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Conserved domains on  [gi|654546378|ref|WP_028014084|]
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MULTISPECIES: two-component system response regulator GlrR [Enterobacter]

Protein Classification

two-component system response regulator QseF/GlrR( domain architecture ID 11487662)

two-component system response regulator QseF/GlrR binds DNA upon phosphorylation and functions as transcriptional regulator, such as transcriptional regulatory protein GlrR, which is part of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter stationary growth phase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15115 PRK15115
response regulator GlrR; Provisional
2-445 0e+00

response regulator GlrR; Provisional


:

Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 948.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   2 TSRKPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPV 81
Cdd:PRK15115   1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  82 IILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDAWRESIVTRSPIMLRLLEQARMVAQSDVSV 161
Cdd:PRK15115  81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDERWREAIVTRSPLMLRLLEQARMVAQSDVSV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 162 LINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDM 241
Cdd:PRK15115 161 LINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 242 PAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANH 321
Cdd:PRK15115 241 PAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 322 LLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFAEARNQFEL 401
Cdd:PRK15115 321 LLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFVEARNQFEL 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 654546378 402 NYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELEANDFKE 445
Cdd:PRK15115 401 NYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFKE 444
 
Name Accession Description Interval E-value
PRK15115 PRK15115
response regulator GlrR; Provisional
2-445 0e+00

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 948.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   2 TSRKPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPV 81
Cdd:PRK15115   1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  82 IILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDAWRESIVTRSPIMLRLLEQARMVAQSDVSV 161
Cdd:PRK15115  81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDERWREAIVTRSPLMLRLLEQARMVAQSDVSV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 162 LINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDM 241
Cdd:PRK15115 161 LINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 242 PAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANH 321
Cdd:PRK15115 241 PAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 322 LLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFAEARNQFEL 401
Cdd:PRK15115 321 LLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFVEARNQFEL 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 654546378 402 NYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELEANDFKE 445
Cdd:PRK15115 401 NYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFKE 444
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
5-436 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: 546.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIIL 84
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDAWRESIVTRSPIMLRLLEQARMVAQSDVSVLIN 164
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDATVLIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 165 GQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDMPAP 244
Cdd:COG2204  161 GESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPLA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 245 LQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANHLLR 324
Cdd:COG2204  241 LQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFLA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 325 QAADRHKPFVRaFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEgentalptfaearnQFELNYL 404
Cdd:COG2204  321 RFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEALE--------------EVERELI 385
                        410       420       430
                 ....*....|....*....|....*....|..
gi 654546378 405 RKLLQITKGNVTHAARMAGRNRTEFYKLLSRH 436
Cdd:COG2204  386 ERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
9-426 9.50e-126

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


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 372.53  E-value: 9.50e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378    9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDAWRES-------IVTRSPIMLRLLEQARMVAQSDVSV 161
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGeaedsaeLIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  162 LINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDM 241
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  242 PAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANH 321
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  322 LLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI--SDALVEQALEGENTALPT-------- 391
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVlvSDLPAELALTGRPASAPDsdgqdswd 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 654546378  392 ------------------FAEARNQFELNYLRKLLQITKGNVTHAARMAGRNR 426
Cdd:TIGR01818 401 ealeawakqalsrgeqglLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGR 453
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
135-432 4.92e-110

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 336.09  E-value: 4.92e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 135 ESIVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNaFIAINCGALPEQLLESELFGHARGAF 214
Cdd:NF041552 267 GKIIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRKGP-FVPVNCSAIPEELFESEFFGYEEGAF 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 215 TGAVSS-REGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFRED 293
Cdd:NF041552 346 TGALKKgKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFRED 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 294 LYYRLNVVNLKIPALAERAEDIPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI 373
Cdd:NF041552 426 LYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNGTI 505
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546378 374 S-DALVEQALE--GENTALPTFA-----EARNQFELNYLRKLLQITKGNVTHAARMAGRNR-TEFYKL 432
Cdd:NF041552 506 TkDSIPEYILEsvKKKEDEEGDYpldlnKAVEKLEIDTIKKALEMSNGNKAKAAKLLNIPRsTLYYKL 573
Sigma54_activat pfam00158
Sigma-54 interaction domain;
137-303 3.33e-107

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 314.34  E-value: 3.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  137 IVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTG 216
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  217 AVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYY 296
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 654546378  297 RLNVVNL 303
Cdd:pfam00158 161 RLNVIPI 167
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
10-124 9.26e-36

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: 128.38  E-value: 9.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGS 89
Cdd:cd17549    2 LLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHGD 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 654546378  90 IPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEH 124
Cdd:cd17549   82 VPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEK 116
resp_reg_YycF NF040534
response regulator YycF;
9-136 5.85e-13

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 68.21  E-value: 5.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQpGMPVIILTAHG 88
Cdd:NF040534   3 ILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKY-DMPIIMLTAKD 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL-EHAAPSGDDAWRES 136
Cdd:NF040534  82 SEIDKVLGLELGADDYVTKPFSTRELIARVKANLrRHQQQNTEEEEEEN 130
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
8-60 1.90e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.82  E-value: 1.90e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 654546378     8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRM 60
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMM 54
 
Name Accession Description Interval E-value
PRK15115 PRK15115
response regulator GlrR; Provisional
2-445 0e+00

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 948.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   2 TSRKPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPV 81
Cdd:PRK15115   1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  82 IILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDAWRESIVTRSPIMLRLLEQARMVAQSDVSV 161
Cdd:PRK15115  81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDERWREAIVTRSPLMLRLLEQARMVAQSDVSV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 162 LINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDM 241
Cdd:PRK15115 161 LINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 242 PAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANH 321
Cdd:PRK15115 241 PAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 322 LLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFAEARNQFEL 401
Cdd:PRK15115 321 LLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFVEARNQFEL 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 654546378 402 NYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELEANDFKE 445
Cdd:PRK15115 401 NYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFKE 444
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
5-436 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: 546.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIIL 84
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDAWRESIVTRSPIMLRLLEQARMVAQSDVSVLIN 164
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDATVLIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 165 GQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDMPAP 244
Cdd:COG2204  161 GESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPLA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 245 LQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANHLLR 324
Cdd:COG2204  241 LQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFLA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 325 QAADRHKPFVRaFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEgentalptfaearnQFELNYL 404
Cdd:COG2204  321 RFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEALE--------------EVERELI 385
                        410       420       430
                 ....*....|....*....|....*....|..
gi 654546378 405 RKLLQITKGNVTHAARMAGRNRTEFYKLLSRH 436
Cdd:COG2204  386 ERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
135-439 2.92e-158

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: 454.61  E-value: 2.92e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 135 ESIVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAF 214
Cdd:COG3829  138 DDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAF 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 215 TGAVSS-REGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFRED 293
Cdd:COG3829  218 TGAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFRED 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 294 LYYRLNVVNLKIPALAERAEDIPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI 373
Cdd:COG3829  298 LYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSEGDVI 377
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654546378 374 S-----DALVEQALEGENTALPTFAEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELE 439
Cdd:COG3829  378 TpehlpEYLLEEAEAASAAEEGSLKEALEEVEKELIEEALEKTGGNKSKAAKALGISRSTLYRKLKKYGIK 448
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
5-432 1.39e-129

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 382.27  E-value: 1.39e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAH-LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVII 83
Cdd:PRK11361   2 TAINrILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  84 LTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALE-----------HAAPSGDDAWrESIVTRSPIMLRLLEQAR 152
Cdd:PRK11361  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQlqsmkkeirhlHQALSTSWQW-GHILTNSPAMMDICKDTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 153 MVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGT 232
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 233 LFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERA 312
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 313 EDIPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI-SDALVEQALEGENTALPT 391
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIfSEDLPPQIRQPVCNAGEV 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 654546378 392 FAEA---RN------QFELNYLRKLLQITKGNVTHAARMAG-RNRTEFYKL 432
Cdd:PRK11361 401 KTAPvgeRNlkeeikRVEKRIIMEVLEQQEGNRTRTALMLGiSRRALMYKL 451
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-435 1.89e-129

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 381.30  E-value: 1.89e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRKpAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMP 80
Cdd:PRK10365   1 MTHDN-IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  81 VIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDD-----AWRESIVTRSPIMLRLLEQARMVA 155
Cdd:PRK10365  80 VLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAEtpavtASQFGMVGKSPAMQHLLSEIALVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 156 QSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFL 235
Cdd:PRK10365 160 PSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 236 DEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDI 315
Cdd:PRK10365 240 DEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 316 PLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVISDAlvEQALEGENTALPTFAEA 395
Cdd:PRK10365 320 PLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISER--ELPLAIASTPIPLGQSQ 397
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 654546378 396 RNQ----FELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSR 435
Cdd:PRK10365 398 DIQplveVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
9-426 9.50e-126

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


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 372.53  E-value: 9.50e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378    9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDAWRES-------IVTRSPIMLRLLEQARMVAQSDVSV 161
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGeaedsaeLIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  162 LINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDM 241
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  242 PAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANH 321
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  322 LLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI--SDALVEQALEGENTALPT-------- 391
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVlvSDLPAELALTGRPASAPDsdgqdswd 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 654546378  392 ------------------FAEARNQFELNYLRKLLQITKGNVTHAARMAGRNR 426
Cdd:TIGR01818 401 ealeawakqalsrgeqglLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGR 453
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
9-438 4.70e-118

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


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 352.13  E-value: 4.70e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378    9 LLLVDDDPGLLKLLgmRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRM-----DEMDGMQLFAEIQKQQPGMPVII 83
Cdd:TIGR02915   1 LLIVEDDLGLQKQL--KWSFADYELAVAADRESAIALVRRHEPAVVTLDLGLppdadGASEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   84 LTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAA---------PSGDDAWRESIVTRSPIMLRLLEQARMV 154
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTletenrrlqSALGGTALRGLITSSPGMQKICRTIEKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  155 AQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLF 234
Cdd:TIGR02915 159 APSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  235 LDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAED 314
Cdd:TIGR02915 239 LDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  315 IPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI-SDALVEQALEGENTALP-TF 392
Cdd:TIGR02915 319 AVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQItAEDLGLDARERAETPLEvNL 398
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 654546378  393 AEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHEL 438
Cdd:TIGR02915 399 REVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
124-436 5.56e-118

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 358.06  E-value: 5.56e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 124 HAAPSGDDAWR--ESIVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQL 201
Cdd:COG3284  308 RAAPAGAPAPAalAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEEL 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 202 LESELFGHARGAFTGAVSS-REGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRD 280
Cdd:COG3284  388 IESELFGYEPGAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRD 467
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 281 LPKVMARNEFREDLYYRLNVVNLKIPALAERaEDIPLLANHLLRQAADRHKPfvRAFSTDAMKRLMAASWPGNVRQLVNV 360
Cdd:COG3284  468 LRELVAAGRFREDLYYRLNGLTLTLPPLRER-EDLPALIEHLLRELAAGRGP--LRLSPEALALLAAYPWPGNVRELRNV 544
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 361 IEQCVALTSSPVIS-----DALVEQALEGENTALPTFAEARNQfELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSR 435
Cdd:COG3284  545 LRTALALADGGVITvedlpDELRAELAAAAPAAAAPLTSLEEA-ERDAILRALRACGGNVSAAARALGISRSTLYRKLKR 623

                 .
gi 654546378 436 H 436
Cdd:COG3284  624 Y 624
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
135-432 4.92e-110

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 336.09  E-value: 4.92e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 135 ESIVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNaFIAINCGALPEQLLESELFGHARGAF 214
Cdd:NF041552 267 GKIIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRKGP-FVPVNCSAIPEELFESEFFGYEEGAF 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 215 TGAVSS-REGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFRED 293
Cdd:NF041552 346 TGALKKgKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFRED 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 294 LYYRLNVVNLKIPALAERAEDIPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI 373
Cdd:NF041552 426 LYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNGTI 505
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546378 374 S-DALVEQALE--GENTALPTFA-----EARNQFELNYLRKLLQITKGNVTHAARMAGRNR-TEFYKL 432
Cdd:NF041552 506 TkDSIPEYILEsvKKKEDEEGDYpldlnKAVEKLEIDTIKKALEMSNGNKAKAAKLLNIPRsTLYYKL 573
Sigma54_activat pfam00158
Sigma-54 interaction domain;
137-303 3.33e-107

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 314.34  E-value: 3.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  137 IVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTG 216
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  217 AVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYY 296
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 654546378  297 RLNVVNL 303
Cdd:pfam00158 161 RLNVIPI 167
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
5-439 1.07e-106

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 324.13  E-value: 1.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIIL 84
Cdd:PRK10923   2 QRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEH------------AAPSGDdawresIVTRSPIMLRLLEQAR 152
Cdd:PRK10923  82 TAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHyqeqqqprniqvNGPTTD------IIGEAPAMQDVFRIIG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 153 MVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGT 232
Cdd:PRK10923 156 RLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 233 LFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERA 312
Cdd:PRK10923 236 LFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERR 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 313 EDIPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNV----------------------IEQCVALTSS 370
Cdd:PRK10923 316 EDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTcrwltvmaagqevliqdlpgelFESTVPESTS 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654546378 371 PVISDALVEQALEGENTALPT-----FAEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELE 439
Cdd:PRK10923 396 QMQPDSWATLLAQWADRALRSghqnlLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
135-407 3.93e-98

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 303.26  E-value: 3.93e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 135 ESIVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAF 214
Cdd:COG3283  204 DHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAF 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 215 TGAVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDL 294
Cdd:COG3283  284 GNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDL 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 295 YYRLNVVNLKIPALAERAEDIPLLANHLLRQAAD---RHKPfvrAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSP 371
Cdd:COG3283  364 YYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQqlgRPRP---RLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGD 440
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 654546378 372 VI------------SDALVEQALEGentalpTFAEARNQFELNYLRKL 407
Cdd:COG3283  441 ELtpedlqlpeyaaSAGLLDDLLEG------SLDEIVKRFERSLLRRL 482
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
137-373 1.63e-96

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: 300.09  E-value: 1.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  137 IVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTG 216
Cdd:TIGR01817 198 IIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTG 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  217 AVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYY 296
Cdd:TIGR01817 278 AIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYY 357
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546378  297 RLNVVNLKIPALAERAEDIPLLANHLLRQ-AADRHKPFvrAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI 373
Cdd:TIGR01817 358 RINVVPIFLPPLRERREDIPLLAEAFLEKfNRENGRPL--TITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTI 433
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
119-435 6.05e-93

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 289.76  E-value: 6.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 119 DSALEHAAPSGDDAwreSIVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALP 198
Cdd:PRK05022 174 DVAEFLRQEALKEG---EMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALP 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 199 EQLLESELFGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATH 278
Cdd:PRK05022 251 ESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATN 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 279 RDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANHLLRQAadRHKPFVR--AFSTDAMKRLMAASWPGNVRQ 356
Cdd:PRK05022 331 RDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQN--RARLGLRslRLSPAAQAALLAYDWPGNVRE 408
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 357 LVNVIEQCV--ALTSSP----VIS----DALVEQALEGENTALP-------TFAEARNQFELNYLRKLLQITKGNVTHAA 419
Cdd:PRK05022 409 LEHVISRAAllARARGAgrivTLEaqhlDLPAEVALPPPEAAAApaavvsqNLREATEAFQRQLIRQALAQHQGNWAAAA 488
                        330
                 ....*....|....*.
gi 654546378 420 RMAGRNRTEFYKLLSR 435
Cdd:PRK05022 489 RALELDRANLHRLAKR 504
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
137-435 1.81e-85

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 275.56  E-value: 1.81e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 137 IVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTG 216
Cdd:PRK15429 378 IIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTG 457
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 217 AVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYY 296
Cdd:PRK15429 458 ASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYY 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 297 RLNVVNLKIPALAERAEDIPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVISDA 376
Cdd:PRK15429 538 RLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVLQLS 617
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654546378 377 LVEQAL-EGENTALPTFAEARNQFELNYLRKLLQITKGNVT---HAARMAGRNRTefyKLLSR 435
Cdd:PRK15429 618 LPDITLpEPETPPAATVVAQEGEDEYQLIVRVLKETNGVVAgpkGAAQRLGLKRT---TLLSR 677
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
78-439 6.66e-83

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 264.66  E-value: 6.66e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  78 GMPVIILTahGSIPD-AVAATQQGVFSFLTKPVdKDALYKAID----SALEHAAPSGDDAWR-----ESIVTRSPIMLRL 147
Cdd:PRK15424 155 GIEAVVGA--GLITDlAEEAGMTGIFIYSAATV-RQAFEDALDmtrmTLRHNTHYATRNALRtryvlGDLLGQSPQMEQV 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 148 LEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASP--------RSKNAFIAINCGALPEQLLESELFGHARGAFTGAV- 218
Cdd:PRK15424 232 RQTILLYARSSAAVLIQGETGTGKELAAQAIHREYFarhdarqgKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRr 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 219 SSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRL 298
Cdd:PRK15424 312 GGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRL 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 299 NVVNLKIPALAERAEDIPLLANHLLRQA----ADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQ-CVALTSSP-- 371
Cdd:PRK15424 392 SILRLQLPPLRERVADILPLAESFLKQSlaalSAPFSAALRQGLQQCETLLLHYDWPGNVRELRNLMERlALFLSVEPtp 471
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546378 372 VISDALVEQALEGENTALPTFAEARNQFELnyLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELE 439
Cdd:PRK15424 472 DLTPQFLQLLLPELARESAKTPAPRLLAAT--LQQALERFNGDKTAAANYLGISRTTLWRRLKAEAKA 537
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
88-433 2.00e-78

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: 252.86  E-value: 2.00e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   88 GSIPD-AVAATQQGVFSFltkpvDKDALYKAIDSALE-------HAAPSGDDAWRESIVTR---------SPIMLRLLEQ 150
Cdd:TIGR02329 153 GLITDlAEQAGLHGVFLY-----SADSVRQAFDDALDvaratrlRQAATLRSATRNQLRTRyrlddllgaSAPMEQVRAL 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  151 ARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGA-VSSREGLFQAAE 229
Cdd:TIGR02329 228 VRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTGArRGGRTGLIEAAH 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  230 GGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALA 309
Cdd:TIGR02329 308 RGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLFYRLSILRIALPPLR 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  310 ERAEDIPLLANHLLRQAAdrhkPFVRAFSTDAMKRLMAAS--------WPGNVRQLVNVIEQ-CVALTSSP--------- 371
Cdd:TIGR02329 388 ERPGDILPLAAEYLVQAA----AALRLPDSEAAAQVLAGVadplqrypWPGNVRELRNLVERlALELSAMPagaltpdvl 463
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654546378  372 -VISDALVEQALEGENTALPtfAEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLL 433
Cdd:TIGR02329 464 rALAPELAEASGKGKTSALS--LRERSRVEALAVRAALERFGGDRDAAAKALGISRTTLWRRL 524
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
141-439 3.85e-72

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: 230.89  E-value: 3.85e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 141 SPIMLRLLEQ-ARMVAQSdvsvlINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESelfghargaftgavs 219
Cdd:COG3604  102 SEEDLRLLETlASLAAVA-----ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES--------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 220 sreglfqaaeggtlfldeigdmpaplqvkllrvLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLN 299
Cdd:COG3604  162 ---------------------------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLN 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 300 VVNLKIPALAERAEDIPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVISDALVE 379
Cdd:COG3604  209 VFPIRLPPLRERREDIPLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLA 288
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 380 qalegentalPTFAEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELE 439
Cdd:COG3604  289 ----------PGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
PRK10820 PRK10820
transcriptional regulator TyrR;
127-368 1.31e-70

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 232.27  E-value: 1.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 127 PSGDDAWRESIVTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESEL 206
Cdd:PRK10820 196 AVNDDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESEL 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 207 FGHARGAFTGAVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMA 286
Cdd:PRK10820 276 FGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQ 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 287 RNEFREDLYYRLNVVNLKIPALAERAEDIPLLANHLLRQAADRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQcvA 366
Cdd:PRK10820 356 KGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYR--A 433

                 ..
gi 654546378 367 LT 368
Cdd:PRK10820 434 LT 435
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
145-438 3.00e-65

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 212.22  E-value: 3.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 145 LRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARGAFTGAVSSREGL 224
Cdd:PRK11608  16 LEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 225 FQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRL--NVVN 302
Cdd:PRK11608  96 FERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLafDVVQ 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 303 LkiPALAERAEDIPLLANHLLRQAA-DRHKPFVRAFSTDAMKRLMAASWPGNVRQLVNVIEQCV--------ALTS---S 370
Cdd:PRK11608 176 L--PPLRERQSDIMLMAEHFAIQMCrELGLPLFPGFTERARETLLNYRWPGNIRELKNVVERSVyrhgtseyPLDNiiiD 253
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546378 371 PVISDALVEQALEGENTALPTFA----EARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHEL 438
Cdd:PRK11608 254 PFKRRPAEEAIAVSETTSLPTLPldlrEWQHQQEKELLQRSLQQAKFNQKRAAELLGLTYHQLRALLKKHQI 325
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
90-444 7.23e-61

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 209.15  E-value: 7.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  90 IPDAvaatQQGVFSFLTKPVDKdaLYKAIDSALEHAAPSGDDawresIVTRSPIMLRLLEQARMVAQSDVSVLINGQSGT 169
Cdd:PRK11388 291 IIEG----QGTSFILLLHPVEQ--MRQLMTSQLGKVSHTFDH-----MPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGV 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 170 GKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHARgafTGAVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKL 249
Cdd:PRK11388 360 GKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLGSDR---TDSENGRLSKFELAHGGTLFLEKVEYLSPELQSAL 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 250 LRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFREDLYYRLNVVNLKIPALAERAEDIPLLANHLLRQAADR 329
Cdd:PRK11388 437 LQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKR 516
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 330 HKPFVRaFSTDAMKRLMAASWPGNVRQLVNVIEQCVALTSSPVI------SDALVEQ-ALEGENTALP---TFAEARNQF 399
Cdd:PRK11388 517 FSTRLK-IDDDALARLVSYRWPGNDFELRSVIENLALSSDNGRIrlsdlpEHLFTEQaTDDVSATRLStslSLAELEKEA 595
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 654546378 400 ELNYLRkllqITKGNVTHAARMAGRNRTEFYKLLSRHELEANDFK 444
Cdd:PRK11388 596 IINAAQ----VCGGRIQEMAALLGIGRTTLWRKMKQHGIDAGQFK 636
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
137-383 1.77e-49

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: 176.18  E-value: 1.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 137 IVTRSPIMLRLLEQARMVA-QSDVSVLINGQSGTGKEILAQAIHN---ASPRSKNAFIAINCGALPEQLLESELFGHARG 212
Cdd:COG4650  186 IATRNAAFNRLIEQIERVAiRSRAPILLTGPTGAGKSQLARRIYElkkARHQVSGRFVEVNCATLRGDGAMSALFGHVKG 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 213 AFTGAVSSREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKVMARNEFRE 292
Cdd:COG4650  266 AFTGAVSDRAGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFRE 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 293 DLYYRLNVVNLKIPALAERAEDIPLLANHLLRQAADRHKPFVRaFSTDAMKRLMA------ASWPGNVRQLVNVIEQCVA 366
Cdd:COG4650  346 DLLARINLWTFRLPGLAERREDIEPNLDYELARFAREQGRRVR-FNKEARARYLAfatspeALWSGNFRDLNASVTRMAT 424
                        250
                 ....*....|....*..
gi 654546378 367 LTSSPVISDALVEQALE 383
Cdd:COG4650  425 LAEGGRITVALVDEEIA 441
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
10-124 9.26e-36

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: 128.38  E-value: 9.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGS 89
Cdd:cd17549    2 LLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHGD 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 654546378  90 IPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEH 124
Cdd:cd17549   82 VPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEK 116
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
10-119 8.82e-35

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 125.34  E-value: 8.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGS 89
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHGD 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 654546378   90 IPDAVAATQQGVFSFLTKPVDKDALYKAID 119
Cdd:pfam00072  82 EDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
9-123 1.00e-34

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: 125.21  E-value: 1.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17569    3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGYA 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  89 SIPDAVAATQQG-VFSFLTKPVDKDALYKAIDSALE 123
Cdd:cd17569   83 DLDAAIEAINEGeIYRFLTKPWDDEELKETIRQALE 118
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
2-127 1.43e-34

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: 125.35  E-value: 1.43e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   2 TSRKPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQK--QQPGM 79
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRAlpRLPDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 654546378  80 PVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAP 127
Cdd:COG0784   81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
10-108 1.80e-32

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 118.48  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGS 89
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 654546378  90 IPDAVAATQQGVFSFLTKP 108
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
6-128 4.59e-31

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: 118.13  E-value: 4.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   6 PAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILT 85
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 654546378  86 AHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPS 128
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAE 123
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
11-126 7.02e-31

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: 117.51  E-value: 7.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  11 LVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGSI 90
Cdd:COG4566    4 IVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHGDV 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  91 PDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAA 126
Cdd:COG4566   84 PMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDR 119
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
9-123 1.07e-30

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: 114.52  E-value: 1.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALE 123
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1-124 2.08e-30

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: 117.19  E-value: 2.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRKPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPG-- 78
Cdd:COG3437    1 MRTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLL-RADPStr 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 654546378  79 -MPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEH 124
Cdd:COG3437   80 dIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALEL 126
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
161-361 2.23e-30

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: 124.45  E-value: 2.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 161 VLINGQSGTGKEILAQAIHN---ASPR-SKNA-FIAINCG--ALPEQLLESELFGHARGAFTGAVSSREGLFQAAEGGTL 233
Cdd:COG1221  133 TLILGPTGVGKSFFAELMYEyaiEIGVlPEDApFVVFNCAdyANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGIL 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 234 FLDEIGDMPAPLQVKLLRVLQERKVRPLG-SNRDIDINVRIISATHRDLPKVMARNEFRedlyyRLNVVnLKIPALAER- 311
Cdd:COG1221  213 FLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPESSLLKTFLR-----RIPMV-IKLPSLEERs 286
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 654546378 312 -AEDIPLLaNHLLRQAADR-HKPFVraFSTDAMKRLMAASWPGNVRQLVNVI 361
Cdd:COG1221  287 lEERLELI-KHFFKEEAKRlNKPIK--VSKEVLKALLLYDCPGNIGQLKSDI 335
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
6-119 7.85e-29

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: 111.54  E-value: 7.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   6 PAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPG---MPVI 82
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRL-RADPRtadIPII 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 654546378  83 ILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAID 119
Cdd:COG3706   80 FLTALDDEEDRARALEAGADDYLTKPFDPEELLARVD 116
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
3-132 1.32e-28

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: 110.78  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   3 SRKPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVI 82
Cdd:COG4567    1 SAEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 654546378  83 ILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDA 132
Cdd:COG4567   81 VLTGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENP 130
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
9-108 4.68e-28

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: 106.78  E-value: 4.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSE-GYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTA 86
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEaGFEVVgEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81
                         90       100
                 ....*....|....*....|..
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKP 108
Cdd:COG4753   82 YSDFEYAQEAIKLGADDYLLKP 103
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
9-124 5.04e-28

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: 107.28  E-value: 5.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEH 124
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKH 116
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
7-121 2.00e-27

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: 105.36  E-value: 2.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTA 86
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKPV-DKDALYKAIDSA 121
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKPIeDLAVLEHAVRRA 116
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
8-117 6.29e-27

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: 104.06  E-value: 6.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAH 87
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 654546378  88 GSIPDAVAATQQGVFSFLTKPVDKDALYKA 117
Cdd:cd17563   82 ASIATAVEAIKLGADDYLAKPADADEILAA 111
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
7-122 1.73e-25

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 100.36  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTA 86
Cdd:cd17537    1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd17537   81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
11-122 2.97e-25

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: 99.65  E-value: 2.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  11 LVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGSI 90
Cdd:cd19919    5 IVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHSDL 84
                         90       100       110
                 ....*....|....*....|....*....|..
gi 654546378  91 PDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd19919   85 DSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
10-108 3.29e-25

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: 99.02  E-value: 3.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGS 89
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*....
gi 654546378  90 IPDAVAATQQGVFSFLTKP 108
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
9-124 4.36e-25

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: 99.33  E-value: 4.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLgMRLV---SEGYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIIL 84
Cdd:cd17536    1 VLIVDDEPLIREGL-KKLIdweELGFEVVgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIIL 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 654546378  85 TAHGsipD---AVAATQQGVFSFLTKPVDKDALYKAIDSALEH 124
Cdd:cd17536   80 SGYD---DfeyAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
7-86 4.34e-24

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 96.14  E-value: 4.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTA 86
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
9-118 8.90e-24

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: 95.23  E-value: 8.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPG---MPVIILT 85
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGgrrTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 654546378  86 AHGSIPDAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
8-123 1.42e-23

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 95.25  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAH 87
Cdd:COG5803    4 KILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTAY 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  88 GSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALE 123
Cdd:COG5803   84 GELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
142-301 2.64e-23

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 95.29  E-value: 2.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 142 PIMLRLLEQARMVAQ--SDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESELFGHargaftGAVS 219
Cdd:cd00009    1 VGQEEAIEALREALElpPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGH------FLVR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378 220 SREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNrdidiNVRIISATHRDLPkvmarNEFREDLYYRLN 299
Cdd:cd00009   75 LLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRPLL-----GDLDRALYDRLD 144

                 ..
gi 654546378 300 VV 301
Cdd:cd00009  145 IR 146
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
5-124 2.77e-23

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 95.04  E-value: 2.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAHLLLVDDDPGLLKLLGmRLVS--EGYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPV 81
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLR-RYLErlPGFEVVgVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 654546378  82 IILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEH 124
Cdd:COG4565   81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEY 123
fixJ PRK09390
response regulator FixJ; Provisional
12-140 4.54e-23

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 96.22  E-value: 4.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  12 VDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGSIP 91
Cdd:PRK09390   9 VDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDVP 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 654546378  92 DAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPS-GDDAWRESIVTR 140
Cdd:PRK09390  89 LAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEAaKSEAVAADIRAR 138
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
9-108 5.19e-22

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: 90.13  E-value: 5.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQP--GMPVIILTA 86
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADfdTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKP 108
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
10-118 5.35e-22

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: 90.59  E-value: 5.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPG--MPVIILTAH 87
Cdd:cd17580    2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLanTPAIALTGY 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 654546378  88 GSIPDAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:cd17580   82 GQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
10-123 6.29e-22

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


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 90.26  E-value: 6.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDP----GLLKLLGMRlvsEGYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIIL 84
Cdd:cd17535    2 LIVDDHPlvreGLRRLLESE---PDIEVVgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVL 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALE 123
Cdd:cd17535   79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
10-159 1.96e-20

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 89.88  E-value: 1.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLgMRLVSE--GYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTA 86
Cdd:COG3279    5 LIVDDEPLARERL-ERLLEKypDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTA 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654546378  87 HgsiPD-AVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPSGDDAWRESIVTRspIMLRLLEQARMVAQSDV 159
Cdd:COG3279   84 Y---DEyALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKDR--IFVKSGGKLVKIPLDDI 152
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
8-109 2.84e-20

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: 85.24  E-value: 2.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPG---MPVIIL 84
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRL-KEDPEtrhIPVIMI 79
                         90       100
                 ....*....|....*....|....*
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKPV 109
Cdd:cd17538   80 TALDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
10-108 1.70e-19

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: 83.48  E-value: 1.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQP--GMPVIILTAH 87
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKtsSIPIIMLTAK 80
                         90       100
                 ....*....|....*....|.
gi 654546378  88 GSIPDAVAATQQGVFSFLTKP 108
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKP 101
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
8-122 2.12e-18

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: 80.67  E-value: 2.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSE-GYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQkQQP---GMPVII 83
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQ-ANPetqSIPVIL 81
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 654546378  84 LTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd17552   82 LTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
7-118 2.14e-18

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: 80.81  E-value: 2.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQ--QPGMPVIIL 84
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLpaYKFTPILML 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:cd17562   81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
pleD PRK09581
response regulator PleD; Reviewed
1-120 2.24e-18

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 86.88  E-value: 2.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRkpahLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPG-- 78
Cdd:PRK09581   1 MTAR----ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRL-KSDPAtt 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 654546378  79 -MPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDS 120
Cdd:PRK09581  76 hIPVVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKS 118
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
138-308 2.33e-18

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 81.23  E-value: 2.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  138 VTRSPIMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLESelfghargaftga 217
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  218 vssreglfqaAEGGTLFLDEIGDMPAPLQVKLLRVLQERKvrplgsnrdiDINVRIISATHRDLPKVMARNEFREDLYYR 297
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 654546378  298 LNVVNLKIPAL 308
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
9-108 2.34e-18

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: 80.24  E-value: 2.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREK-IDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAH 87
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81
                         90       100
                 ....*....|....*....|.
gi 654546378  88 GSIPDAVAATQQGVFSFLTKP 108
Cdd:cd18160   82 AAAAPELLSDAVGDNATLKKP 102
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
10-108 2.46e-18

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: 79.89  E-value: 2.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGS 89
Cdd:cd19926    2 LVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYGS 81
                         90
                 ....*....|....*....
gi 654546378  90 IPDAVAATQQGVFSFLTKP 108
Cdd:cd19926   82 LDTAIEALKAGAFDFLTKP 100
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
10-122 4.31e-18

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: 79.76  E-value: 4.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVV-TAESGQEGLKVLSREKIDLVISDLRM-DEMDGMQLFAEIQKQQPgMPVIILTAH 87
Cdd:cd17534    4 LIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLkGDMDGIEAAREIREKFD-IPVIFLTAY 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  88 gSIPDAVA-ATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd17534   83 -SDEETLErAKETNPYGYLVKPFNERELKAAIELAL 117
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
10-118 8.86e-18

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: 78.74  E-value: 8.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLfAEIQKQQPG---MPVIILTA 86
Cdd:cd17548    3 LIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEA-TRLLKEDPAtrdIPVIALTA 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:cd17548   82 YAMKGDREKILEAGCDGYISKPIDTREFLETV 113
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
9-108 1.48e-17

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


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 78.16  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKP 101
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
10-122 2.20e-17

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: 77.65  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGS 89
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 654546378  90 IPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
10-122 2.53e-17

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: 77.70  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17542    4 LIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAMG 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd17542   84 QEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
orf27 CHL00148
Ycf27; Reviewed
1-122 5.07e-17

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 80.15  E-value: 5.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRKpAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQpGMP 80
Cdd:CHL00148   2 MENSK-EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES-DVP 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 654546378  81 VIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:CHL00148  80 IIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
9-123 5.95e-17

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 77.02  E-value: 5.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLgMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17596    3 ILVVDDEVRSLEAL-RRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  89 SIPDAVAATQQ-GVFSFLTKPVDKDALYKAIDSALE 123
Cdd:cd17596   82 DSEDIIAGINEaGIYQYLTKPWHPDQLLLTVRNAAR 117
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
9-114 6.83e-17

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 76.21  E-value: 6.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGM---PVIILT 85
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKI-KSDPDLkdiPVILLT 79
                         90       100
                 ....*....|....*....|....*....
gi 654546378  86 AHGSIPDAVAATQQGVFSFLTKPVDKDAL 114
Cdd:cd17598   80 TLSDPRDVIRGLECGADNFITKPYDEKYL 108
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
9-109 1.34e-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: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQP---GMPVIILT 85
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRL-KADPatrHIPVIFLT 79
                         90       100
                 ....*....|....*....|....
gi 654546378  86 AHGSIPDAVAATQQGVFSFLTKPV 109
Cdd:cd19920   80 ALTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
10-108 1.48e-16

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: 74.89  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAHGS 89
Cdd:cd17620    2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRL-REWSAVPVIVLSARDE 80
                         90
                 ....*....|....*....
gi 654546378  90 IPDAVAATQQGVFSFLTKP 108
Cdd:cd17620   81 ESDKIAALDAGADDYLTKP 99
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-125 1.69e-16

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 77.30  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRKpahLLLVDDDPGLLKLLGMRLVSEGYTVVT-AESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPgM 79
Cdd:COG3707    1 MRGLR---VLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-A 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654546378  80 PVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHA 125
Cdd:COG3707   77 PVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARF 122
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
10-114 1.75e-16

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 74.97  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLS--REKIDLVISDLRMDEMDGMQLFAEIQKqQPGMPVIILTAH 87
Cdd:cd17584    2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIRL-EMDLPVIMMSAD 80
                         90       100
                 ....*....|....*....|....*..
gi 654546378  88 GSIPDAVAATQQGVFSFLTKPVDKDAL 114
Cdd:cd17584   81 GSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
9-108 6.21e-16

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: 73.47  E-value: 6.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKP 100
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
7-110 6.63e-16

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: 73.63  E-value: 6.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYT-VVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGM---PVI 82
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGYLeVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRL-RALPGLedvPIV 79
                         90       100
                 ....*....|....*....|....*...
gi 654546378  83 ILTAHGSIPDAVAATQQGVFSFLTKPVD 110
Cdd:cd17551   80 MITADTDREVRLRALEAGATDFLTKPFD 107
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
9-108 9.57e-16

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: 72.47  E-value: 9.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVKP 100
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
9-108 1.54e-15

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: 72.46  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQpGMPVIILTAHG 88
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKP 99
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
9-110 2.93e-15

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 71.75  E-value: 2.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90       100
                 ....*....|....*....|..
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVD 110
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFA 102
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
9-122 3.99e-15

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: 71.60  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVT-AESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEI--QKQQPGMPVIILT 85
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIraDGALSHLPVLMVT 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 654546378  86 AHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd19923   83 AEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
9-122 4.37e-15

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: 71.43  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd17553   83 ELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
9-110 6.42e-15

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 70.80  E-value: 6.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAHG 88
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKEL-RKTSQVPVLMLTARG 79
                         90       100
                 ....*....|....*....|..
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVD 110
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFN 101
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
11-108 1.53e-14

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: 69.01  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  11 LVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAHGSI 90
Cdd:cd19936    3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRL-RQKSTLPVIFLTSKDDE 81
                         90
                 ....*....|....*...
gi 654546378  91 PDAVAATQQGVFSFLTKP 108
Cdd:cd19936   82 IDEVFGLRMGADDYITKP 99
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
9-122 1.58e-14

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: 69.75  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGmPVIILTAH 87
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLTAY 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 654546378  88 GSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd19932   82 SQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAI 116
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
8-120 1.78e-14

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 69.75  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPG--LLKLLGMRLVSEGYTVVTAESGQEGLKVLSRE-------KIDLVISDLRMDEMDGMQLFAEIqKQQPG 78
Cdd:cd17557    1 TILLVEDNPGdaELIQEAFKEAGVPNELHVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREI-KADPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 654546378  79 ---MPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDS 120
Cdd:cd17557   80 lrrIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
9-108 2.26e-14

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: 69.33  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKP 100
ompR PRK09468
osmolarity response regulator; Provisional
8-147 4.62e-14

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 71.54  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAH 87
Cdd:PRK09468   7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAK 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654546378  88 GSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEH------AAPSGDDAwresIVTRSPIMLRL 147
Cdd:PRK09468  87 GEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRqapelpGAPSQEEE----VIAFGKFKLNL 148
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
9-108 1.51e-13

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: 66.37  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
9-122 1.72e-13

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 69.83  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSrEKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAHG 88
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKEL-RQTHQTPVIMLTARG 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:PRK10955  82 SELDRVLGLELGADDYLPKPFNDRELVARIRAIL 115
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
9-114 1.89e-13

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 66.66  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100
                 ....*....|....*....|....*.
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDAL 114
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDEL 106
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
7-108 4.28e-13

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 65.49  E-value: 4.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTA 86
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTREL-REQSEVGIILVTG 79
                         90       100
                 ....*....|....*....|..
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKP 108
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKP 101
resp_reg_YycF NF040534
response regulator YycF;
9-136 5.85e-13

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 68.21  E-value: 5.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQpGMPVIILTAHG 88
Cdd:NF040534   3 ILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKY-DMPIIMLTAKD 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL-EHAAPSGDDAWRES 136
Cdd:NF040534  82 SEIDKVLGLELGADDYVTKPFSTRELIARVKANLrRHQQQNTEEEEEEN 130
PRK10643 PRK10643
two-component system response regulator PmrA;
9-108 1.39e-12

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 66.98  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKP 102
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
8-114 1.90e-12

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 69.62  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAh 87
Cdd:PRK10841 803 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTA- 881
                         90       100       110
                 ....*....|....*....|....*....|..
gi 654546378  88 gsipDAVAATQQ-----GVFSFLTKPVDKDAL 114
Cdd:PRK10841 882 ----NALAEEKQrcleaGMDSCLSKPVTLDVL 909
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
8-60 1.90e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.82  E-value: 1.90e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 654546378     8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRM 60
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMM 54
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
8-120 2.57e-12

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: 63.32  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLgMRLVSEGY--TVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILT 85
Cdd:cd17593    2 KVLICDDSSMARKQL-ARALPADWdvEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 654546378  86 ahGSI-PDAVAATQQ-GVFSFLTKPVDKDALYKAIDS 120
Cdd:cd17593   81 --GDVqPEAKERVLElGALAFLKKPFDPEKLAQLLEE 115
PRK15479 PRK15479
transcriptional regulator TctD;
9-114 4.84e-12

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 65.13  E-value: 4.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARS 82
                         90       100
                 ....*....|....*....|....*.
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDAL 114
Cdd:PRK15479  83 AVADRVKGLNVGADDYLPKPFELEEL 108
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
10-85 5.40e-12

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: 61.98  E-value: 5.40e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSRE-KIDLVISDLRM-DEMDGMQLFAEIQKQQPGMPVIILT 85
Cdd:cd18161    2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMpGGMNGSQLAEEARRRRPDLKVLLTS 79
PRK15347 PRK15347
two component system sensor kinase;
8-123 6.30e-12

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 67.74  E-value: 6.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFA----EIQKQQPGMPVII 83
Cdd:PRK15347 692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQlwrdDPNNLDPDCMIVA 771
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 654546378  84 LTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALE 123
Cdd:PRK15347 772 LTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALELAAE 811
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
7-108 1.17e-11

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 61.33  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTA 86
Cdd:cd17626    1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQI-RAESGVPIVMLTA 79
                         90       100
                 ....*....|....*....|..
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKP 108
Cdd:cd17626   80 KSDTVDVVLGLESGADDYVAKP 101
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
8-119 1.35e-11

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 61.49  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVS-EGYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILT 85
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEQvPGFTVIgTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVT 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 654546378  86 AHGSIPDAVAATQQGVFSFLTKPVDKDALYKAID 119
Cdd:cd19925   82 AANDVETVREALRLGVVDYLIKPFTFERLRQRLE 115
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
10-108 1.88e-11

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: 61.00  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREK-IDLVISDLRMDEMDGMQLFAEIQKQQP--GMPVIILTA 86
Cdd:cd17544    4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSrdQLAIIGISA 83
                         90       100
                 ....*....|....*....|..
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKP 108
Cdd:cd17544   84 SGDNALSARFIKAGANDFLTKP 105
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
9-108 2.80e-11

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 60.08  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLS---------REKIDLVISDLRMDEMDGMQLFAEIqKQQPGM 79
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFEL-RDDPRL 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 654546378  80 ---PVIILTAHGSIPDAVAATQQGVFSFLTKP 108
Cdd:cd19924   80 aniPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
7-108 6.07e-11

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: 59.57  E-value: 6.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPG--MPVIIL 84
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTrdIPIIML 80
                         90       100
                 ....*....|....*....|....
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKP 108
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKP 104
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
8-110 1.34e-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: 58.23  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAH 87
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTI-RARSDVPIIIISGD 79
                         90       100
                 ....*....|....*....|....
gi 654546378  88 -GSIPDAVAATQQGVFSFLTKPVD 110
Cdd:cd17594   80 rRDEIDRVVGLELGADDYLAKPFG 103
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
6-158 1.43e-10

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 60.97  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   6 PAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILT 85
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDL-RQWSAIPVIVLS 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654546378  86 AHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL-EHAAPSGDDawreSIVTRSPIMLRLLeqARMVAQSD 158
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALrRHSATPAPD----PLVKFSDVTVDLA--ARVIHRGE 147
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
10-118 2.53e-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: 57.55  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDP----GLLKLL----GMRLVSEgytvvtAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKqQPGMPV 81
Cdd:cd17532    2 LIVDDEPlareELRYLLeehpDIEIVGE------AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSK-LAKPPL 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 654546378  82 II-LTAHGSIpdAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:cd17532   75 IVfVTAYDEY--AVEAFELNAVDYLLKPFSEERLAEAL 110
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
10-108 2.77e-10

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 57.79  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSE-GYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPgMPVIILTAH 87
Cdd:cd17541    4 LIVDDSAVMRKLLSRILESDpDIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVSSL 82
                         90       100
                 ....*....|....*....|...
gi 654546378  88 GS--IPDAVAATQQGVFSFLTKP 108
Cdd:cd17541   83 TEegAEITLEALELGAVDFIAKP 105
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
9-110 3.35e-10

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 57.39  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGmPVIILTAHG 88
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG-PILLLTALD 81
                         90       100
                 ....*....|....*....|..
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVD 110
Cdd:cd17622   82 SDIDHILGLELGADDYVVKPVE 103
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
9-122 4.16e-10

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 56.91  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPgMPVIILTAHG 88
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSRD 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
160-298 4.17e-10

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 58.15  E-value: 4.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   160 SVLINGQSGTGKEILAQAIHNASPRSKNAFIAINCGALPEQLLE--SELFGHARGAFTGAVSSREGLFQAAEG---GTLF 234
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDqlLLIIVGGKKASGSGELRLRLALALARKlkpDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654546378   235 LDEIGDMPAPLQVKLLRVLQERKVrplGSNRDIDINVRIISATHR--DLPKVMARNEFREDLYYRL 298
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEELRL---LLLLKSEKNLTVILTTNDekDLGPALLRRRFDRRIVLLL 146
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-118 6.21e-10

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 61.40  E-value: 6.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRKPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQP--- 77
Cdd:PRK11107 662 DESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELI-RQLPhnq 740
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654546378  78 GMPVIILTAHgsipdAVAA-----TQQGVFSFLTKPVDKDALYKAI 118
Cdd:PRK11107 741 NTPIIAVTAH-----AMAGererlLSAGMDDYLAKPIDEAMLKQVL 781
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1-162 8.88e-10

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 58.50  E-value: 8.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRKPAHLLLVDDDP----GLLKLLGMrlvSEGYTVVT-AESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQ 75
Cdd:PRK10651   1 MSNQEPATILLIDDHPmlrtGVKQLISM---APDITVVGeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  76 QPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIdsaleHAAPSGDDAWRESIvtrSPIMLRLLEQARMVA 155
Cdd:PRK10651  78 SLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKAL-----QQAAAGEMVLSEAL---TPVLAASLRANRATT 149

                 ....*..
gi 654546378 156 QSDVSVL 162
Cdd:PRK10651 150 ERDVNQL 156
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
11-109 1.19e-09

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 55.36  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  11 LVDDDPGLLKLLGMRLVSE--GYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGmPVIILTAHG 88
Cdd:cd17565    3 IVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSN-GKFIMISQV 81
                         90       100
                 ....*....|....*....|..
gi 654546378  89 SIPDAVA-ATQQGVFSFLTKPV 109
Cdd:cd17565   82 SDKEMIGkAYQAGIEFFINKPI 103
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
9-123 1.44e-09

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: 56.19  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGM---RLVSEGYTVVTAESGQEGLKVLSR-----EKIDLVISDLRMDEMDGMQLFAEIQKQQPGMP 80
Cdd:cd17595    3 ILTVDDDPQVLRAVARdlrRQYGKDYRVLRADSGAEALDALKElklrgEAVALFLVDQRMPEMDGVEFLEKAMELFPEAK 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654546378  81 VIILTAHGSIPDAVAATQQ-GVFSFLTKPVD--KDALYKAIDSALE 123
Cdd:cd17595   83 RVLLTAYADTDAAIRAINDvQLDYYLLKPWDppEEKLYPVLDDLLD 128
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
9-108 1.63e-09

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 54.90  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAHG 88
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQL-RARSNVPVIMVTAKD 79
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
PRK10610 PRK10610
chemotaxis protein CheY;
5-123 2.14e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 55.37  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAHLLLVDDDP-------GLLKLLGMRLVSEgytvvtAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQK--Q 75
Cdd:PRK10610   4 KELKFLVVDDFStmrrivrNLLKELGFNNVEE------AEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRAdgA 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 654546378  76 QPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALE 123
Cdd:PRK10610  78 MSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
9-118 4.05e-09

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: 53.97  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
9-123 1.08e-08

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 53.04  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLG--MRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTA 86
Cdd:cd19930    1 VLIAEDQEMVRGALAalLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 654546378  87 H---GSIPDAVAAtqqGVFSFLTKPVDKDALYKAIDSALE 123
Cdd:cd19930   81 FgrpGYFRRALAA---GVDGYVLKDRPIEELADAIRTVHA 117
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
8-109 1.57e-08

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 52.38  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAH 87
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREV-REHSHVPILMLTAR 79
                         90       100
                 ....*....|....*....|..
gi 654546378  88 GSIPDAVAATQQGVFSFLTKPV 109
Cdd:cd19939   80 TEEMDRVLGLEMGADDYLCKPF 101
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
9-108 6.20e-08

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: 50.48  E-value: 6.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREK--IDLVISDLRMDEMDGMQLFAEI--QKQQPGMPVIIL 84
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQneIDLILTEVDLPVSSGFKLLSYImrHKICKNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKP 108
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
PRK13557 PRK13557
histidine kinase; Provisional
8-129 7.25e-08

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 54.68  E-value: 7.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSRE-KIDLVISDLRM-DEMDGMQLFAEIQKQQPGMPVIILT 85
Cdd:PRK13557 417 TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMpGGMNGVMLAREARRRQPKIKVLLTT 496
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654546378  86 --AHGSIPDAVAATQQgvFSFLTKPVDKDALYKAIDSALEhaAPSG 129
Cdd:PRK13557 497 gyAEASIERTDAGGSE--FDILNKPYRRAELARRVRMVLD--GPTG 538
PRK10766 PRK10766
two-component system response regulator TorR;
8-110 8.01e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 52.73  E-value: 8.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPgllkLLGMRLVS----EGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVII 83
Cdd:PRK10766   4 HILVVEDEP----VTRARLQGyfeqEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTREL-RSRSTVGIIL 78
                         90       100
                 ....*....|....*....|....*..
gi 654546378  84 LTAHGSIPDAVAATQQGVFSFLTKPVD 110
Cdd:PRK10766  79 VTGRTDSIDRIVGLEMGADDYVTKPLE 105
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
6-72 1.02e-07

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 50.66  E-value: 1.02e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654546378   6 PAHLLLVDDDPGLLKLLGMRLVSE-GYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEI 72
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEpDIEVVgEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
12-108 1.15e-07

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: 49.67  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  12 VDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQ--PGMPVIILTAHGS 89
Cdd:cd17602    4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSalKDTPIIMLTGKDG 83
                         90
                 ....*....|....*....
gi 654546378  90 IPDAVAATQQGVFSFLTKP 108
Cdd:cd17602   84 LVDRIRAKMAGASGYLTKP 102
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
9-185 1.27e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 52.23  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAPsgddAWRESIVTRSPIMLRLLeqARMVAQSDVSVLINGQSG 168
Cdd:PRK09836  83 TIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAA----VIIESQFQVADLMVDLV--SRKVTRSGTRITLTSKEF 156
                        170
                 ....*....|....*..
gi 654546378 169 TGKEILAQAIHNASPRS 185
Cdd:PRK09836 157 TLLEFFLRHQGEVLPRS 173
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
9-114 1.85e-07

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 49.32  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDP---GLLKLLGMRLvseGYTVVTAESGQEGLKVLSREK--IDLVISDLRMDEMDGMQLFAEIQKQQPGM--PV 81
Cdd:cd19933    3 VLLVDDNAvnrMVTKGLLEKL---GCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRKLFGRRerPL 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 654546378  82 II-LTAHGSIPDAVAATQQGVFSFLTKPVDKDAL 114
Cdd:cd19933   80 IVaLTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
7-108 2.25e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 51.50  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   7 AHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTA 86
Cdd:PRK11083   4 PTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTA 83
                         90       100
                 ....*....|....*....|..
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKP 108
Cdd:PRK11083  84 RSDEVDRLVGLEIGADDYVAKP 105
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
9-158 3.05e-07

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 52.81  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378    9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546378   89 SIPDAVAATQQGVFSFLTKPVDKDALYKAIDS--ALEHAAPSGDDAWRESIVTRSPIMLRLLEQARMVAQSD 158
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQlhQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHE 1112
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
8-108 3.44e-07

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: 48.53  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAH 87
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREI-RRFSDVPIIMVTAR 79
                         90       100
                 ....*....|....*....|.
gi 654546378  88 GSIPDAVAATQQGVFSFLTKP 108
Cdd:cd19938   80 VEEIDRLLGLELGADDYICKP 100
PRK11517 PRK11517
DNA-binding response regulator HprR;
9-108 9.75e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 49.51  E-value: 9.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPgMPVIILTAHG 88
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQ-TPVICLTARD 81
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:PRK11517  82 SVDDRVRGLDSGANDYLVKP 101
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
10-109 1.22e-06

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 47.36  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSRE-----------KIDLVISDLRMDEMDGMQLFAEIQKQQP- 77
Cdd:cd17581    2 LAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEdeedssnfnepKVNMIITDYCMPGMTGYDLLKKVKESSAl 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 654546378  78 -GMPVIILTAHGSIPDAVAATQQGVFSFLTKPV 109
Cdd:cd17581   82 kEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1-118 1.97e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 48.70  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRKPAHLLLVDDDP----GLLKLLGMRLVSEgyTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQ 76
Cdd:PRK10403   1 MPEATPFQVLIVDDHPlmrrGVRQLLELDPGFE--VVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 654546378  77 PGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:PRK10403  79 VTAQIIILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAI 120
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
9-122 2.17e-06

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: 46.57  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDP----GLLKLLGMrlvSEGYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVII 83
Cdd:cd19931    1 VLLIDDHPllrkGIKQLIEL---DPDFTVVgEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVI 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 654546378  84 LTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:cd19931   78 LTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAA 116
PRK10693 PRK10693
two-component system response regulator RssB;
36-109 2.41e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 49.22  E-value: 2.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654546378  36 AESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPV 109
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPV 76
PRK10816 PRK10816
two-component system response regulator PhoP;
9-108 3.56e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 47.81  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKP 102
PRK10336 PRK10336
two-component system response regulator QseB;
9-108 4.25e-06

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 47.58  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82
                         90       100
                 ....*....|....*....|
gi 654546378  89 SIPDAVAATQQGVFSFLTKP 108
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKP 102
PRK09483 PRK09483
response regulator; Provisional
10-118 5.61e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 47.02  E-value: 5.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPglLKLLGMRLVSE---GYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILT 85
Cdd:PRK09483   5 LLVDDHE--LVRAGIRRILEdikGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLT 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 654546378  86 AHGSIPDAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:PRK09483  83 VHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAI 115
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
9-127 6.11e-06

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 47.41  E-value: 6.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQ--QPGMPVIILTA 86
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKREsmTRDIPVVMLTA 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSALEHAAP 127
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISP 125
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
9-109 9.40e-06

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


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 44.39  E-value: 9.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:cd19922    1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDHWE 80
                         90       100
                 ....*....|....*....|.
gi 654546378  89 SIPDAVAATQQGVFSFLTKPV 109
Cdd:cd19922   81 DLQEELEEVQRFAVSYVVKPV 101
PRK10360 PRK10360
transcriptional regulator UhpA;
9-156 1.39e-05

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 45.74  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDD----PGLLKLLGMrlvsEGYTVVTAE--SGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKqqpGMPVI 82
Cdd:PRK10360   4 VALIDDHlivrSGFAQLLGL----EPDLQVVAEfgSGREALAGLPGRGVQVCICDISMPDISGLELLSQLPK---GMATI 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654546378  83 ILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSalehAAPSG-----DDAWRESIVTRSPIMLRLLEQARMVAQ 156
Cdd:PRK10360  77 MLSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHT----VATGGcyltpDIAIKLASGRQDPLTKRERQVAEKLAQ 151
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
9-114 2.95e-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: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGY-TVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAH 87
Cdd:cd17530    3 VLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSGL 82
                         90       100       110
                 ....*....|....*....|....*....|..
gi 654546378  88 GSIPDAVAATQQG-----VFSFLTKPVDKDAL 114
Cdd:cd17530   83 DGGILESAETLAGanglnLLGTLSKPFSPEEL 114
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
10-121 2.97e-05

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 44.89  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPglLKLLGMR--LVSEGYTVVTA-ESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTA 86
Cdd:PRK09958   4 IIIDDHP--LAIAAIRnlLIKNDIEILAElTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSA 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSA 121
Cdd:PRK09958  82 KNDHFYGKHCADAGANGFVSKKEGMNNIIAAIEAA 116
PRK13856 PRK13856
two-component response regulator VirG; Provisional
8-108 3.19e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 45.19  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQpGMPVIILT-A 86
Cdd:PRK13856   3 HVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATKS-DVPIIIISgD 81
                         90       100
                 ....*....|....*....|..
gi 654546378  87 HGSIPDAVAATQQGVFSFLTKP 108
Cdd:PRK13856  82 RLEEADKVVALELGATDFIAKP 103
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
10-114 3.29e-05

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 43.07  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEgYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQ--KQQPGMPVIILTAH 87
Cdd:cd17539    2 LLVDDRPSSAERIAAMLSSE-HEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRslERTRQLPILAVADP 80
                         90       100
                 ....*....|....*....|....*..
gi 654546378  88 GSIPDAVAATQQGVFSFLTKPVDKDAL 114
Cdd:cd17539   81 GDRGRLIRALEIGVNDYLVRPIDPNEL 107
PRK11697 PRK11697
two-component system response regulator BtsR;
10-119 4.02e-05

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 44.84  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYTVVTAESGQ--EGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQpgMP-VIILTA 86
Cdd:PRK11697   5 LIVDDEPLAREELRELLQEEGDIEIVGECSNaiEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPEH--MPyIVFVTA 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 654546378  87 HgsipD--AVAATQQGVFSFLTKPVDKDALYKAID 119
Cdd:PRK11697  83 F----DeyAIKAFEEHAFDYLLKPIDPARLAKTLA 113
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
9-123 5.38e-05

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 45.67  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSR-EKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAH 87
Cdd:PRK11466 684 LLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNsEPFAAALVDFDLPDYDGITLARQLAQQYPSLVLIGFSAH 763
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 654546378  88 gSIPDAVAATQQGVF-SFLTKPVDKDALYKAIDSALE 123
Cdd:PRK11466 764 -VIDETLRQRTSSLFrGIIPKPVPREVLGQLLAHYLQ 799
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
9-88 6.87e-05

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: 41.83  E-value: 6.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVS-EGYTVV-TAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQ-KQQPGMP-VIIL 84
Cdd:cd17561    4 VLIADDNREFVQLLEEYLNSqPDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRrMRLEKRPkIIML 83

                 ....
gi 654546378  85 TAHG 88
Cdd:cd17561   84 TAFG 87
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
160-279 7.88e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 42.28  E-value: 7.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  160 SVLINGQSGTGK----EILAQAIHNASPRSKnafiaincgALPEQLLESELFGHARGAFTGAVSSREGLFQAA-EGGTLF 234
Cdd:pfam07728   1 GVLLVGPPGTGKtelaERLAAALSNRPVFYV---------QLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAArEGEIAV 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 654546378  235 LDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDI---NVRIISATHR 279
Cdd:pfam07728  72 LDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLIATMNP 119
PLN03029 PLN03029
type-a response regulator protein; Provisional
1-109 1.03e-04

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 43.48  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   1 MTSRKPAHLLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLS-------------------RE-KIDLVISDLRM 60
Cdd:PLN03029   3 ITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddrsnpdtpsvspnshQEvEVNLIITDYCM 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 654546378  61 DEMDGMQLFAEIQKQQP--GMPVIILTAHgSIPDAVA-ATQQGVFSFLTKPV 109
Cdd:PLN03029  83 PGMTGYDLLKKIKESSSlrNIPVVIMSSE-NVPSRITrCLEEGAEEFFLKPV 133
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
10-122 1.83e-04

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: 41.08  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPgllkLLGMRL----VSEGYTVV-TAESGQEGLKVLSREKIDLVISDLRM-DEMDGMQLFAEIQKQQPgMPVII 83
Cdd:cd17540    4 LIIEDEP----LIAMDLeqivEDLGHQVVgIARTRDEAVALARRERPDLILADIQLaDGSSGIDAVNEILTTHD-VPVIF 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 654546378  84 LTAHgsiPDAVAATQQGVFSFL-TKPVDKDALYKAIDSAL 122
Cdd:cd17540   79 VTAY---PERLLTGERPEPTFLiTKPFDPEMVKAAISQAL 115
pleD PRK09581
response regulator PleD; Reviewed
5-114 3.13e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 42.97  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAHLLLVDDDPGLLKLLGmRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQP--GMPVI 82
Cdd:PRK09581 154 EDGRILLVDDDVSQAERIA-NILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERtrYVPIL 232
                         90       100       110
                 ....*....|....*....|....*....|..
gi 654546378  83 ILTAHGSIPDAVAATQQGVFSFLTKPVDKDAL 114
Cdd:PRK09581 233 LLVDEDDDPRLVKALELGVNDYLMRPIDKNEL 264
PRK11173 PRK11173
two-component response regulator; Provisional
29-108 3.50e-04

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 41.92  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  29 EGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIqKQQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKP 108
Cdd:PRK11173  26 EGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLAREL-REQANVALMFLTGRDNEVDKILGLEIGADDYITKP 104
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
10-114 3.86e-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: 39.94  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378  10 LLVDDDPGLLKLLGMRLVSEGYT-VVTAESGQEGLKVLSREKIDLVISDLRM-DEMDGMQLFAEIQKQQ---PGMPVIIL 84
Cdd:cd17589    2 LIVDDQPTFRSMLKSMLRSLGVTrIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELRHKKlisPSTVFIMV 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 654546378  85 TAHGSIPDAVAATQQGVFSFLTKPVDKDAL 114
Cdd:cd17589   82 TGESSRAMVLSALELEPDDYLLKPFTVSEL 111
PRK13558 PRK13558
bacterio-opsin activator; Provisional
9-151 7.20e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 42.13  E-value: 7.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMPVIILTAHG 88
Cdd:PRK13558  10 VLFVGDDPEAGPVDCDLDEDGRLDVTQIRDFVAARDRVEAGEIDCVVADHEPDGFDGLALLEAVRQTTAVPPVVVVPTAG 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654546378  89 SIPDAVAATQQGVFSFLtkPVDKDALYKAIDSALEHAAPSGD-DAWRESIVTRSPIM--LRLLEQA 151
Cdd:PRK13558  90 DEAVARRAVDADAAAYV--PAVSDDATAAIAERIESAVPEHSrDTEARMPISDLTVEsdRRLKERA 153
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
9-85 2.82e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 39.23  E-value: 2.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654546378   9 LLLVDDDPGLLKLLGMRLVSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGmPVIILT 85
Cdd:PRK10701   4 IVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG-PIVLLT 79
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
5-122 5.72e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 37.93  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAHLLLVDDDP----GLLKLLGMRlvSEGYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGMP 80
Cdd:PRK09935   2 KPASVIIMDTHPiirmSIEVLLQKN--SELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVK 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 654546378  81 VIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSAL 122
Cdd:PRK09935  80 VLFLSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMIL 121
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
8-118 6.04e-03

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 39.15  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   8 HLLLVDDDPglLKLLGMRLVSE--GYTVVTAESGQEGLKVLSREKIDLVISDLRMDEMDGMQLFAEIQKQQPGM---PVI 82
Cdd:PRK11091 527 NILLVEDIE--LNVIVARSVLEklGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREdlpPLV 604
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654546378  83 ILTAHgSIPDAVAATQQGVFSFLTKPVDKDALYKAI 118
Cdd:PRK11091 605 ALTAN-VLKDKKEYLDAGMDDVLSKPLSVPALTAMI 639
PRK15369 PRK15369
two component system response regulator;
5-121 6.36e-03

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 37.75  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546378   5 KPAHLLLVDDDPGLLK-LLGMRLVSEGYTVVtaESGQEGLKVLS---REKIDLVISDLRMDEMDGMQLFAEIQKQQPGMP 80
Cdd:PRK15369   2 KNYKILLVDDHELIINgIKNMLAPYPRYKIV--GQVDNGLEVYNacrQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMN 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 654546378  81 VIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYKAIDSA 121
Cdd:PRK15369  80 ILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTV 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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