.73  E-value: 7.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYevlqAGDCKAAVKQME-------YSpnVILCDVFLPDGNGVDFIKTIKKISPESEI 75
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGY----ACDCASTAREAEallesghYS--LVVLDLGLPDEDGLHLLRRWRQKKYTLPV 75
                         90       100
                 ....*....|....*....|....*.
gi 815678357  76 ILLTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10643  76 LILTARDTLEDRVAGLDVGADDYLVK 101
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
4-112 7.47e-08

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 50.49  E-value: 7.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKlYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLI 112
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDELVARI 110
PRK09483 PRK09483
response regulator; Provisional
1-102 8.55e-08

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 52.42  E-value: 8.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARIL-GLEGYEVL-QAGDCKAAVKQ-MEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIIL 77
Cdd:PRK09483   1 MINVLLVDDHELVRAGIRRILeDIKGIKVVgEACCGEDAVKWcRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIM 80
                         90       100
                 ....*....|....*....|....*
gi 815678357  78 LTAHGNIPDGVQAIKNGAFDYITKG 102
Cdd:PRK09483  81 LTVHTENPLPAKVMQAGAAGYLSKG 105
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
165-289 1.74e-07

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 49.90  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  165 VLLTGETGTGKEVFAQAIHHESKRnkgNFVAINCSAfskelLESEIFGHKAGSFtgalkdkKGLFEEAHNGT---IFLDE 241
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGA---PFIEISGSE-----LVSKYVGESEKRL-------RELFEAAKKLApcvIFIDE 65
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 815678357  242 I-----------GEMAIELQAKLLRVLEtgeyikiGETKPTSvNVRIIAATNRnlPEEI 289
Cdd:pfam00004  66 IdalagsrgsggDSESRRVVNQLLTELD-------GFTSSNS-KVIVIAATNR--PDKL 114
pleD PRK09581
response regulator PleD; Reviewed
3-101 3.04e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 52.60  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDD-EPQIRQLLARILgLEGYEVLQAGDCKAAVKQMEYS-PNVILCDVFLPDGNGVDFIKTIKKiSPESE---IIL 77
Cdd:PRK09581   4 RILVVDDiPANVKLLEAKLL-AEYYTVLTASSGAEAIAICEREqPDIILLDVMMPGMDGFEVCRRLKS-DPATThipVVM 81
                         90       100
                 ....*....|....*....|....
gi 815678357  78 LTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK09581  82 VTALDDPEDRVRGLEAGADDFLTK 105
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
4-116 3.37e-07

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: 48.88  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLE-GYEVL-QAGDCKAAVK-QMEYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDpDFTVVgEASSGEEGIElAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAM 116
Cdd:cd19931   81 SDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAA 116
PRK10766 PRK10766
two-component system response regulator TorR;
3-101 3.55e-07

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 50.81  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAH 81
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHvDLILLDINLPGEDGLMLTRELRSRS-TVGIILVTGR 82
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10766  83 TDSIDRIVGLEMGADDYVTK 102
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
3-101 3.67e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 50.69  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARIL------------GLEGYEVLQAGDCkaavkqmeyspNVILCDVFLPDGNGVDFIKTIKKIS 70
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLteagfvvdladnGLNGYHLAMTGDY-----------DLIILDIMLPDVNGWDIVRMLRSAN 70
                         90       100       110
                 ....*....|....*....|....*....|.
gi 815678357  71 PESEIILLTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK09836  71 KGMPILLLTALGTIEHRVKGLELGADDYLVK 101
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
4-98 3.89e-07

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: 48.87  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGL---EGYEVLQAGDCKAA---VKQMEYSPNVI---LCDVFLPDGNGVDFIKTIKKISPESE 74
Cdd:cd17595    3 ILTVDDDPQVLRAVARDLRRqygKDYRVLRADSGAEAldaLKELKLRGEAValfLVDQRMPEMDGVEFLEKAMELFPEAK 82
                         90       100
                 ....*....|....*....|....
gi 815678357  75 IILLTAHGNIPDGVQAIKNGAFDY 98
Cdd:cd17595   83 RVLLTAYADTDAAIRAINDVQLDY 106
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
3-82 6.75e-07

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: 47.50  E-value: 6.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSPNV--ILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIdiVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80

                 ..
gi 815678357  81 HG 82
Cdd:cd18160   81 GA 82
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
164-283 7.35e-07

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: 48.06  E-value: 7.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  164 PVLLTGETGTGK----EVFAQAIhheskrNKGNFVAINCSAFSKellESEIFGH-----KAGSFT-GALKDKkglFEEAH 233
Cdd:pfam07728   1 GVLLVGPPGTGKtelaERLAAAL------SNRPVFYVQLTRDTT---EEDLFGRrnidpGGASWVdGPLVRA---AREGE 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 815678357  234 ngTIFLDEIGEMAIELQAKLLRVLETGEYIKI---GETKPTSVNVRIIAATNR 283
Cdd:pfam07728  69 --IAVLDEINRANPDVLNSLLSLLDERRLLLPdggELVKAAPDGFRLIATMNP 119
PRK15479 PRK15479
transcriptional regulator TctD;
3-101 9.23e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 49.72  E-value: 9.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAA--VKQMEYSPNVILcDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAAdhLLQSEMYALAVL-DINMPGMDGLEVLQRLRKRGQTLPVLLLTA 80
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK15479  81 RSAVADRVKGLNVGADDYLPK 101
PRK10816 PRK10816
two-component system response regulator PhoP;
3-101 1.45e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 48.97  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAH 81
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLnEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10816  82 ESWQDKVEVLSAGADDYVTK 101
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
2-84 2.15e-06

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: 46.67  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   2 NKVLIIDDEPQIRQLLARILG-LEGYEVLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:cd17530    1 LRVLVLDDDPFQCMMAATILEdLGPGNVDEADDGREALVILLcNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80

                 ....*
gi 815678357  80 AHGNI 84
Cdd:cd17530   81 GLDGG 85
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
4-101 3.63e-06

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: 45.13  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAHG 82
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLnARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79
                         90
                 ....*....|....*....
gi 815678357  83 NIPDGVQAIKNGAFDYITK 101
Cdd:cd19936   80 DEIDEVFGLRMGADDYITK 98
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
3-101 4.66e-06

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: 45.44  E-value: 4.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQ-MEYSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAH 81
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRiIDEQPSLVVLDIMLPGMDGLTVCREVREHS-HVPILMLTAR 79
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:cd19939   80 TEEMDRVLGLEMGADDYLCK 99
PRK11517 PRK11517
DNA-binding response regulator HprR;
3-101 8.64e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 46.82  E-value: 8.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVK-QMEYSPNVILCDVFLPDGNGVDFIKTIKKiSPESEIILLTAH 81
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYlALKDDYALIILDIMLPGMDGWQILQTLRT-AKQTPVICLTAR 80
                         90       100
                 ....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITK 101
Cdd:PRK11517  81 DSVDDRVRGLDSGANDYLVK 100
PRK15369 PRK15369
two component system response regulator;
3-101 9.12e-06

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 46.61  E-value: 9.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEP----QIRQLLA-----RIL-----GLEGYEVLQAgdckaavkqmeYSPNVILCDVFLPDGNGVDFIKTIKK 68
Cdd:PRK15369   5 KILLVDDHEliinGIKNMLApypryKIVgqvdnGLEVYNACRQ-----------LEPDIVILDLGLPGMNGLDVIPQLHQ 73
                         90       100       110
                 ....*....|....*....|....*....|...
gi 815678357  69 ISPESEIILLTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK15369  74 RWPAMNILVLTARQEEHMASRTLAAGALGYVLK 106
PRK11173 PRK11173
two-component response regulator; Provisional
3-139 1.30e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 46.16  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISpESEIILLTAH 81
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILsENDINLVIMDINLPGKNGLLLARELREQA-NVALMFLTGR 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  82 GNIPDGVQAIKNGAFDYITKgddnnkiiP------------LISRAMekartNGVKNRPEKETFQQYSFN 139
Cdd:PRK11173  84 DNEVDKILGLEIGADDYITK--------PfnpreltirarnLLSRTM-----NLGTVSEERRSVESYKFN 140
PRK11697 PRK11697
two-component system response regulator BtsR;
1-101 1.44e-05

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 45.99  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEG-YEVLqaGDCKAAVKQM----EYSPNVILCDVFLPDGNGVDFIKTikkISPES-- 73
Cdd:PRK11697   1 MIKVLIVDDEPLAREELRELLQEEGdIEIV--GECSNAIEAIgaihRLKPDVVFLDIQMPRISGLELVGM---LDPEHmp 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 815678357  74 EIILLTAHgnipD--GVQAIKNGAFDYITK 101
Cdd:PRK11697  76 YIVFVTAF----DeyAIKAFEEHAFDYLLK 101
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
5-115 1.77e-05

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 45.66  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   5 LIIDDEPQIRQLLARILGLEGYEVL-QAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILaELTEGGSAVQRVEtLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKN 83
                         90       100       110
                 ....*....|....*....|....*....|...
gi 815678357  83 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRA 115
Cdd:PRK09958  84 DHFYGKHCADAGANGFVSKKEGMNNIIAAIEAA 116
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
4-101 2.09e-05

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: 43.16  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSPN---VILCDVFLPDGNGVDFIKTI--KKISPESEIILL 78
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeidLILTEVDLPVSSGFKLLSYImrHKICKNIPVIMM 80
                         90       100
                 ....*....|....*....|...
gi 815678357  79 TAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVK 103
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-101 2.26e-05

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


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 43.32  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLE-GYEVLQAGDCKAAVKQMEYSPN--VILCDVFLPDG-NG--VDFikTIKKISPeseII 76
Cdd:cd19921    1 KVLIVEDSKTFSKVLKHLIAQElGLEVDVAETLAEAKALLEEGDDyfAALVDLNLPDApNGeaVDL--VLEKGIP---VI 75
                         90       100
                 ....*....|....*....|....*..
gi 815678357  77 LLTahGNIPDGV--QAIKNGAFDYITK 101
Cdd:cd19921   76 VLT--GSFDEDKreTLLSKGVVDYVLK 100
PRK14084 PRK14084
DNA-binding response regulator;
3-122 3.00e-05

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 45.13  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEP----QIRQLLARILGLEgyEVLQAGDCKAAVKQMEY-SPNVILCDVFLPDGNGVDFIKTIKKISPESEIIL 77
Cdd:PRK14084   2 KALIVDDEPlarnELTYLLNEIGGFE--EINEAENVKETLEALLInQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIF 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 815678357  78 LTAHGNIpdGVQAIKNGAFDYITKGDDNNKIIPLISR-AMEKARTN 122
Cdd:PRK14084  80 ATAHDQF--AVKAFELNATDYILKPFEQKRIEQAVNKvRATKAKDD 123
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
166-290 3.12e-05

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 44.48  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 166 LLTGETGTGKEVFAQAIHHESKRNKGNFVAINCSAFSKELLESEIFG--------HKAGSFTGALKDKKglfeeahNGTI 237
Cdd:cd19499   45 LFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMEKHSVSRLIGappgyvgyTEGGQLTEAVRRKP-------YSVV 117
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 815678357 238 FLDEIGEMAIELQAKLLRVLETGEyIKIGETKPTSV-NVRIIAATNRNLPEEIN 290
Cdd:cd19499  118 LLDEIEKAHPDVQNLLLQVLDDGR-LTDSHGRTVDFkNTIIIMTSNHFRPEFLN 170
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
3-104 6.20e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 44.07  E-value: 6.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGLE-GYEVL-QAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELDpGFEVVaEAGDGASAIDLAnRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILT 87
                         90       100
                 ....*....|....*....|....*
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITKGDD 104
Cdd:PRK10403  88 VSDASSDVFALIDAGADGYLLKDSD 112
PRK10430 PRK10430
two-component system response regulator DcuR;
1-101 6.45e-05

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 44.33  E-value: 6.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQL----LARILGLEGYEVL----QAgdcKAAVKQMEYSPNVILCDVFLPDGNGVDFIKTIKKISPE 72
Cdd:PRK10430   1 MINVLIVDDDAMVAELnrryVAQIPGFQCCGTAstleQA---KEIIFNSDTPIDLILLDIYMQQENGLDLLPVLHEAGCK 77
                         90       100
                 ....*....|....*....|....*....
gi 815678357  73 SEIILLTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10430  78 SDVIVISSAADAATIKDSLHYGVVDYLIK 106
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
165-289 8.48e-05

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 42.66  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 165 VLLTGETGTGKEVFAQAIHHESKRnkgNFVAINCSAF-SKELLESEIFGHKagsftgalkdkkgLFEEAHN---GTIFLD 240
Cdd:cd19481   29 ILLYGPPGTGKTLLAKALAGELGL---PLIVVKLSSLlSKYVGESEKNLRK-------------IFERARRlapCILFID 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815678357 241 EI------------GEMAIELQAKLLRVLETGEyikigetkpTSVNVRIIAATNRnlPEEI 289
Cdd:cd19481   93 EIdaigrkrdssgeSGELRRVLNQLLTELDGVN---------SRSKVLVIAATNR--PDLL 142
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
165-289 1.45e-04

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 42.28  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 165 VLLTGETGTGKEVFAQAIHHESkrnKGNFVAINC-SAFSKELLESEifghkagsftgalKDKKGLFEEAHNGT---IFLD 240
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEA---GANFLSISGpSIVSKYLGESE-------------KNLREIFEEARSHApsiIFID 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 241 EI-----------GEMAIELQAKLLRVLETgeyikIGETKptsvNVRIIAATNRnlPEEI 289
Cdd:cd19503  101 EIdalapkreedqREVERRVVAQLLTLMDG-----MSSRG----KVVVIAATNR--PDAI 149
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
4-101 1.91e-04

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: 40.81  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARIL------------GLEGYEVLQAGDCKAAVKQMEYSPNVILCDVFLPDGNGVDFIKTIKKISP 71
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLrisscrvtavdsGKRALEFLGLEDEEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 815678357  72 ESEI-ILLTAHGNIPDGV-QAIKNGAFDYITK 101
Cdd:cd17581   81 LKEIpVVIMSSENIPTRIsRCLEEGAEDFLLK 112
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
165-316 2.19e-04

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 43.07  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 165 VLLTGETGTGKEVFAQAIHHESKRnkgNFVAINCSAF-SKELLESEIfghkagsftgALKDkkgLFEEAHNGT---IFLD 240
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAGELGA---PFIRVRGSELvSKYIGEGAR----------NVRE---VFELAREKApsiIFID 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 241 EIGemAIelqAKllRVLETGEyikIGETK-------------PTSVNVRIIAATNRnlPEEINA-----GHFREDLFY-- 300
Cdd:COG1222  179 EID--AI---AA--RRTDDGT---SGEVQrtvnqllaeldgfESRGDVLIIAATNR--PDLLDPallrpGRFDRVIEVpl 246
                        170       180
                 ....*....|....*....|.
gi 815678357 301 -----RLSVFQIHlppLRERP 316
Cdd:COG1222  247 pdeeaREEILKIH---LRDMP 264
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
165-321 2.78e-04

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 42.98  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 165 VLLTGETGTGKEVFAQAIHHESkrnKGNFVAINCSA-FSKELLESEIfghkagsftgALKDkkgLFEEAH---NGTIFLD 240
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSDlVSKYVGETEK----------NLRE---VFDKARglaPCVLFID 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 241 EI-----------GEMAIELQAKLLRVLETGEYikigetkptsvNVRIIAATNRnlPEEINAGHFR--EDLFY------- 300
Cdd:COG0464  258 EAdalagkrgevgDGVGRRVVNTLLTEMEELRS-----------DVVVIAATNR--PDLLDPALLRrfDEIIFfplpdae 324
                        170       180
                 ....*....|....*....|..
gi 815678357 301 -RLSVFQIHLPPlRERPGDIRL 321
Cdd:COG0464  325 eRLEIFRIHLRK-RPLDEDVDL 345
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
3-101 2.78e-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: 40.28  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARILGL-EGYEVL-QAGDCKAAVKQM-EYSPNVILCDVFLP--DGNGVdfIKTI--KKISPESEI 75
Cdd:cd17561    3 KVLIADDNREFVQLLEEYLNSqPDMEVVgVAHNGQEALELIeEKEPDVLLLDIIMPhlDGIGV--LEKLrrMRLEKRPKI 80
                         90       100
                 ....*....|....*....|....*.
gi 815678357  76 ILLTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:cd17561   81 IMLTAFGQEDITQRAVELGASYYILK 106
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
165-302 2.84e-04

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 41.11  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 165 VLLTGETGTGKEVFAQAIHHESKRnkgNFVAINCSA-FSKELLESEifghkagsftGALKDkkgLFEEAHNGT---IFLD 240
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGL---NFISVKGPElFSKYVGESE----------RAVRE---IFQKARQAApciIFFD 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 241 EI--------GEMAIELQAKLLRVLETgEYIKIGETKptsvNVRIIAATNRnlPEEINAGHFREDLFYRL 302
Cdd:cd19511   94 EIdslaprrgQSDSSGVTDRVVSQLLT-ELDGIESLK----GVVVIAATNR--PDMIDPALLRPGRLDKL 156
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1-101 4.14e-04

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 41.93  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVL--QAGDCKAAVKQMEySPNVILCDVFLPdgnGVDFIKTIKKISP--ESEII 76
Cdd:PRK10701   1 MNKIVFVEDDAEVGSLIAAYLAKHDIDVTvePRGDRAEATILRE-QPDLVLLDIMLP---GKDGMTICRDLRPkwQGPIV 76
                         90       100
                 ....*....|....*....|....*
gi 815678357  77 LLTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10701  77 LLTSLDSDMNHILALEMGACDYILK 101
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
4-102 8.25e-04

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: 38.90  E-value: 8.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQME----YSPNV------ILCDVFLPDGNGVDFIKTIKKiSPES 73
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakEGNDLskeldlIITDIEMPKMDGYELTFELRD-DPRL 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 815678357  74 E---IILLTAHGNIPDGVQAIKNGAFDYITKG 102
Cdd:cd19924   80 AnipVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10360 PRK10360
transcriptional regulator UhpA;
1-101 1.06e-03

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 39.96  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEG--YEVLQAGDCKAAVKQMEYS-PNVILCDVFLPDGNGVDFIKTIKKispESEIIL 77
Cdd:PRK10360   1 MITVALIDDHLIVRSGFAQLLGLEPdlQVVAEFGSGREALAGLPGRgVQVCICDISMPDISGLELLSQLPK---GMATIM 77
                         90       100
                 ....*....|....*....|....
gi 815678357  78 LTAHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK10360  78 LSVHDSPALVEQALNAGARGFLSK 101
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
4-82 2.45e-03

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 40.49  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357    4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLTAHG 82
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHyDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
4-101 3.06e-03

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 37.24  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQ----AGDCKAAVKQMEYspNVILCDVFLPDG-NG---VDFIKTIKKISPESEI 75
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGVTRIDtassGEEALRMCENKTY--DIVLCDYNLGKGkNGqqlLEELRHKKLISPSTVF 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 815678357  76 ILLTAhgnipDGVQAIKNGAF-----DYITK 101
Cdd:cd17589   79 IMVTG-----ESSRAMVLSALelepdDYLLK 104
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
3-122 3.58e-03

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 37.60  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLL----ARILGLEGYE-----VLQAGDCKAAVKQME-YSPNVILCDVFLPDGNGVDFIKTIKKISPE 72
Cdd:cd17533    2 NIFILEDDKIQRVRLeeiiENILKIENIEyvielTGKTEELLEKIKERGkNGIYFLDIDIKMEEKNGLEVAQKIRKYDPY 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 815678357  73 SEIILLTAHGN-IPDGVQaIKNGAFDYITKGDDNNKIIPLISRAMEKARTN 122
Cdd:cd17533   82 AIIIFVTTHSEfAPLTFE-YKVAALDFILKPLKLEEFKKRIEECIKYAQKN 131
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
165-302 3.90e-03

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 37.86  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357 165 VLLTGETGTGKEVFAQAIHHESkrnKGNFVAINC-SAFSKELLESEifghkagsftgalKDKKGLFEEAHNGT---IFLD 240
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATES---NANFISVKGpELLSKWVGESE-------------KAIREIFRKARQVApcvIFFD 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815678357 241 EIGEMAIE------------LQAKLLRVLETGEYIKigetkptsvNVRIIAATNRnlPEEINAGHFREDLFYRL 302
Cdd:cd19529   94 EIDSIAPRrgttgdsgvterVVNQLLTELDGLEEMN---------GVVVIAATNR--PDIIDPALLRAGRFDRL 156
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
3-114 4.57e-03

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: 36.75  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   3 KVLIIDDEPQIRQLLARIL-GLEGYEVLQAGDCKAAVKQM-EYSPNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTa 80
Cdd:cd17593    2 KVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILrEGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS- 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 815678357  81 hGNI-PDGVQ-AIKNGAFDYITKGDDNNKIIPLISR 114
Cdd:cd17593   81 -GDVqPEAKErVLELGALAFLKKPFDPEKLAQLLEE 115
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1-101 5.07e-03

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 38.64  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   1 MNKVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLT 79
Cdd:PRK13856   1 MKHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETvDVVVVDLNLGREDGLEIVRSLATKSDVPIIIISG 80
                         90       100
                 ....*....|....*....|..
gi 815678357  80 AHGNIPDGVQAIKNGAFDYITK 101
Cdd:PRK13856  81 DRLEEADKVVALELGATDFIAK 102
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
3-80 5.45e-03

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 39.19  E-value: 5.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815678357   3 KVLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAVKQMEYSP-NVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:PRK10841 803 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHiDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTA 881
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
4-101 6.75e-03

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


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 36.30  E-value: 6.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357   4 VLIIDDEPQIRQLLARILGLEGYEVLQAGDCKAAV---KQMEYspNVILCDVFLPDGNGVDFIKTIKKISPESEIILLTA 80
Cdd:cd19922    1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALslaLETDY--DLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDH 78
                         90       100
                 ....*....|....*....|.
gi 815678357  81 HGNIPDGVQAIKNGAFDYITK 101
Cdd:cd19922   79 WEDLQEELEEVQRFAVSYVVK 99
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
165-311 8.11e-03

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 38.73  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815678357  165 VLLTGETGTGKEVFAQAIHHESkrnKGNFVAINC-SAFSKELLESEifghkagsftgalKDKKGLFEEAHNGT---IFLD 240
Cdd:TIGR01243 490 VLLFGPPGTGKTLLAKAVATES---GANFIAVRGpEILSKWVGESE-------------KAIREIFRKARQAApaiIFFD 553
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815678357  241 EIGEMA----IELQAKLLRVLETGEYIKIGETKPTSvNVRIIAATNRnlPEEINAGHFREDLFYRLsvfqIHLPP 311
Cdd:TIGR01243 554 EIDAIApargARFDTSVTDRIVNQLLTEMDGIQELS-NVVVIAATNR--PDILDPALLRPGRFDRL----ILVPP 621
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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