NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495938351|ref|WP_008662930|]
View 

MULTISPECIES: sigma-54 dependent transcriptional regulator [Bacteroides]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-445 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: 534.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVRLEKLekkvgqtysfDSILGESKVLKDAVSLAQKVS 160
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAED----------SGLIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 161 GTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFL 240
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 241 DEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDI 320
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 321 RLLAKAFIKSFAEQLARPVVeIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDiqnahyehsndssp 400
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA-------------- 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 495938351 401 gsfeLSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEY 445
Cdd:COG2204  377 ----LEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-445 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: 534.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVRLEKLekkvgqtysfDSILGESKVLKDAVSLAQKVS 160
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAED----------SGLIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 161 GTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFL 240
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 241 DEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDI 320
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 321 RLLAKAFIKSFAEQLARPVVeIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDiqnahyehsndssp 400
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA-------------- 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 495938351 401 gsfeLSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEY 445
Cdd:COG2204  377 ----LEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
3-447 7.14e-135

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 395.76  E-value: 7.14e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVRLEKLEKKVGQTYSFDSILGESKVLKDAVSLAQKVSGT 162
Cdd:PRK11361  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 163 DVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDE 242
Cdd:PRK11361 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 243 IGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRL 322
Cdd:PRK11361 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 323 LAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDIQN--AHYEHSNDSSP 400
Cdd:PRK11361 326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQpvCNAGEVKTAPV 405
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495938351 401 GSFELSAM----ERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEYKI 447
Cdd:PRK11361 406 GERNLKEEikrvEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-444 1.39e-122

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: 364.83  E-value: 1.39e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351    4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVrleKLEKKVGQTYSFDSILGESKVLKDAVSLAQKVSGTD 163
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQV---ALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  164 VPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEI 243
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  244 GEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLL 323
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  324 AKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDIQNAHYEHSNDSSPGSF 403
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQD 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495938351  404 ELSAMERRHIARV------------------------LEYTKGNKTEAARLLKIGLTTLYRKIEE 444
Cdd:TIGR01818 398 SWDEALEAWAKQAlsrgeqglldralpeferplleaaLQHTRGHKQEAAALLGWGRNTLTRKLKE 462
Sigma54_activat pfam00158
Sigma-54 interaction domain;
142-309 1.39e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 302.78  E-value: 1.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  142 ILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTG 221
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  222 ALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFY 301
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 495938351  302 RLSVFQIH 309
Cdd:pfam00158 161 RLNVIPIE 168
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
129-440 8.62e-93

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 290.24  E-value: 8.62e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 129 LEKKVGQTYSFDSILGESKVLKDAVSLAQKVSGTD-VPVLLTGETGTGKEVFAQAIHYSSKRARQ---NFVAVNCSSFSK 204
Cdd:NF038308 168 REQAEAVSFLKSGIATRNAAFNRLIEQIERVALRSrAPILLTGPTGAGKSFLARRIYELKKRRHQvsgPFVEVNCATLRG 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 205 ELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNR 284
Cdd:NF038308 248 DLAMSELFGHVKGAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNR 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 285 NLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPV---VEIAPAFL--EALDSQPWKGNI 359
Cdd:NF038308 328 DLRQEVAEGRFREDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRQVrfnKEARFRYLafATSPEALWPGNF 407
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 360 RELRNVIERSMIVCESGYLDIADLPFDI-----QNAHYEHSNDSSPGSFELSA-----------MERRHIARVLEYTKGN 423
Cdd:NF038308 408 RELSASVTRMATLADGGRITEELVEEEIarlraAWQSAPAAADDDALADLLGGeqlaeldlfdrVQLAAVLRVCRQSRSL 487
                        330
                 ....*....|....*..
gi 495938351 424 KTEAARLLKIGLTTLYR 440
Cdd:NF038308 488 SAAGRRLFGVSRQQKAS 504
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
4-122 9.76e-34

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: 122.98  E-value: 9.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARM 122
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRL 119
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
3-56 7.91e-13

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 62.97  E-value: 7.91e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 495938351     3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLP 56
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-445 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: 534.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVRLEKLekkvgqtysfDSILGESKVLKDAVSLAQKVS 160
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAED----------SGLIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 161 GTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFL 240
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 241 DEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDI 320
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 321 RLLAKAFIKSFAEQLARPVVeIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDiqnahyehsndssp 400
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA-------------- 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 495938351 401 gsfeLSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEY 445
Cdd:COG2204  377 ----LEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
117-448 1.26e-169

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: 483.89  E-value: 1.26e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 117 VEKARMNVRLEKLEKKVGQTYSFDSILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVA 196
Cdd:COG3829  115 LKRLERKLREEELERGLSAKYTFDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 197 VNCSSFSKELLESEMFGHKAGSFTGALK-DKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVN 275
Cdd:COG3829  195 VNCAAIPENLLESELFGYEKGAFTGAKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVD 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 276 VRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPVVEIAPAFLEALDSQPW 355
Cdd:COG3829  275 VRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDW 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 356 KGNIRELRNVIERSMIVCESGYLDIADLPFDIQNAHyEHSNDSSPGSFE--LSAMERRHIARVLEYTKGNKTEAARLLKI 433
Cdd:COG3829  355 PGNVRELENVIERAVVLSEGDVITPEHLPEYLLEEA-EAASAAEEGSLKeaLEEVEKELIEEALEKTGGNKSKAAKALGI 433
                        330
                 ....*....|....*
gi 495938351 434 GLTTLYRKIEEYKIS 448
Cdd:COG3829  434 SRSTLYRKLKKYGIK 448
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
3-447 7.14e-135

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 395.76  E-value: 7.14e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVRLEKLEKKVGQTYSFDSILGESKVLKDAVSLAQKVSGT 162
Cdd:PRK11361  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 163 DVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDE 242
Cdd:PRK11361 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 243 IGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRL 322
Cdd:PRK11361 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 323 LAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDIQN--AHYEHSNDSSP 400
Cdd:PRK11361 326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQpvCNAGEVKTAPV 405
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495938351 401 GSFELSAM----ERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEYKI 447
Cdd:PRK11361 406 GERNLKEEikrvEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
137-446 1.67e-133

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 398.12  E-value: 1.67e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 137 YSFDSILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKA 216
Cdd:COG3284  318 AALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEP 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 217 GSFTGALKD-KKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRF 295
Cdd:COG3284  398 GAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRF 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 296 REDLFYRLSVFQIHLPPLRERAgDIRLLAKAFIKSFAEqlARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCES 375
Cdd:COG3284  478 REDLYYRLNGLTLTLPPLRERE-DLPALIEHLLRELAA--GRGPLRLSPEALALLAAYPWPGNVRELRNVLRTALALADG 554
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495938351 376 GYLDIADLPFDIQNAHYEHSNDSSPGSFELSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEYK 446
Cdd:COG3284  555 GVITVEDLPDELRAELAAAAPAAAAPLTSLEEAERDAILRALRACGGNVSAAARALGISRSTLYRKLKRYG 625
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-444 1.39e-122

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: 364.83  E-value: 1.39e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351    4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVrleKLEKKVGQTYSFDSILGESKVLKDAVSLAQKVSGTD 163
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQV---ALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  164 VPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEI 243
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  244 GEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLL 323
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  324 AKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDIQNAHYEHSNDSSPGSF 403
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQD 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495938351  404 ELSAMERRHIARV------------------------LEYTKGNKTEAARLLKIGLTTLYRKIEE 444
Cdd:TIGR01818 398 SWDEALEAWAKQAlsrgeqglldralpeferplleaaLQHTRGHKQEAAALLGWGRNTLTRKLKE 462
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
3-444 2.48e-110

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 333.38  E-value: 2.48e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:PRK10923   5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEkarmNVRLEKLEKKVGQTYSFDSILGESKVLKDAVSLAQKVSGT 162
Cdd:PRK10923  85 SDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIS----HYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 163 DVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDE 242
Cdd:PRK10923 161 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 243 IGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRL 322
Cdd:PRK10923 241 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 323 LAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDIQNAHY-EHSNDSSPG 401
Cdd:PRK10923 321 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVpESTSQMQPD 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495938351 402 SFE----------------------LSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEE 444
Cdd:PRK10923 401 SWAtllaqwadralrsghqnllseaQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKE 465
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-442 1.28e-109

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 330.84  E-value: 1.28e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIipliSRAVEKARMNVRLEKLEKKVGQTYSFdSILGESKVLKDAVSLAQKVSGTD 163
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNL----QATLEKALAHTHSIDAETPAVTASQF-GMVGKSPAMQHLLSEIALVAPSE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 164 VPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEI 243
Cdd:PRK10365 163 ATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 244 GEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLL 323
Cdd:PRK10365 243 GDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 324 AKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDIQNA--HYEHSNDSSPg 401
Cdd:PRK10365 323 AGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTpiPLGQSQDIQP- 401
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 495938351 402 sfeLSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKI 442
Cdd:PRK10365 402 ---LVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
4-448 1.56e-107

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 325.55  E-value: 1.56e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351    4 ILIIDDEVQIRTLLTrmMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLP-DGNGVDLVLA----IKKAAPNVEVIL 78
Cdd:TIGR02915   1 LLIVEDDLGLQKQLK--WSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPpDADGASEGLAalqqILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   79 LTAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVRLEKLEKKVGQTySFDSILGESKVLKDAVSLAQK 158
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGT-ALRGLITSSPGMQKICRTIEK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  159 VSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTI 238
Cdd:TIGR02915 158 IAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  239 FLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAG 318
Cdd:TIGR02915 238 FLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  319 DIRLLAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDiqnahyEHSNDS 398
Cdd:TIGR02915 318 DAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLGLD------ARERAE 391
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495938351  399 SPGSFELSAM----ERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEYKIS 448
Cdd:TIGR02915 392 TPLEVNLREVreraEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGIK 445
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
120-448 4.38e-107

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 326.76  E-value: 4.38e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 120 ARMNVRLEKLekKVGQTYSFDSILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNC 199
Cdd:COG3283  186 ARLGEQLQAL--QVNDDSGFDHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNC 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 200 SSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRII 279
Cdd:COG3283  264 AALPDDVAESELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVI 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 280 AATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNI 359
Cdd:COG3283  344 CATQKDLAELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNV 423
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 360 RELRNVIERSMIVCESGYLDIADLPFDIQNAHYEHSNDSSPGSFElSAMER--RHIARVL--EYTKGNKTeAARLlkiGL 435
Cdd:COG3283  424 RQLENALYRAVSLLEGDELTPEDLQLPEYAASAGLLDDLLEGSLD-EIVKRfeRSLLRRLypSYPSTRKL-AKRL---GV 498
                        330
                 ....*....|....*
gi 495938351 436 --TTLYRKIEEYKIS 448
Cdd:COG3283  499 shTAIANKLREYGIG 513
Sigma54_activat pfam00158
Sigma-54 interaction domain;
142-309 1.39e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 302.78  E-value: 1.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  142 ILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTG 221
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  222 ALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFY 301
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 495938351  302 RLSVFQIH 309
Cdd:pfam00158 161 RLNVIPIE 168
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
91-440 2.13e-99

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 306.71  E-value: 2.13e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  91 AIKNGAFDYITkgDDNNKIIPLISRAVekARMNVRLEKLEKK------VGQTYSFDS-----ILGESKV---LKDAVSLa 156
Cdd:PRK05022 131 ALDPGQFDAFS--DEELRALAALAAAT--LRNALLIEQLESQaelpqdVAEFLRQEAlkegeMIGQSPAmqqLKKEIEV- 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 157 qkVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNG 236
Cdd:PRK05022 206 --VAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGG 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 237 TIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRER 316
Cdd:PRK05022 284 TLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRER 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 317 AGDIRLLAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGY------LDIADLPFDIQNA 390
Cdd:PRK05022 364 GDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVISRAALLARARGagrivtLEAQHLDLPAEVA 443
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495938351 391 HYEHSNDSSPGSFE-------LSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYR 440
Cdd:PRK05022 444 LPPPEAAAAPAAVVsqnlreaTEAFQRQLIRQALAQHQGNWAAAARALELDRANLHR 500
PRK15115 PRK15115
response regulator GlrR; Provisional
2-440 3.41e-99

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 304.07  E-value: 3.41e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:PRK15115   6 AHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  82 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEkarmnvrlekLEKKVGQTYSFDSILGESKVLKDAVSLAQKVSG 161
Cdd:PRK15115  86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALE----------QSAPATDERWREAIVTRSPLMLRLLEQARMVAQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 162 TDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLD 241
Cdd:PRK15115 156 SDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 242 EIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIR 321
Cdd:PRK15115 236 EIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 322 LLAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIAdlpfdIQNAHYEHSNDSSPG 401
Cdd:PRK15115 316 LLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDA-----LVEQALEGENTALPT 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 495938351 402 SFELSA-MERRHIARVLEYTKGNKTEAARLLKIGLTTLYR 440
Cdd:PRK15115 391 FVEARNqFELNYLRKLLQITKGNVTHAARMAGRNRTEFYK 430
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
116-436 1.73e-97

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: 302.79  E-value: 1.73e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  116 AVEKARMNVRLEKLEKKV--GQTYSFDSILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQN 193
Cdd:TIGR01817 170 IAEAVQLSKQLRDKAPEIarRRSGKEDGIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRP 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  194 FVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTR 273
Cdd:TIGR01817 250 FVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLK 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  274 VNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPvVEIAPAFLEALDSQ 353
Cdd:TIGR01817 330 VDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRP-LTITPSAIRVLMSC 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  354 PWKGNIRELRNVIERSMIVCESGYLDIADLPFD------------------IQNAHYEHSNDSSPGSFELSAM------- 408
Cdd:TIGR01817 409 KWPGNVRELENCLERTATLSRSGTITRSDFSCQsgqclspmlaktcphghiSIDPLAGTTPPHSPASAALPGEpglsgpt 488
                         330       340       350
                  ....*....|....*....|....*....|
gi 495938351  409 --ERRHIARVLEYTKGNKTEAARLLkiGLT 436
Cdd:TIGR01817 489 lsERERLIAALEQAGWVQAKAARLL--GMT 516
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
129-440 8.62e-93

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 290.24  E-value: 8.62e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 129 LEKKVGQTYSFDSILGESKVLKDAVSLAQKVSGTD-VPVLLTGETGTGKEVFAQAIHYSSKRARQ---NFVAVNCSSFSK 204
Cdd:NF038308 168 REQAEAVSFLKSGIATRNAAFNRLIEQIERVALRSrAPILLTGPTGAGKSFLARRIYELKKRRHQvsgPFVEVNCATLRG 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 205 ELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNR 284
Cdd:NF038308 248 DLAMSELFGHVKGAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNR 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 285 NLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPV---VEIAPAFL--EALDSQPWKGNI 359
Cdd:NF038308 328 DLRQEVAEGRFREDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRQVrfnKEARFRYLafATSPEALWPGNF 407
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 360 RELRNVIERSMIVCESGYLDIADLPFDI-----QNAHYEHSNDSSPGSFELSA-----------MERRHIARVLEYTKGN 423
Cdd:NF038308 408 RELSASVTRMATLADGGRITEELVEEEIarlraAWQSAPAAADDDALADLLGGeqlaeldlfdrVQLAAVLRVCRQSRSL 487
                        330
                 ....*....|....*..
gi 495938351 424 KTEAARLLKIGLTTLYR 440
Cdd:NF038308 488 SAAGRRLFGVSRQQKAS 504
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
116-444 2.59e-84

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 268.51  E-value: 2.59e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 116 AVEKARMnVRLEKLEKKVGQT----YSFDSILGESKVL---KDAVSLAQKVSGTdvpVLLTGETGTGKEVFAQAIH---- 184
Cdd:PRK15424 192 ALDMTRM-TLRHNTHYATRNAlrtrYVLGDLLGQSPQMeqvRQTILLYARSSAA---VLIQGETGTGKELAAQAIHreyf 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 185 ----YSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSFTGALKD-KKGLFEEANNGTIFLDEIGEMAFELQAKLLRILE 259
Cdd:PRK15424 268 arhdARQGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGgRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLE 347
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 260 TGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPV 339
Cdd:PRK15424 348 EKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALSAPF 427
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 340 VEIAPAFL----EALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFdIQNAHYEHSNDSSpgSFELSAMERRHIAR 415
Cdd:PRK15424 428 SAALRQGLqqceTLLLHYDWPGNVRELRNLMERLALFLSVEPTPDLTPQF-LQLLLPELARESA--KTPAPRLLAATLQQ 504
                        330       340
                 ....*....|....*....|....*....
gi 495938351 416 VLEYTKGNKTEAARLLKIGLTTLYRKIEE 444
Cdd:PRK15424 505 ALERFNGDKTAAANYLGISRTTLWRRLKA 533
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
137-443 1.34e-83

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: 266.34  E-value: 1.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  137 YSFDSILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKA 216
Cdd:TIGR02329 209 YRLDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEE 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  217 GSFTGALKD-KKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRF 295
Cdd:TIGR02329 289 GAFTGARRGgRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRF 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  296 REDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPVVEIA----PAFLEALDSQPWKGNIRELRNVIERsmI 371
Cdd:TIGR02329 369 RRDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPDSEAAaqvlAGVADPLQRYPWPGNVRELRNLVER--L 446
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495938351  372 VCESGYLDIADLPFD-IQNAHYEHSNDSSPGSFE-LSAMERRH-----IARVLEYTKGNKTEAARLLKIGLTTLYRKIE 443
Cdd:TIGR02329 447 ALELSAMPAGALTPDvLRALAPELAEASGKGKTSaLSLRERSRvealaVRAALERFGGDRDAAAKALGISRTTLWRRLK 525
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
168-448 1.12e-82

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: 258.24  E-value: 1.12e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 168 LTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESemfghkagsftgalkdkkglfeeanngtifldeigema 247
Cdd:COG3604  120 ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 248 felqakllriLETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLLAKAF 327
Cdd:COG3604  162 ----------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHF 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 328 IKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLDIADLPFDIQNAhyehsndsspgsfeLSA 407
Cdd:COG3604  232 LEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGSREA--------------LEE 297
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 495938351 408 MERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEYKIS 448
Cdd:COG3604  298 VEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
PRK10820 PRK10820
transcriptional regulator TyrR;
120-448 3.36e-80

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 257.31  E-value: 3.36e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 120 ARMNVRLEKLekKVGQTYSFDSILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNC 199
Cdd:PRK10820 186 ARMGRQLQNL--AVNDDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNC 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 200 SSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRII 279
Cdd:PRK10820 264 ASIPDDVVESELFGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVI 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 280 AATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNI 359
Cdd:PRK10820 344 CATQKNLVELVQKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNV 423
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 360 RELRNVIERSMIVCESGYL---DIaDLP-FDIQNAH----YEHSNDSSPGSFELSAMERRHiarvLEYTKGNKTeaARLL 431
Cdd:PRK10820 424 RQLKNAIYRALTQLEGYELrpqDI-LLPdYDAAVAVgedaMEGSLDEITSRFERSVLTRLY----RNYPSTRKL--AKRL 496
                        330
                 ....*....|....*..
gi 495938351 432 KIGLTTLYRKIEEYKIS 448
Cdd:PRK10820 497 GVSHTAIANKLREYGLS 513
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
139-447 1.50e-75

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 249.36  E-value: 1.50e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 139 FDSILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGS 218
Cdd:PRK15429 375 FGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGA 454
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 219 FTGALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFRED 298
Cdd:PRK15429 455 FTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSD 534
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 299 LFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYL 378
Cdd:PRK15429 535 LYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVL 614
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495938351 379 DIAdLPfDIQNAhyehSNDSSPGSFELSAM---ERRHIARVLEYTKG---NKTEAARLLKIGLTTLYRKIEEYKI 447
Cdd:PRK15429 615 QLS-LP-DITLP----EPETPPAATVVAQEgedEYQLIVRVLKETNGvvaGPKGAAQRLGLKRTTLLSRMKRLGI 683
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
63-447 8.80e-75

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 246.13  E-value: 8.80e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  63 LVLAIKKAAP--NVEVILLTAHGNIpDGVQAIKngafdyITKGDDNNKIIPLIsRAVEKARmnvrlEKLEKKVGQT-YSF 139
Cdd:PRK11388 258 LQQAIKQAHPlkHVEVTFESQGQFI-DAVITLK------PIIEGQGTSFILLL-HPVEQMR-----QLMTSQLGKVsHTF 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 140 DSILGESKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHKAGSF 219
Cdd:PRK11388 325 DHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLGSDRTDS 404
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 220 TGALKDKkglFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDL 299
Cdd:PRK11388 405 ENGRLSK---FELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQL 481
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 300 FYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFaEQLARPVVEIAPAFLEALDSQPWKGNIRELRNVIERSMIVCESGYLD 379
Cdd:PRK11388 482 YYALHAFEITIPPLRMRREDIPALVNNKLRSL-EKRFSTRLKIDDDALARLVSYRWPGNDFELRSVIENLALSSDNGRIR 560
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 380 IADLPFDIQNAHYEHSNDSSPGSFELS--AMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEYKI 447
Cdd:PRK11388 561 LSDLPEHLFTEQATDDVSATRLSTSLSlaELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGI 630
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
140-436 1.46e-70

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 226.48  E-value: 1.46e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 140 DSILGES----KVLKDAVSLAQkvsgTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHK 215
Cdd:PRK11608   6 DNLLGEAnsflEVLEQVSRLAP----LDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 216 AGSFTGALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRF 295
Cdd:PRK11608  82 AGAFTGAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 296 REDLFYRLSVFQIHLPPLRERAGDIRLLAKAFIKSFAEQLARPVVeiaPAFLEA----LDSQPWKGNIRELRNVIERSMI 371
Cdd:PRK11608 162 RADLLDRLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLPLF---PGFTERaretLLNYRWPGNIRELKNVVERSVY 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495938351 372 --VCESGYLD--IADlPFDIQNAHYEH---SNDSSPG-SFEL----SAMERRHIARVLEYTKGNKTEAARLLkiGLT 436
Cdd:PRK11608 239 rhGTSEYPLDniIID-PFKRRPAEEAIavsETTSLPTlPLDLrewqHQQEKELLQRSLQQAKFNQKRAAELL--GLT 312
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
165-381 7.09e-45

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: 163.85  E-value: 7.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 165 PVLLTGETGTGKEVFAQAIhYSSKRARQ----NFVAVNCSSFSKELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFL 240
Cdd:COG4650  210 PILLTGPTGAGKSQLARRI-YELKKARHqvsgRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGLLRSADGGVLFL 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 241 DEIGEMAFELQAKLLRILETGEYIKIGDTKPTRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPLRERAGDI 320
Cdd:COG4650  289 DEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPGLAERREDI 368
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495938351 321 R-----LLAKafiksFAEQLARPV---VEIAPAFLE-ALDSQ-PWKGNIRELRNVIERSMIVCESGYLDIA 381
Cdd:COG4650  369 EpnldyELAR-----FAREQGRRVrfnKEARARYLAfATSPEaLWSGNFRDLNASVTRMATLAEGGRITVA 434
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
126-389 1.84e-38

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: 148.72  E-value: 1.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 126 LEKLEKKVGQTYSFDSILGESKVLKDAVSLAqKVS------GtdVPVLLTGETGTGKEVFAQAIH-Y--SSKRARQN--F 194
Cdd:COG1221   90 LAEKENNEEEEDPFDNLIGANGSLKNAIEQA-KAAilyppkG--LHTLILGPTGVGKSFFAELMYeYaiEIGVLPEDapF 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 195 VAVNCSSFS--KELLESEMFGHKAGSFTGALKDKKGLFEEANNGTIFLDEIGEMAFELQAKLLRILETGEYIKIGDTKPT 272
Cdd:COG1221  167 VVFNCADYAnnPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGETEKT 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 273 R-VNVRIIAATNRNLSQeivagrfredlfYRLSVF------QIHLPPLRERAGDIRL-LAKAFIKSFAEQLARPVVeIAP 344
Cdd:COG1221  247 RkANVRIIFATTEDPES------------SLLKTFlrripmVIKLPSLEERSLEERLeLIKHFFKEEAKRLNKPIK-VSK 313
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495938351 345 AFLEALDSQPWKGNIRELRNVIErsmIVCESGYL------------DIADLPFDIQN 389
Cdd:COG1221  314 EVLKALLLYDCPGNIGQLKSDIQ---LACAKAFLnyitnkkeeieiTLSDLPENVKK 367
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
4-122 9.76e-34

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: 122.98  E-value: 9.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARM 122
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRL 119
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
4-118 6.47e-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: 6.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVE 118
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1-102 5.24e-28

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: 110.05  E-value: 5.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTK 102
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
4-102 5.41e-28

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 106.85  E-value: 5.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351    4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90
                  ....*....|....*....
gi 495938351   84 NIPDGVQAIKNGAFDYITK 102
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSK 99
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
5-102 1.70e-27

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 105.39  E-value: 1.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   5 LIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHGN 84
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*...
gi 495938351  85 IPDGVQAIKNGAFDYITK 102
Cdd:cd00156   81 EEDAVRALELGADDYLVK 98
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
2-121 2.12e-26

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 105.00  E-value: 2.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:COG4567    5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTG 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495938351  82 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKAR 121
Cdd:COG4567   85 YASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAP 124
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-102 5.54e-26

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 102.36  E-value: 5.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMME-LEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVIL 78
Cdd:COG4565    3 MIRVLIVEDDPMVAELLRRYLErLPGFEVVgVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIV 82
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIK 106
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
3-102 2.44e-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: 2.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMME-LEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEwEAGFEVVgEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:COG4753   81 GYSDFEYAQEAIKLGADDYLLK 102
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
160-304 3.37e-25

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: 100.68  E-value: 3.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 160 SGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESEMFGHkagsftGALKDKKGLFEEANNGTIF 239
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGH------FLVRLLFELAEKAKPGVLF 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495938351 240 LDEIGEMAFELQAKLLRILETGEyikigDTKPTRVNVRIIAATNRNLSqeivaGRFREDLFYRLS 304
Cdd:cd00009   90 IDEIDSLSRGAQNALLRVLETLN-----DLRIDRENVRVIGATNRPLL-----GDLDRALYDRLD 144
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
3-102 5.29e-25

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 98.81  E-value: 5.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGA 81
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:cd17555   82 GVMSDAVEALRLGAWDYLTK 101
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
3-130 9.91e-25

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: 101.78  E-value: 9.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKK--AAPNVEVILLT 80
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRAdpSTRDIPVIFLT 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARMNVRLEKLE 130
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLV 137
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
3-121 2.07e-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: 97.61  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKK--AAPNVEVILLT 80
Cdd:COG0784    7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRAlpRLPDIPIIALT 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKAR 121
Cdd:COG0784   87 AYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
3-102 2.29e-24

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 97.13  E-value: 2.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:cd17563   82 ASIATAVEAIKLGADDYLAK 101
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1-102 2.76e-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: 99.21  E-value: 2.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKK--AAPNVEVIL 78
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAdpRTADIPIIF 80
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTK 104
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
5-102 2.59e-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: 93.63  E-value: 2.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   5 LIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHGN 84
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*...
gi 495938351  85 IPDGVQAIKNGAFDYITK 102
Cdd:cd17574   81 EEDKVLGLELGADDYITK 98
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
3-117 1.29e-22

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: 92.34  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 495938351  83 GNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAV 117
Cdd:cd19919   82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
4-121 2.11e-22

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: 94.40  E-value: 2.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKAR 121
Cdd:COG4566   82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDR 119
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
4-119 3.54e-21

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: 88.55  E-value: 3.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYD---VCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEK 119
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
158-313 7.91e-21

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 88.17  E-value: 7.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  158 KVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLESemfghkagsftgalkdkkglfeeANNGT 237
Cdd:pfam14532  16 QAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ-----------------------AKGGT 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495938351  238 IFLDEIGEMAFELQAKLLRILETGEyikigdtkptRVNVRIIAATNRNLSQEIVAGRFREDLFYRLSVFQIHLPPL 313
Cdd:pfam14532  73 LYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFELSALRLHVPPL 138
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
4-102 1.08e-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: 84.56  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEK 99
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
4-102 1.09e-19

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 83.75  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAHG 83
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSARD 79
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd17620   80 EESDKIAALDAGADDYLTK 98
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1-121 1.68e-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: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMME-LEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVIL 78
Cdd:COG3279    1 MMKILIVDDEPLARERLERLLEkYPDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495938351  79 LTAHGNipDGVQAIKNGAFDYITKGDDNNKIIplisRAVEKAR 121
Cdd:COG3279   81 TTAYDE--YALEAFEVNAVDYLLKPIDEERLA----KALEKAK 117
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
4-102 3.21e-19

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: 82.55  E-value: 3.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPK 99
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
2-102 8.83e-19

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: 81.91  E-value: 8.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAA--PNVEVILL 79
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEmtRDIPIIML 80
                         90       100
                 ....*....|....*....|...
gi 495938351  80 TAHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITK 103
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
3-117 1.12e-18

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 81.56  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSA 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAV 117
Cdd:cd17542   82 MGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
3-102 1.13e-18

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: 81.00  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIK--KAAPNVEVILLT 80
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKedPETRHIPVIMIT 80
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSK 102
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
4-116 1.17e-18

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 81.49  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRA 116
Cdd:cd17537   83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQA 115
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
3-102 1.48e-18

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: 81.24  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:cd17615   81 DSVEDRIAGLTAGGDDYVTK 100
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
4-120 1.81e-18

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: 80.63  E-value: 1.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELE-GYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpDIEVVgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495938351  82 HGNIPDGVQAIKNGAFDYITKGDDNNKIIplisRAVEKA 120
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPEELI----EAIRAV 115
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1-118 2.00e-18

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 80.61  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:COG5803    2 MKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMT 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVE 118
Cdd:COG5803   82 AYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
3-136 2.52e-18

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 82.70  E-value: 2.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPnVEVILLTA 81
Cdd:COG3707    5 RVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVILLTA 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495938351  82 HGNiPDGVQ-AIKNGAFDYITKGDDNNKIIPLISRAVEKARmnvRLEKLEKKVGQT 136
Cdd:COG3707   84 YSD-PELIErALEAGVSAYLVKPLDPEDLLPALELALARFR---ELRALRRELAKL 135
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
4-102 4.24e-18

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: 79.84  E-value: 4.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVK 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
4-102 1.31e-17

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 78.50  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKaAPNVEVILLTAHG 83
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTARG 79
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd17623   80 DDIDRILGLELGADDYLPK 98
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
4-102 3.21e-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: 76.81  E-value: 3.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTK 99
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
3-118 4.01e-17

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: 77.06  E-value: 4.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGY 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 495938351  83 GNIPDGVQAIKNGA-FDYITKGDDNNKIIPLISRAVE 118
Cdd:cd17569   82 ADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
2-105 5.95e-17

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 76.49  E-value: 5.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
                         90       100
                 ....*....|....*....|....
gi 495938351  82 HGNIPDGVQAIKNGAfdYITKGDD 105
Cdd:cd17554   81 YSEYKSDFSSWAADA--YVVKSSD 102
orf27 CHL00148
Ycf27; Reviewed
3-141 1.53e-16

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 78.60  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAH 82
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES-DVPIIMLTAL 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495938351  83 GNIPDGVQAIKNGAFDYITKgddnnkiiPLISRAVEkARMNVRLEKLEKKVGQTYSFDS 141
Cdd:CHL00148  87 GDVSDRITGLELGADDYVVK--------PFSPKELE-ARIRSVLRRTNKKSFSSKIPNS 136
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
4-102 1.72e-16

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 75.11  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVK 99
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
4-102 1.74e-16

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: 74.85  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDlVLAIKKAAP---NVEVILLT 80
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFE-VCRRLKADPatrHIPVIFLT 79
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd19920   80 ALTDTEDKVKGFELGAVDYITK 101
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
4-102 7.01e-16

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: 73.61  E-value: 7.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAHG 83
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd17614   80 SEVDKVLGLELGADDYVTK 98
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
5-102 1.05e-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: 73.08  E-value: 1.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   5 LIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAP--NVEVILLTAH 82
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKtsSIPIIMLTAK 80
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:cd19937   81 GEEFDKVLGLELGADDYITK 100
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
3-128 6.60e-15

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: 70.74  E-value: 6.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMME-LEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEqVPGFTVIgTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVT 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495938351  81 AhGNIPDGVQ-AIKNGAFDYITKgddnnkiiplisrAVEKARMNVRLEK 128
Cdd:cd19925   82 A-ANDVETVReALRLGVVDYLIK-------------PFTFERLRQRLER 116
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
4-102 6.82e-15

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: 70.56  E-value: 6.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAP--NVEVILLTA 81
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTG 80
                         90       100
                 ....*....|....*....|..
gi 495938351  82 HGNIPDGVQAIKNGaFD-YITK 102
Cdd:cd17580   81 YGQPEDRERALEAG-FDaHLVK 101
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
4-102 7.36e-15

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 70.58  E-value: 7.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKK---AAPNVEVILLT 80
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRElegGGRRTPIIALT 80
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSK 102
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
3-102 7.45e-15

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


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 70.65  E-value: 7.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKK--AAPNVEVILLT 80
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEdpATRDIPVIALT 80
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISK 102
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
3-102 2.39e-14

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 72.06  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAA--PNVEVILLT 80
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESmtRDIPVVMLT 83
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10161  84 ARGEEEDRVRGLETGADDYITK 105
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
5-102 3.96e-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: 68.40  E-value: 3.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   5 LIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHGN 84
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90
                 ....*....|....*...
gi 495938351  85 IPDGVQAIKNGAFDYITK 102
Cdd:cd17625   81 VEDRVKGLDLGADDYLPK 98
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1-117 4.00e-14

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 71.37  E-value: 4.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLElQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLT 80
Cdd:PRK10955   1 MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTH-QTPVIMLT 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLIsRAV 117
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFNDRELVARI-RAI 114
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
4-102 4.07e-14

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 67.85  E-value: 4.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVK 99
fixJ PRK09390
response regulator FixJ; Provisional
6-121 4.43e-14

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 70.80  E-value: 4.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   6 IIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHGNI 85
Cdd:PRK09390   8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDV 87
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495938351  86 PDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKAR 121
Cdd:PRK09390  88 PLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAP 123
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
4-102 4.76e-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: 68.18  E-value: 4.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAHG 83
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS-EVGIILVTGRD 81
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd17619   82 DEVDRIVGLEIGADDYVTK 100
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
3-109 4.98e-14

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: 68.35  E-value: 4.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81
                         90       100
                 ....*....|....*....|....*..
gi 495938351  83 GNIPDGVQAIKNGAFDYITKGDDNNKI 109
Cdd:cd17553   82 GELDMIQESKELGALTHFAKPFDIDEI 108
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
4-102 7.49e-14

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: 67.69  E-value: 7.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAHG 83
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQIS-NVPIIFISSRD 79
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd18159   80 DNMDQVMAINMGGDDYITK 98
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-131 1.26e-13

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 69.99  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDV--CQAGdcRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVIL 78
Cdd:PRK11083   3 QPTILLVEDEQAIADTLVYALQSEGFTVewFERG--LPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIF 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITKgddnnkiiPLISRAVeKARMNVRLEKLEK 131
Cdd:PRK11083  81 LTARSDEVDRLVGLEIGADDYVAK--------PFSPREV-AARVRTILRRVKK 124
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-102 1.54e-13

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: 67.16  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLElQNPDV--VLCDVFLPDGNGVDLVLAIKKAAP--NVEVIL 78
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLE-QHPDIklVITDYNMPEMDGFELVREIRKKYSrdQLAIIG 80
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17544   81 ISASGDNALSARFIKAGANDFLTK 104
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
2-102 3.65e-13

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: 65.57  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIkKAAPNVEVILLTA 81
Cdd:cd17626    1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQI-RAESGVPIVMLTA 79
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17626   80 KSDTVDVVLGLESGADDYVAK 100
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1-102 5.90e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 67.91  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPnVEVILLT 80
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA-IPVIVLS 79
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSK 101
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
3-56 7.91e-13

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 62.97  E-value: 7.91e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 495938351     3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLP 56
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
3-102 1.10e-12

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: 64.35  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDG-NGVDLVLAIKKAApNVEVILLT 80
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKGDmDGIEAAREIREKF-DIPVIFLT 80
                         90       100
                 ....*....|....*....|...
gi 495938351  81 AHGNiPDGVQ-AIKNGAFDYITK 102
Cdd:cd17534   81 AYSD-EETLErAKETNPYGYLVK 102
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
2-102 6.02e-12

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: 62.46  E-value: 6.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVCQA-GDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPN--VEVIL 78
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGYLEVVSfTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLedVPIVM 80
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTK 104
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
4-102 9.45e-12

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: 61.91  E-value: 9.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTK 99
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
4-102 9.51e-12

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: 61.24  E-value: 9.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAP--NVEVILLTA 81
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADfdTIPVIFLTA 80
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITK 102
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSK 101
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
4-129 1.13e-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: 62.00  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMElEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 495938351  84 NIPDGVQAIKN-GAFDYITKGDDNNKIIPLISRAVEKARMNVRLEKL 129
Cdd:cd17596   82 DSEDIIAGINEaGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERL 128
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
4-102 1.59e-11

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 60.67  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIkKAAPNVEVILLTAHG 83
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQL-RARSNVPVIMVTAKD 79
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd17621   80 SEIDKVVGLELGADDYVTK 98
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
3-102 3.26e-11

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 60.48  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELE-GYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPnVEVILLT 80
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDpDIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVS 80
                         90       100
                 ....*....|....*....|....
gi 495938351  81 AH--GNIPDGVQAIKNGAFDYITK 102
Cdd:cd17541   81 SLteEGAEITLEALELGAVDFIAK 104
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1-67 3.51e-11

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: 60.68  E-value: 3.51e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELE-GYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAI 67
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEpDIEVVgEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
ompR PRK09468
osmolarity response regulator; Provisional
1-102 3.59e-11

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 63.07  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:PRK09468   5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLT 84
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK09468  85 AKGEEVDRIVGLEIGADDYLPK 106
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
165-303 4.19e-11

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 60.85  E-value: 4.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   165 PVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSKELLES---EMFGHKAGSFTGAlKDKKGLFEEANN---GTI 238
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGE-LRLRLALALARKlkpDVL 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495938351   239 FLDEIGEMAFELQAKLLRILETGEYIKIgdtKPTRVNVRIIAATNR--NLSQEIVAGRFREDLFYRL 303
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLLEELRLLLL---LKSEKNLTVILTTNDekDLGPALLRRRFDRRIVLLL 146
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
3-102 7.28e-11

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 59.49  E-value: 7.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELE-GYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDlVLAIKKAAP---NVEVIL 78
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLA-TLKKLQANPetqSIPVIL 81
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17552   82 LTAKAQPSDRQRFASLGVAGVIAK 105
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
4-102 7.32e-11

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 59.18  E-value: 7.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLElQNP---DVVLCDVFLPDGNGVDLVLAIKKAaPNVEVILLT 80
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLR-ENKdefDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMS 78
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17584   79 ADGSTSTVMKGLAHGACDYLLK 100
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
3-119 8.01e-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: 58.96  E-value: 8.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDL--VLAIKKAAPnveVILL 79
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAakIITSENIAP---IVLL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495938351  80 TAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEK 119
Cdd:cd19932   79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
PRK11173 PRK11173
two-component response regulator; Provisional
3-102 1.48e-10

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 61.18  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAH 82
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQA-NVALMFLTGR 83
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:PRK11173  84 DNEVDKILGLEIGADDYITK 103
PRK10766 PRK10766
two-component system response regulator TorR;
3-102 2.18e-10

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 60.44  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAH 82
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS-TVGIILVTGR 82
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10766  83 TDSIDRIVGLEMGADDYVTK 102
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
4-113 2.22e-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: 57.83  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLI 113
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
3-102 4.05e-10

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: 57.35  E-value: 4.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGY-DVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIK-----KAAPnveV 76
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRadgalSHLP---V 78
                         90       100
                 ....*....|....*....|....*.
gi 495938351  77 ILLTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd19923   79 LMVTAEAKKENVIAAAQAGVNNYIVK 104
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
3-113 4.23e-10

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 57.07  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIkKAAPNVEVILLTAH 82
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTI-RARSDVPIIIISGD 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 495938351  83 -GNIPDGVQAIKNGAFDYITKGDDNNKIIPLI 113
Cdd:cd17594   80 rRDEIDRVVGLELGADDYLAKPFGLRELLARV 111
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
4-102 4.58e-10

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 56.78  E-value: 4.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGY--DVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDieIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIpdGVQAIKNGAFDYITK 102
Cdd:cd17532   81 YDEY--AVEAFELNAVDYLLK 99
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
4-102 5.71e-10

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: 56.30  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAHG 83
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79
                         90
                 ....*....|....*....
gi 495938351  84 NIPDGVQAIKNGAFDYITK 102
Cdd:cd19936   80 DEIDEVFGLRMGADDYITK 98
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
4-102 7.89e-10

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: 56.13  E-value: 7.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGyD---VCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELED-DlevVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVT 79
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd19930   80 TFGRPGYFRRALAAGVDGYVLK 101
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
4-102 8.42e-10

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: 56.18  E-value: 8.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIK--KAAPNVEVILLTA 81
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKsdPDLKDIPVILLTT 80
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITK 101
PRK15479 PRK15479
transcriptional regulator TctD;
3-102 1.06e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 58.19  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTAR 81
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:PRK15479  82 SAVADRVKGLNVGADDYLPK 101
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
405-444 1.22e-09

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 53.17  E-value: 1.22e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 495938351  405 LSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEE 444
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
4-102 3.43e-09

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: 53.91  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAA--PNVEVILLTA 81
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSalKDTPIIMLTG 80
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTK 101
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
3-115 4.04e-09

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: 54.23  E-value: 4.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKK--AAPNVEVILLT 80
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKlpAYKFTPILMLT 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISR 115
Cdd:cd17562   82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKK 116
pleD PRK09581
response regulator PleD; Reviewed
1-102 5.33e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 57.99  E-value: 5.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDD-EVQIRTLLTRMMeLEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKK--AAPNVEVI 77
Cdd:PRK09581   2 TARILVVDDiPANVKLLEAKLL-AEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSdpATTHIPVV 80
                         90       100
                 ....*....|....*....|....*
gi 495938351  78 LLTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK09581  81 MVTALDDPEDRVRGLEAGADDFLTK 105
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
3-102 6.18e-09

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 56.09  E-value: 6.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:PRK09836  82 GTIEHRVKGLELGADDYLVK 101
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
3-102 8.70e-09

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: 53.15  E-value: 8.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKaAPNVEVILLTAH 82
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRR-FSDVPIIMVTAR 79
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:cd19938   80 VEEIDRLLGLELGADDYICK 99
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
2-102 1.12e-08

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 53.15  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTA 81
Cdd:cd17622    1 TRILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY-QGPILLLTA 79
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVK 100
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
3-102 1.78e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 55.93  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELE-GYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPnVEVIL-- 78
Cdd:PRK00742   5 RVLVVDDSAFMRRLISEILNSDpDIEVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRP-TPVVMvs 83
                         90       100
                 ....*....|....*....|....*....
gi 495938351  79 -LTAhgnipDG----VQAIKNGAFDYITK 102
Cdd:PRK00742  84 sLTE-----RGaeitLRALELGAVDFVTK 107
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
3-83 2.38e-08

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 51.73  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNP-DVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80

                 ..
gi 495938351  82 HG 83
Cdd:cd18160   81 GA 82
PRK10643 PRK10643
two-component system response regulator PmrA;
3-102 4.38e-08

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 53.50  E-value: 4.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10643  82 DTLEDRVAGLDVGADDYLVK 101
dpiA PRK10046
two-component response regulator DpiA; Provisional
4-122 4.44e-08

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 53.48  E-value: 4.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEvqirTLLTRM-----MELEGYD-VCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVI 77
Cdd:PRK10046   7 LLIVEDE----TPLAEMhaeyiRHIPGFSqILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVV 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495938351  78 LLTAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLISRAVEKARM 122
Cdd:PRK10046  83 FTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHM 127
PRK10816 PRK10816
two-component system response regulator PhoP;
3-102 4.75e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 53.59  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAH 82
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10816  82 ESWQDKVEVLSAGADDYVTK 101
PRK09483 PRK09483
response regulator; Provisional
1-117 5.01e-08

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 53.19  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMME-LEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVIL 78
Cdd:PRK09483   1 MINVLLVDDHELVRAGIRRILEdIKGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITKGDDNNKIIPLIsRAV 117
Cdd:PRK09483  81 LTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAI-RSV 118
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
165-284 5.11e-08

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: 51.52  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  165 PVLLTGETGTGKEVFAQaiHYSSKRARQNFVAVNCSSFSKellESEMFGHKAGSFTGALKDKKGLFEEANNG-TIFLDEI 243
Cdd:pfam07728   1 GVLLVGPPGTGKTELAE--RLAAALSNRPVFYVQLTRDTT---EEDLFGRRNIDPGGASWVDGPLVRAAREGeIAVLDEI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 495938351  244 GEMAFELQAKLLRILETGEYIKIGDTKPTRV---NVRIIAATNR 284
Cdd:pfam07728  76 NRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLIATMNP 119
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
4-80 3.38e-07

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: 48.50  E-value: 3.38e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQ-NPDVVLCDVFLPDG-NGVDLVLAIKKAAPNVEVILLT 80
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGGmNGSQLAEEARRRRPDLKVLLTS 79
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
3-102 4.36e-07

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: 47.99  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMEL-EGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLP--DGNGVDLVLAIKKAAPNVEVIL 78
Cdd:cd17561    3 KVLIADDNREFVQLLEEYLNSqPDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPhlDGIGVLEKLRRMRLEKRPKIIM 82
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17561   83 LTAFGQEDITQRAVELGASYYILK 106
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
4-113 5.81e-07

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: 48.17  E-value: 5.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLI 113
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDELVARI 110
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
4-83 7.01e-07

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 52.04  E-value: 7.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351    4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
2-82 1.81e-06

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 46.47  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDG-NGVDLVLAIKKAApNVEVILL 79
Cdd:cd17540    1 TRVLIIEDEPLIAMDLEQIVEDLGHQVVgIARTRDEAVALARRERPDLILADIQLADGsSGIDAVNEILTTH-DVPVIFV 79

                 ...
gi 495938351  80 TAH 82
Cdd:cd17540   80 TAY 82
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
4-102 1.81e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 48.49  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGyDVC---QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:PRK10651   9 ILLIDDHPMLRTGVKQLISMAP-DITvvgEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFS 87
                         90       100
                 ....*....|....*....|..
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10651  88 VSNHEEDVVTALKRGADGYLLK 109
PRK10360 PRK10360
transcriptional regulator UhpA;
1-102 2.33e-06

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 48.05  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEG--YDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAapnVEVIL 78
Cdd:PRK10360   1 MITVALIDDHLIVRSGFAQLLGLEPdlQVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQLPKG---MATIM 77
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10360  78 LSVHDSPALVEQALNAGARGFLSK 101
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
126-304 2.37e-06

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: 47.56  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 126 LEKLEKKV-GQTYSFDSIlgeSKVLKDAVSLAQKVSGTDVPVLLTGETGTGKEVFAQAIHYSSKRARQNFVAVNCSSFSK 204
Cdd:cd19499    6 EERLHERVvGQDEAVKAV---SDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 205 EllesemfgHKAGSFTGA-----LKDKKGLFEEAN----NGTIFLDEIGEMAFELQAKLLRILETGeyiKIGDTKPTRVN 275
Cdd:cd19499   83 K--------HSVSRLIGAppgyvGYTEGGQLTEAVrrkpYSVVLLDEIEKAHPDVQNLLLQVLDDG---RLTDSHGRTVD 151
                        170       180       190
                 ....*....|....*....|....*....|..
gi 495938351 276 VR---IIAATNrnlsqeivagRFREDLFYRLS 304
Cdd:cd19499  152 FKntiIIMTSN----------HFRPEFLNRID 173
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
166-284 2.55e-06

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: 46.43  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  166 VLLTGETGTGKEVFAQAIhysSKRARQNFVAVNCSSfskelLESEMFGHKAGSFTGALKDKKglfeEANNGTIFLDEI-- 243
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAV---AKELGAPFIEISGSE-----LVSKYVGESEKRLRELFEAAK----KLAPCVIFIDEIda 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 495938351  244 ---------GEMAFELQAKLLRILEtgeyikigDTKPTRVNVRIIAATNR 284
Cdd:pfam00004  69 lagsrgsggDSESRRVVNQLLTELD--------GFTSSNSKVIVIAATNR 110
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
3-102 2.66e-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: 46.21  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTAH 82
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS-HVPILMLTAR 79
                         90       100
                 ....*....|....*....|
gi 495938351  83 GNIPDGVQAIKNGAFDYITK 102
Cdd:cd19939   80 TEEMDRVLGLEMGADDYLCK 99
PRK14084 PRK14084
DNA-binding response regulator;
3-155 2.98e-06

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 48.21  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMM-ELEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:PRK14084   2 KALIVDDEPLARNELTYLLnEIGGFEEInEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIFAT 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495938351  81 AHGNIpdGVQAIKNGAFDYITKgddnnkiiplisrAVEKARMNVRLEKLEKKVGQTYSFDSILGESKVLKDAVSL 155
Cdd:PRK14084  82 AHDQF--AVKAFELNATDYILK-------------PFEQKRIEQAVNKVRATKAKDDNNASAIANDMSANFDQSL 141
PRK11697 PRK11697
two-component system response regulator BtsR;
1-131 5.30e-06

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 47.53  E-value: 5.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGyDVCQAGDCRAA---LKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAA-PNveV 76
Cdd:PRK11697   1 MIKVLIVDDEPLAREELRELLQEEG-DIEIVGECSNAieaIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPEHmPY--I 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495938351  77 ILLTAHgnipD--GVQAIKNGAFDYITKgddnnkiiPlisraVEKARMNVRLEKLEK 131
Cdd:PRK11697  78 VFVTAF----DeyAIKAFEEHAFDYLLK--------P-----IDPARLAKTLARLRQ 117
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
138-337 5.49e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 48.08  E-value: 5.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 138 SFDSILGESKV---LKDAVSLAQKVS------GTDVP--VLLTGETGTGKEVFAQAIhysSKRARQNFVAVNCSSF-SKE 205
Cdd:COG1222   76 TFDDIGGLDEQieeIREAVELPLKNPelfrkyGIEPPkgVLLYGPPGTGKTLLAKAV---AGELGAPFIRVRGSELvSKY 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 206 LLESEmfghkagsftGALKDkkgLFEEANNGT---IFLDEI-------------GEMAfELQAKLLRILetgeyikigDT 269
Cdd:COG1222  153 IGEGA----------RNVRE---VFELAREKApsiIFIDEIdaiaarrtddgtsGEVQ-RTVNQLLAEL---------DG 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 270 KPTRVNVRIIAATNRnlsQEIV------AGRFREDLFY-------RLSVFQIHLPPLR-ERAGDIRLLAKAF-------I 328
Cdd:COG1222  210 FESRGDVLIIAATNR---PDLLdpallrPGRFDRVIEVplpdeeaREEILKIHLRDMPlADDVDLDKLAKLTegfsgadL 286

                 ....*....
gi 495938351 329 KSFAEQLAR 337
Cdd:COG1222  287 KAIVTEAGM 295
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
4-79 6.82e-06

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 44.57  E-value: 6.82e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495938351   4 ILIIDDEVQIRTLLTRMMELE--GYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILL 79
Cdd:cd17565    1 FYIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMI 78
PRK13435 PRK13435
response regulator; Provisional
1-102 7.89e-06

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 45.43  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDG-NGVDLVLAIkKAAPNVEVIL 78
Cdd:PRK13435   5 QLKVLIVEDEALIALELEKLVEEAGHEVVgIAMSSEQAIALGRRRQPDVALVDVHLADGpTGVEVARRL-SADGGVEVVF 83
                         90       100
                 ....*....|....*....|....*
gi 495938351  79 LTA-HGNIPDGVQaiknGAFDYITK 102
Cdd:PRK13435  84 MTGnPERVPHDFA----GALGVIAK 104
PRK11517 PRK11517
DNA-binding response regulator HprR;
3-102 9.45e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 46.43  E-value: 9.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALkQLELQNP-DVVLCDVFLPDGNGVDLVLAIKkAAPNVEVILLTA 81
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGL-YLALKDDyALIILDIMLPGMDGWQILQTLR-TAKQTPVICLTA 79
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK11517  80 RDSVDDRVRGLDSGANDYLVK 100
PRK15369 PRK15369
two component system response regulator;
3-102 1.15e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 46.23  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEV----QIRTLLTRMMELE-------GYDVCQAgdCRaalkQLElqnPDVVLCDVFLPDGNGVDLVLAIKKAA 71
Cdd:PRK15369   5 KILLVDDHEliinGIKNMLAPYPRYKivgqvdnGLEVYNA--CR----QLE---PDIVILDLGLPGMNGLDVIPQLHQRW 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 495938351  72 PNVEVILLTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK15369  76 PAMNILVLTARQEEHMASRTLAAGALGYVLK 106
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-102 1.35e-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: 44.09  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELE-GYDVCQAGDCRAALKQLElQNPD--VVLCDVFLPDG-NG--VDLVLaiKKAAPnveV 76
Cdd:cd19921    1 KVLIVEDSKTFSKVLKHLIAQElGLEVDVAETLAEAKALLE-EGDDyfAALVDLNLPDApNGeaVDLVL--EKGIP---V 74
                         90       100
                 ....*....|....*....|....*...
gi 495938351  77 ILLTahGNIPDGV--QAIKNGAFDYITK 102
Cdd:cd19921   75 IVLT--GSFDEDKreTLLSKGVVDYVLK 100
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
3-102 1.74e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.41  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELE-GYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPnVEVILLT 80
Cdd:PRK12555   2 RIGIVNDSPLAVEALRRALARDpDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERP-CPILIVT 80
                         90       100
                 ....*....|....*....|....*.
gi 495938351  81 AhgNIPDGV----QAIKNGAFDYITK 102
Cdd:PRK12555  81 S--LTERNAsrvfEAMGAGALDAVDT 104
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
4-102 2.05e-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: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNP--DVVLCDVFLPDGNGVDLVLAI--KKAAPNVEVILL 79
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYImrHKICKNIPVIMM 80
                         90       100
                 ....*....|....*....|...
gi 495938351  80 TAHGNIPDGVQAIKNGAFDYITK 102
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVK 103
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
4-102 2.40e-05

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 43.49  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGY--DVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDftVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITK 102
Cdd:cd19931   81 SDAEDDVVTALRAGADGYLLK 101
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
3-85 3.59e-05

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: 43.20  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYD-VCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTA 81
Cdd:cd17530    2 RVLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSG 81

                 ....
gi 495938351  82 HGNI 85
Cdd:cd17530   82 LDGG 85
PRK13557 PRK13557
histidine kinase; Provisional
4-80 1.01e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 44.66  E-value: 1.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQN-PDVVLCDVFLPDG-NGVDLVLAIKKAAPNVEVILLT 80
Cdd:PRK13557 418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPeVDLLFTDLIMPGGmNGVMLAREARRRQPKIKVLLTT 496
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
5-116 1.02e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 43.35  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   5 LIIDDEVQIRTLLTRMMELEGYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHG 83
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILaELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKN 83
                         90       100       110
                 ....*....|....*....|....*....|...
gi 495938351  84 NIPDGVQAIKNGAFDYITKGDDNNKIIPLISRA 116
Cdd:PRK09958  84 DHFYGKHCADAGANGFVSKKEGMNNIIAAIEAA 116
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
4-103 1.04e-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: 41.60  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLEL---------QNPDVVLCDVFLPDGNGVDLVLAIKK--AAP 72
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 495938351  73 NVEVILLTAHGNIPDGVQAIKNGAFDYITKG 103
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10430 PRK10430
two-component system response regulator DcuR;
1-102 1.22e-04

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 43.56  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMM-ELEGYDVCQAGDCRAALKQLeLQNP----DVVLCDVFLPDGNGVDLVLAIKKAAPNVE 75
Cdd:PRK10430   1 MINVLIVDDDAMVAELNRRYVaQIPGFQCCGTASTLEQAKEI-IFNSdtpiDLILLDIYMQQENGLDLLPVLHEAGCKSD 79
                         90       100
                 ....*....|....*....|....*..
gi 495938351  76 VILLTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10430  80 VIVISSAADAATIKDSLHYGVVDYLIK 106
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
3-105 1.93e-04

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 42.53  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELE-GYDVC-QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLT 80
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELDpGFEVVaEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILT 87
                         90       100
                 ....*....|....*....|....*
gi 495938351  81 AHGNIPDGVQAIKNGAFDYITKGDD 105
Cdd:PRK10403  88 VSDASSDVFALIDAGADGYLLKDSD 112
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
3-115 2.27e-04

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: 40.60  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTR-MMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTa 81
Cdd:cd17593    2 KVLICDDSSMARKQLARaLPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS- 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495938351  82 hGNI-PDGVQ-AIKNGAFDYITKGDDNNKIIPLISR 115
Cdd:cd17593   81 -GDVqPEAKErVLELGALAFLKKPFDPEKLAQLLEE 115
fis PRK00430
DNA-binding transcriptional regulator Fis;
405-445 2.68e-04

DNA-binding transcriptional regulator Fis;


Pssm-ID: 179020 [Multi-domain]  Cd Length: 95  Bit Score: 40.05  E-value: 2.68e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 495938351 405 LSAMERRHIARVLEYTKGNKTEAARLLKIGLTTLYRKIEEY 445
Cdd:PRK00430  52 LAEVEAPLLDMVMQYTRGNQTRAALMLGINRGTLRKKLKKY 92
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
4-102 3.19e-04

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: 40.32  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMELEGY-DVCQAGDCRAALKQLELQNPDVVLCDVFLPDG-NGVDLVLAIKKA---APNVEVIL 78
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKGkNGQQLLEELRHKkliSPSTVFIM 80
                         90       100
                 ....*....|....*....|....*....
gi 495938351  79 LTAhgnipDGVQAIKNGAF-----DYITK 102
Cdd:cd17589   81 VTG-----ESSRAMVLSALelepdDYLLK 104
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1-102 6.27e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 41.34  E-value: 6.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLV--LAIKKAAPnvEVIL 78
Cdd:PRK13856   1 MKHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVrsLATKSDVP--IIII 78
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK13856  79 SGDRLEEADKVVALELGATDFIAK 102
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
4-99 7.31e-04

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 39.63  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   4 ILIIDDEVQIRTLLTRMMEL---EGYDVCQAGDCRAAL---KQLELQNPDV--VLCDVFLPDGNGVDLVLAIKKAAPNVE 75
Cdd:cd17595    3 ILTVDDDPQVLRAVARDLRRqygKDYRVLRADSGAEALdalKELKLRGEAValFLVDQRMPEMDGVEFLEKAMELFPEAK 82
                         90       100
                 ....*....|....*....|....
gi 495938351  76 VILLTAHGNIPDGVQAIKNGAFDY 99
Cdd:cd17595   83 RVLLTAYADTDAAIRAINDVQLDY 106
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
149-284 9.31e-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: 39.57  E-value: 9.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 149 LKDAVSLAQKVS------GTDVP--VLLTGETGTGKEVFAQAIhysSKRARQNFVAVNCSS-FSKELLESEMfghkagsf 219
Cdd:cd19511    5 LKEAVEWPLKHPdafkrlGIRPPkgVLLYGPPGCGKTLLAKAL---ASEAGLNFISVKGPElFSKYVGESER-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 220 tgALKDkkgLFEEANNGT---IFLDEI------------GEMAFELQAKLLRILETGEyikigdtkpTRVNVRIIAATNR 284
Cdd:cd19511   74 --AVRE---IFQKARQAApciIFFDEIdslaprrgqsdsSGVTDRVVSQLLTELDGIE---------SLKGVVVIAATNR 139
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
166-284 1.04e-03

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: 39.57  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 166 VLLTGETGTGKEVFAQAIhysSKRARQNFVAVNCSSF-SKELLESEMFGHKagsftgalkdkkgLFEEANN---GTIFLD 241
Cdd:cd19481   29 ILLYGPPGTGKTLLAKAL---AGELGLPLIVVKLSSLlSKYVGESEKNLRK-------------IFERARRlapCILFID 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495938351 242 EI------------GEMAFELQAKLLRILetgeyikigDTKPTRVNVRIIAATNR 284
Cdd:cd19481   93 EIdaigrkrdssgeSGELRRVLNQLLTEL---------DGVNSRSKVLVIAATNR 138
PRK10693 PRK10693
two-component system response regulator RssB;
30-102 1.04e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 40.74  E-value: 1.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495938351  30 QAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVILLTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLK 74
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
166-284 1.07e-03

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: 39.58  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 166 VLLTGETGTGKEVFAQAIhysskrARQ---NFVAVNCSSF-SKELLESEmfghkagsftgalKDKKGLFEEANNGT---I 238
Cdd:cd19503   37 VLLHGPPGTGKTLLARAV------ANEagaNFLSISGPSIvSKYLGESE-------------KNLREIFEEARSHApsiI 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495938351 239 FLDEI-----------GEMAFELQAKLLRILetgeyikigDTKPTRVNVRIIAATNR 284
Cdd:cd19503   98 FIDEIdalapkreedqREVERRVVAQLLTLM---------DGMSSRGKVVVIAATNR 145
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
120-350 1.22e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 40.84  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 120 ARMnvRLEKLEKKVGQtysfDSILGESKVLKDAVSLAQKVSgtdvpVLLTGETGTGKEVFAQAIhysSKRARQNFVAVNC 199
Cdd:PRK13342   4 ERM--RPKTLDEVVGQ----EHLLGPGKPLRRMIEAGRLSS-----MILWGPPGTGKTTLARII---AGATDAPFEALSA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 200 SSFSKellesemfghkagsftgalKDKKGLFEEA------NNGTI-FLDEIGEMAFELQAKLLRILETGEYIkigdtkpt 272
Cdd:PRK13342  70 VTSGV-------------------KDLREVIEEArqrrsaGRRTIlFIDEIHRFNKAQQDALLPHVEDGTIT-------- 122
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495938351 273 rvnvrIIAATNRNLSQEIVAGrfredLFYRLSVFQIHlpPLREraGDIR-LLAKAfiksfAEQLARPVVEIAPAFLEAL 350
Cdd:PRK13342 123 -----LIGATTENPSFEVNPA-----LLSRAQVFELK--PLSE--EDIEqLLKRA-----LEDKERGLVELDDEALDAL 182
PRK15347 PRK15347
two component system sensor kinase;
3-102 1.25e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 41.17  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVE----VIL 78
Cdd:PRK15347 692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDpdcmIVA 771
                         90       100
                 ....*....|....*....|....
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK15347 772 LTANAAPEEIHRCKKAGMNHYLTK 795
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
2-102 2.53e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 39.28  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   2 SKILIIDDEVQIRTLLTRMMELEGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAApNVEVILLTA 81
Cdd:PRK10710  11 PRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS-DIPIVMVTA 89
                         90       100
                 ....*....|....*....|.
gi 495938351  82 HGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10710  90 KIEEIDRLLGLEIGADDYICK 110
PRK10336 PRK10336
two-component system response regulator QseB;
3-166 2.53e-03

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 39.11  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   3 KILIIDDEV----QIRTLLTRMmeleGYDVCQAGDCRAALKQLELQNPDVVLCDVFLPDGNGVDLVLAIKKAAPNVEVIL 78
Cdd:PRK10336   2 RILLIEDDMligdGIKTGLSKM----GFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351  79 LTAHGNIPDGVQAIKNGAFDYITKGddnnkiIPLISRAvekarmnVRLEKLEKKV-GQTysfDSILGESKVLKDAVSLAQ 157
Cdd:PRK10336  78 LTARDALAERVEGLRLGADDYLCKP------FALIEVA-------ARLEALMRRTnGQA---SNELRHGNVMLDPGKRIA 141

                 ....*....
gi 495938351 158 KVSGTDVPV 166
Cdd:PRK10336 142 TLAGEPLTL 150
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1-102 2.59e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 39.23  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351   1 MSKILIIDDEVQIRTLLTRMMELEGYDVC--QAGDcrAALKQLELQNPDVVLCDVFLPDGNGVDLV--LAIKKAAPnveV 76
Cdd:PRK10701   1 MNKIVFVEDDAEVGSLIAAYLAKHDIDVTvePRGD--RAEATILREQPDLVLLDIMLPGKDGMTICrdLRPKWQGP---I 75
                         90       100
                 ....*....|....*....|....*.
gi 495938351  77 ILLTAHGNIPDGVQAIKNGAFDYITK 102
Cdd:PRK10701  76 VLLTSLDSDMNHILALEMGACDYILK 101
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
138-259 6.07e-03

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 38.82  E-value: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495938351 138 SFDSILGESKVLKDAVSLAQkvSGTDVPVLLTGETGTGK----EVFAQAIHYSSKRArqNFVAVNCSSF----SKELLES 209
Cdd:PRK12402  13 LLEDILGQDEVVERLSRAVD--SPNLPHLLVQGPPGSGKtaavRALARELYGDPWEN--NFTEFNVADFfdqgKKYLVED 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495938351 210 EMFGHKAGSFTGALKDKKGLFEE------------ANNGTIFLDEIGEMAFELQAKLLRILE 259
Cdd:PRK12402  89 PRFAHFLGTDKRIRSSKIDNFKHvlkeyasyrplsADYKTILLDNAEALREDAQQALRRIME 150
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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