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Conserved domains on  [gi|15599920|ref|NP_253414|]
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two-component response regulator CbrB [Pseudomonas aeruginosa PAO1]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-466 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: 517.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMT 76
Cdd:COG2204   2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRelraLDPDLPVILLT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSanggkaggergaspavadgeiGIIGSCAPM 156
Cdd:COG2204  82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS---------------------GLIGRSPAM 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 157 QELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 236
Cdd:COG2204 141 QEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 237 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLK 316
Cdd:COG2204 221 FELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 317 LPALRERGNDVMEIARAFLARQCTRMGRaPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLLgidiel 396
Cdd:COG2204 301 LPPLRERREDIPLLARHFLARFAAELGK-PVKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDL------ 373
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599920 397 ddleddfaadlglgpagaaasnhepteDLSLEDYFQHFVLE----HQDHMTETelARKLGISRKCLWERRQRLG 466
Cdd:COG2204 374 ---------------------------PEALEEVERELIERaleeTGGNVSRA--AELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-466 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: 517.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMT 76
Cdd:COG2204   2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRelraLDPDLPVILLT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSanggkaggergaspavadgeiGIIGSCAPM 156
Cdd:COG2204  82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS---------------------GLIGRSPAM 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 157 QELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 236
Cdd:COG2204 141 QEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 237 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLK 316
Cdd:COG2204 221 FELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 317 LPALRERGNDVMEIARAFLARQCTRMGRaPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLLgidiel 396
Cdd:COG2204 301 LPPLRERREDIPLLARHFLARFAAELGK-PVKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDL------ 373
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599920 397 ddleddfaadlglgpagaaasnhepteDLSLEDYFQHFVLE----HQDHMTETelARKLGISRKCLWERRQRLG 466
Cdd:COG2204 374 ---------------------------PEALEEVERELIERaleeTGGNVSRA--AELLGISRRTLYRKLKKYG 418
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-439 1.82e-128

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: 380.62  E-value: 1.82e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920     4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLIMTSYA 79
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLpqikKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAapvsanggkaggerGASPAVADGEIGIIGSCAPMQEL 159
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVAL--------------PADAGEAEDSAELIGEAPAMQEV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   160 YSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEA 239
Cdd:TIGR01818 147 FRAIGRLSRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   240 ADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPA 319
Cdd:TIGR01818 227 ADGGTLFLDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPP 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   320 LRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLLgidielddl 399
Cdd:TIGR01818 307 LRERREDIPRLARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDL--------- 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 15599920   400 eddfAADLGLGPAGAAASNHEPTEDLS--LEDYFQHFVLEHQ 439
Cdd:TIGR01818 378 ----PAELALTGRPASAPDSDGQDSWDeaLEAWAKQALSRGE 415
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-464 1.15e-122

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 365.12  E-value: 1.15e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSYA 79
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKeikaLNPAIPVLIMTAYS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRsaapvsanggkaggerGASPAVADGEIGIIGSCAPMQEL 159
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSID----------------AETPAVTASQFGMVGKSPAMQHL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  160 YSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEA 239
Cdd:PRK10365 152 LSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  240 ADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPA 319
Cdd:PRK10365 232 ADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPS 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  320 LRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHadllgidielddl 399
Cdd:PRK10365 312 LRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYIS------------- 378
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599920  400 eddfAADLGLGPAGAAASNHEPTEDLSLEDYFQHFVLEHQDHM--TETELARKLGISRKCLWERRQR 464
Cdd:PRK10365 379 ----ERELPLAIASTPIPLGQSQDIQPLVEVEKEVILAALEKTggNKTEAARQLGITRKTLLAKLSR 441
Sigma54_activat pfam00158
Sigma-54 interaction domain;
149-315 3.84e-112

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 327.82  E-value: 3.84e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   149 IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTG 228
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   229 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYY 308
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 15599920   309 RLHVISL 315
Cdd:pfam00158 161 RLNVIPI 167
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
149-390 3.14e-107

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 329.93  E-value: 3.14e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  149 IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRaKAPLISVNCAAIPETLIESELFGHEKGAFTG 228
Cdd:NF041552 269 IIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGR-KGPFVPVNCSAIPEELFESEFFGYEEGAFTG 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  229 AS-AGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLY 307
Cdd:NF041552 348 ALkKGKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFREDLY 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  308 YRLHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHA 387
Cdd:NF041552 428 YRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNGTITK 507

                 ...
gi 15599920  388 DLL 390
Cdd:NF041552 508 DSI 510
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
1-478 1.65e-104

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 321.44  E-value: 1.65e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    1 MAHILIVEDETIIRSALRRLLERNQYQVSE--AGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG-IPVLIMTS 77
Cdd:NF038308  27 RPTVALCQQPDLPVDRLELLHDRRDRALAErvAADIEEVSPETEVRLVPVVLRDPWDFEEVYGALLDFARAyPFDTENED 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   78 Y------------ASLRSAVDSMKMGAvDYIAKPFDHDEMLQAVARI-----LKDRQENRSAApvsanggkaggERGASP 140
Cdd:NF038308 107 YlvhittgthvaqICWFLLVEARYLPA-RLLQTSPPRDKEEGTYEIIdldlsRYDALAQRFAR-----------EQAEAV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  141 AVADGeiGIIGSCAPMQELYSKIRKVAPTD-STVLIQGESGTGKELVARALHNLSKRA---KAPLISVNCAAIPETLIES 216
Cdd:NF038308 175 SFLKS--GIATRNAAFNRLIEQIERVALRSrAPILLTGPTGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMS 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  217 ELFGHEKGAFTGASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTL 296
Cdd:NF038308 253 ELFGHVKGAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQE 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  297 AKTGQFREDLYYRLHVISLKLPALRERGNDVMEIARAFLARQCTRMGR----------APLSFAHDAEqairhYPWPGNV 366
Cdd:NF038308 333 VAEGRFREDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRqvrfnkearfRYLAFATSPE-----ALWPGNF 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  367 RELENAIERAVILSESQEIHADLLGidielddleddfAADLGLGPAGAAASnhEPTEDLSLEDYFQHFVLEHQDHMTETE 446
Cdd:NF038308 408 RELSASVTRMATLADGGRITEELVE------------EEIARLRAAWQSAP--AAADDDALADLLGGEQLAELDLFDRVQ 473
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15599920  447 LARKLGISRKCLWER---RQRLGIPRRKSGASADS 478
Cdd:NF038308 474 LAAVLRVCRQSRSLSaagRRLFGVSRQQKASPNDA 508
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
156-313 2.09e-27

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 107.23  E-value: 2.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 156 MQELYSKIRKVA--PTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEkgaftgASAGR 233
Cdd:cd00009   3 QEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 234 AGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVgsvqsQKVDVRLIAATHRDLKtlaktGQFREDLYYRLHVI 313
Cdd:cd00009  77 FELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRI-----DRENVRVIGATNRPLL-----GDLDRALYDRLDIR 146
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
172-292 3.34e-12

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 63.93  E-value: 3.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    172 TVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIES---ELFGHEKGAFTGASAGRAG--LVEAADGGTLF 246
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 15599920    247 LDEIGELPLEAQARLLRVLQEgeiRRVGSVQSQKVDVRLIAATHRD 292
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTNDE 126
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-466 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: 517.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMT 76
Cdd:COG2204   2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRelraLDPDLPVILLT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSanggkaggergaspavadgeiGIIGSCAPM 156
Cdd:COG2204  82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS---------------------GLIGRSPAM 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 157 QELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 236
Cdd:COG2204 141 QEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 237 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLK 316
Cdd:COG2204 221 FELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 317 LPALRERGNDVMEIARAFLARQCTRMGRaPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLLgidiel 396
Cdd:COG2204 301 LPPLRERREDIPLLARHFLARFAAELGK-PVKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDL------ 373
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599920 397 ddleddfaadlglgpagaaasnhepteDLSLEDYFQHFVLE----HQDHMTETelARKLGISRKCLWERRQRLG 466
Cdd:COG2204 374 ---------------------------PEALEEVERELIERaleeTGGNVSRA--AELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
148-467 1.06e-156

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: 452.30  E-value: 1.06e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 148 GIIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFT 227
Cdd:COG3829 139 DIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAFT 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 228 GASA-GRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDL 306
Cdd:COG3829 219 GAKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFREDL 298
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 307 YYRLHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIH 386
Cdd:COG3829 299 YYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSEGDVIT 378
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 387 ADLLGIDIELDDLEDDFAADLGLGPAGAAAsnheptEDLSLEDYFQHFvlehqdHMTETELARKLGISRKCLWERRQRLG 466
Cdd:COG3829 379 PEHLPEYLLEEAEAASAAEEGSLKEALEEV------EKELIEEALEKT------GGNKSKAAKALGISRSTLYRKLKKYG 446

                .
gi 15599920 467 I 467
Cdd:COG3829 447 I 447
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-439 1.82e-128

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: 380.62  E-value: 1.82e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920     4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLIMTSYA 79
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLpqikKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAapvsanggkaggerGASPAVADGEIGIIGSCAPMQEL 159
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVAL--------------PADAGEAEDSAELIGEAPAMQEV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   160 YSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEA 239
Cdd:TIGR01818 147 FRAIGRLSRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   240 ADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPA 319
Cdd:TIGR01818 227 ADGGTLFLDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPP 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   320 LRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLLgidielddl 399
Cdd:TIGR01818 307 LRERREDIPRLARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDL--------- 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 15599920   400 eddfAADLGLGPAGAAASNHEPTEDLS--LEDYFQHFVLEHQ 439
Cdd:TIGR01818 378 ----PAELALTGRPASAPDSDGQDSWDeaLEAWAKQALSRGE 415
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-464 1.15e-122

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 365.12  E-value: 1.15e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSYA 79
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKeikaLNPAIPVLIMTAYS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRsaapvsanggkaggerGASPAVADGEIGIIGSCAPMQEL 159
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSID----------------AETPAVTASQFGMVGKSPAMQHL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  160 YSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEA 239
Cdd:PRK10365 152 LSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  240 ADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPA 319
Cdd:PRK10365 232 ADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPS 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  320 LRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHadllgidielddl 399
Cdd:PRK10365 312 LRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYIS------------- 378
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599920  400 eddfAADLGLGPAGAAASNHEPTEDLSLEDYFQHFVLEHQDHM--TETELARKLGISRKCLWERRQR 464
Cdd:PRK10365 379 ----ERELPLAIASTPIPLGQSQDIQPLVEVEKEVILAALEKTggNKTEAARQLGITRKTLLAKLSR 441
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-467 2.32e-121

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 362.24  E-value: 2.32e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSYA 79
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKemrsHETRTPVILMTAYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK---DRQENRSAAPVSANGGKAGGERGASPAvadgeigiigscapM 156
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQlqsMKKEIRHLHQALSTSWQWGHILTNSPA--------------M 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  157 QELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGL 236
Cdd:PRK11361 153 MDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  237 VEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLK 316
Cdd:PRK11361 233 FERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLI 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  317 LPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLLgidiel 396
Cdd:PRK11361 313 LPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDL------ 386
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599920  397 ddleddfAADLGLGPAGAAASNHEPTEDLSLEDYFQHF-------VLEHQDHmTETELARKLGISRKCLWERRQRLGI 467
Cdd:PRK11361 387 -------PPQIRQPVCNAGEVKTAPVGERNLKEEIKRVekriimeVLEQQEG-NRTRTALMLGISRRALMYKLQEYGI 456
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
86-467 5.36e-120

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 360.64  E-value: 5.36e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   86 DSMKMGAVDYIAkpfdhDEMLQAVARIlkdrqenrSAAPVS-----------ANGGKAGGERGASPAVADGEIgiIGSCA 154
Cdd:PRK05022 130 DALDPGQFDAFS-----DEELRALAAL--------AAATLRnallieqlesqAELPQDVAEFLRQEALKEGEM--IGQSP 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  155 PMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRA 234
Cdd:PRK05022 195 AMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRS 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  235 GLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVIS 314
Cdd:PRK05022 275 GKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFP 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  315 LKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQ------EIHAD 388
Cdd:PRK05022 355 LSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVISRAALLARARgagrivTLEAQ 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  389 LLGIDIELDDLeddfaadlglGPAGAAASNHEPTEDLSLE-DYFQHFVLE-----HQDHMTETelARKLGISRKCLWERR 462
Cdd:PRK05022 435 HLDLPAEVALP----------PPEAAAAPAAVVSQNLREAtEAFQRQLIRqalaqHQGNWAAA--ARALELDRANLHRLA 502

                 ....*
gi 15599920  463 QRLGI 467
Cdd:PRK05022 503 KRLGL 507
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
4-467 3.15e-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: 354.05  E-value: 3.15e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920     4 ILIVEDETIIRSALRRLLErnQYQVSEAGSVQEA--QERYTIPSfdMVVSDLRLPGAPGT---------ELIKLAEGIPV 72
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAiaLVRRHEPA--VVTLDLGLPPDADGaseglaalqQILAIAPDTKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    73 LIMTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKD---RQENRSAApvSANGGKAGGergaspavadgeiGI 149
Cdd:TIGR02915  77 IVITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLytlETENRRLQ--SALGGTALR-------------GL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   150 IGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGA 229
Cdd:TIGR02915 142 ITSSPGMQKICRTIEKIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   230 SAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYR 309
Cdd:TIGR02915 222 VKQTLGKIEYAHGGTLFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   310 LHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADl 389
Cdd:TIGR02915 302 IAEISITIPPLRSRDGDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAE- 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   390 lgidielddleddfaaDLGLgPAGAAASNHEPTEDLSLEDYFQHFVLEHQDHMTETELARK---LGISRKCLWERRQRLG 466
Cdd:TIGR02915 381 ----------------DLGL-DARERAETPLEVNLREVRERAEREAVRKAIARVDGNIARAaelLGITRPTLYDLMKKHG 443

                  .
gi 15599920   467 I 467
Cdd:TIGR02915 444 I 444
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
103-466 8.65e-116

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 353.44  E-value: 8.65e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 103 DEMLQAVARILKDRQENRSAA--PVSANGGKAGGERG-------------ASPAVADGEIGIIGSCAPMQELYSKIRKVA 167
Cdd:COG3284 262 EELFGLDLEALPDGARRAPASprPLRLRDGRRLGALLrlrparraaraapAGAPAPAALAALAGGDPAMRRALRRARRLA 341
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 168 PTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASA-GRAGLVEAADGGTLF 246
Cdd:COG3284 342 DRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRkGRPGKIEQADGGTLF 421
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 247 LDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPALRERGnD 326
Cdd:COG3284 422 LDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRERE-D 500
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 327 VMEIARAFLARQCTRMGraPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLLGIDIELDDLEDDFAAD 406
Cdd:COG3284 501 LPALIEHLLRELAAGRG--PLRLSPEALALLAAYPWPGNVRELRNVLRTALALADGGVITVEDLPDELRAELAAAAPAAA 578
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 407 LGLGPAgaaasnhEPTEDLSLEDYFQhfvlEHQDHMTETelARKLGISRKCLWERRQRLG 466
Cdd:COG3284 579 APLTSL-------EEAERDAILRALR----ACGGNVSAA--ARALGISRSTLYRKLKRYG 625
Sigma54_activat pfam00158
Sigma-54 interaction domain;
149-315 3.84e-112

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 327.82  E-value: 3.84e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   149 IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTG 228
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   229 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYY 308
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 15599920   309 RLHVISL 315
Cdd:pfam00158 161 RLNVIPI 167
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
4-385 4.00e-111

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 336.46  E-value: 4.00e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG----IPVLIMTSYA 79
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQrhpmLPVIIMTAHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSANGgkaggergaspAVADgeigIIGSCAPMQEL 159
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNG-----------PTTD----IIGEAPAMQDV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  160 YSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEA 239
Cdd:PRK10923 151 FRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQ 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  240 ADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPA 319
Cdd:PRK10923 231 ADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPP 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599920  320 LRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEI 385
Cdd:PRK10923 311 LRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEV 376
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
149-390 3.14e-107

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 329.93  E-value: 3.14e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  149 IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRaKAPLISVNCAAIPETLIESELFGHEKGAFTG 228
Cdd:NF041552 269 IIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGR-KGPFVPVNCSAIPEELFESEFFGYEEGAFTG 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  229 AS-AGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLY 307
Cdd:NF041552 348 ALkKGKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEGKFREDLY 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  308 YRLHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHA 387
Cdd:NF041552 428 YRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVLSKNGTITK 507

                 ...
gi 15599920  388 DLL 390
Cdd:NF041552 508 DSI 510
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
103-388 3.51e-107

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: 328.60  E-value: 3.51e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   103 DEMLQAVARILKDRQENRSAAPVSANGGKAGGERGASPAvadgeigiigscapMQELYSKIRKVAPTDSTVLIQGESGTG 182
Cdd:TIGR01817 166 RERLIAEAVQLSKQLRDKAPEIARRRSGKEDGIIGKSPA--------------MRQVVDQARVVARSNSTVLLRGESGTG 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   183 KELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEAADGGTLFLDEIGELPLEAQARLL 262
Cdd:TIGR01817 232 KELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   263 RVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPALRERGNDVMEIARAFLARQCTRM 342
Cdd:TIGR01817 312 RVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNREN 391
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 15599920   343 GRaPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHAD 388
Cdd:TIGR01817 392 GR-PLTITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITRS 436
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
149-454 2.34e-105

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 323.29  E-value: 2.34e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 149 IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTG 228
Cdd:COG3283 206 IVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFGN 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 229 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYY 308
Cdd:COG3283 286 AREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLYY 365
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 309 RLHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHAD 388
Cdd:COG3283 366 RLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGDELTPE 445
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599920 389 llgidielddleddfaaDLGLGPAGAAASNHEPTEDLSLEDYFQHF---VLE--HQDHMTETELARKLGIS 454
Cdd:COG3283 446 -----------------DLQLPEYAASAGLLDDLLEGSLDEIVKRFersLLRrlYPSYPSTRKLAKRLGVS 499
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
1-478 1.65e-104

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 321.44  E-value: 1.65e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    1 MAHILIVEDETIIRSALRRLLERNQYQVSE--AGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG-IPVLIMTS 77
Cdd:NF038308  27 RPTVALCQQPDLPVDRLELLHDRRDRALAErvAADIEEVSPETEVRLVPVVLRDPWDFEEVYGALLDFARAyPFDTENED 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   78 Y------------ASLRSAVDSMKMGAvDYIAKPFDHDEMLQAVARI-----LKDRQENRSAApvsanggkaggERGASP 140
Cdd:NF038308 107 YlvhittgthvaqICWFLLVEARYLPA-RLLQTSPPRDKEEGTYEIIdldlsRYDALAQRFAR-----------EQAEAV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  141 AVADGeiGIIGSCAPMQELYSKIRKVAPTD-STVLIQGESGTGKELVARALHNLSKRA---KAPLISVNCAAIPETLIES 216
Cdd:NF038308 175 SFLKS--GIATRNAAFNRLIEQIERVALRSrAPILLTGPTGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMS 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  217 ELFGHEKGAFTGASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTL 296
Cdd:NF038308 253 ELFGHVKGAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQE 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  297 AKTGQFREDLYYRLHVISLKLPALRERGNDVMEIARAFLARQCTRMGR----------APLSFAHDAEqairhYPWPGNV 366
Cdd:NF038308 333 VAEGRFREDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRqvrfnkearfRYLAFATSPE-----ALWPGNF 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  367 RELENAIERAVILSESQEIHADLLGidielddleddfAADLGLGPAGAAASnhEPTEDLSLEDYFQHFVLEHQDHMTETE 446
Cdd:NF038308 408 RELSASVTRMATLADGGRITEELVE------------EEIARLRAAWQSAP--AAADDDALADLLGGEQLAELDLFDRVQ 473
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15599920  447 LARKLGISRKCLWER---RQRLGIPRRKSGASADS 478
Cdd:NF038308 474 LAAVLRVCRQSRSLSaagRRLFGVSRQQKASPNDA 508
PRK15115 PRK15115
response regulator GlrR; Provisional
2-385 1.33e-100

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 308.69  E-value: 1.33e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPG----TELIKLAEGIPVLIMTS 77
Cdd:PRK15115   6 AHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGmqlfAEIQKVQPGMPVIILTA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRqenrsaAPVSANGGKAGgergaspavadgeigIIGSCAPMQ 157
Cdd:PRK15115  86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQS------APATDERWREA---------------IVTRSPLML 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  158 ELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLV 237
Cdd:PRK15115 145 RLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLF 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  238 EAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKL 317
Cdd:PRK15115 225 QAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKI 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599920  318 PALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEI 385
Cdd:PRK15115 305 PALAERTEDIPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVI 372
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
149-377 2.14e-90

psp operon transcriptional activator PspF; Members of this protein family are PspF, the sigma-54-dependent transcriptional activator of the phage shock protein (psp) operon, in Escherichia coli and numerous other species. The psp operon is induced by a number of stress conditions, including heat shock, ethanol, and filamentous phage infection. Changed com_name to adhere to TIGR role notes conventions. 09/15/06 - DMH [Regulatory functions, DNA interactions]


Pssm-ID: 274371 [Multi-domain]  Cd Length: 329  Bit Score: 278.41  E-value: 2.14e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   149 IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTG 228
Cdd:TIGR02974   1 LIGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   229 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYY 308
Cdd:TIGR02974  81 AQKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLD 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   309 RLHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLS-FAHDAEQAIRHYPWPGNVRELENAIERAV 377
Cdd:TIGR02974 161 RLAFDVITLPPLRERQEDIMLLAEHFAIRMARELGLPLFPgFTPQAREQLLEYHWPGNVRELKNVVERSV 230
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
149-464 2.07e-88

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 280.07  E-value: 2.07e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  149 IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALH--------NLSKRAKAPLISVNCAAIPETLIESELFG 220
Cdd:PRK15424 221 LLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHreyfarhdARQGKKSHPFVAVNCGAIAESLLEAELFG 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  221 HEKGAFTGAS-AGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKT 299
Cdd:PRK15424 301 YEEGAFTGSRrGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQ 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  300 GQFREDLYYRLHVISLKLPALRERGNDVMEIARAFLaRQCTRMGRAPLSFAHDAE-----QAIRHYPWPGNVRELENAIE 374
Cdd:PRK15424 381 GRFRRDLFYRLSILRLQLPPLRERVADILPLAESFL-KQSLAALSAPFSAALRQGlqqceTLLLHYDWPGNVRELRNLME 459
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  375 RAVILSESQEIHAdllgidiELDDLEDDFAADLGLGPAGAAASnhePTEDLSLEDYFQHFvleHQDHmteTELARKLGIS 454
Cdd:PRK15424 460 RLALFLSVEPTPD-------LTPQFLQLLLPELARESAKTPAP---RLLAATLQQALERF---NGDK---TAAANYLGIS 523
                        330
                 ....*....|
gi 15599920  455 RKCLWERRQR 464
Cdd:PRK15424 524 RTTLWRRLKA 533
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
121-463 7.78e-88

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: 278.28  E-value: 7.78e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   121 SAAPVSANGGKAGGERGASPAvadgeiGIIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAP 200
Cdd:TIGR02329 192 RQAATLRSATRNQLRTRYRLD------DLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFP 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   201 LISVNCAAIPETLIESELFGHEKGAFTGA-SAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQ 279
Cdd:TIGR02329 266 FVAINCGAIAESLLEAELFGYEEGAFTGArRGGRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPV 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   280 KVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPALRERGNDVMEIARAFLaRQCTRMGRAPLSFA-----HDAE 354
Cdd:TIGR02329 346 PVDVRVVAATHCALTTAVQQGRFRRDLFYRLSILRIALPPLRERPGDILPLAAEYL-VQAAAALRLPDSEAaaqvlAGVA 424
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   355 QAIRHYPWPGNVRELENAIERAVILSESQEIHAdlLGIDIELDDLEDDFAADLGLGPAGAAASNHEPTEDLSLEDYFQHF 434
Cdd:TIGR02329 425 DPLQRYPWPGNVRELRNLVERLALELSAMPAGA--LTPDVLRALAPELAEASGKGKTSALSLRERSRVEALAVRAALERF 502
                         330       340
                  ....*....|....*....|....*....
gi 15599920   435 VLEHqdhmteTELARKLGISRKCLWERRQ 463
Cdd:TIGR02329 503 GGDR------DAAAKALGISRTTLWRRLK 525
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
144-470 2.53e-86

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 278.64  E-value: 2.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  144 DGEIG-IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHE 222
Cdd:PRK15429 372 DSEFGeIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHE 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  223 KGAFTGASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQF 302
Cdd:PRK15429 452 RGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREF 531
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  303 REDLYYRLHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSES 382
Cdd:PRK15429 532 RSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRG 611
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  383 QEIHADLlgidielddleddfaADLGLG-PAGAAASNHEPTEDlslEDYFQHFVLEhqdhMTETE--------LARKLGI 453
Cdd:PRK15429 612 NVLQLSL---------------PDITLPePETPPAATVVAQEG---EDEYQLIVRV----LKETNgvvagpkgAAQRLGL 669
                        330
                 ....*....|....*..
gi 15599920  454 SRKCLWERRQRLGIPRR 470
Cdd:PRK15429 670 KRTTLLSRMKRLGIDKS 686
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
158-377 1.52e-78

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 247.66  E-value: 1.52e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  158 ELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLV 237
Cdd:PRK11608  17 EVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  238 EAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKL 317
Cdd:PRK11608  97 ERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQL 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599920  318 PALRERGNDVMEIARAFLARQCTRMGRaPL--SFAHDAEQAIRHYPWPGNVRELENAIERAV 377
Cdd:PRK11608 177 PPLRERQSDIMLMAEHFAIQMCRELGL-PLfpGFTERARETLLNYRWPGNIRELKNVVERSV 237
PRK10820 PRK10820
transcriptional regulator TyrR;
149-475 4.00e-78

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 252.69  E-value: 4.00e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  149 IIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTG 228
Cdd:PRK10820 206 IVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPN 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  229 ASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYY 308
Cdd:PRK10820 286 ALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYY 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  309 RLHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHad 388
Cdd:PRK10820 366 RLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLEGYELR-- 443
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  389 llgidielddleddfAADLGLGPAGAAASNHEPTEDLSLEDY---FQHFVLE--HQDHMTETELARKLGISRKCLWERRQ 463
Cdd:PRK10820 444 ---------------PQDILLPDYDAAVAVGEDAMEGSLDEItsrFERSVLTrlYRNYPSTRKLAKRLGVSHTAIANKLR 508
                        330
                 ....*....|..
gi 15599920  464 RLGIPRRKSGAS 475
Cdd:PRK10820 509 EYGLSQKKGEED 520
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
175-390 6.86e-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: 6.86e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 175 IQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESelfghekgaftgasagraglveaadggtlfldeigelp 254
Cdd:COG3604 120 ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------------- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 255 leaqarllrvLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPALRERGNDVMEIARAF 334
Cdd:COG3604 162 ----------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHF 231
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599920 335 LARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLL 390
Cdd:COG3604 232 LEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDL 287
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
156-467 6.76e-50

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 180.26  E-value: 6.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  156 MQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGhekGAFTGASAGRAG 235
Cdd:PRK11388 334 MRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SDRTDSENGRLS 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  236 LVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISL 315
Cdd:PRK11388 411 KFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAFEI 490
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  316 KLPALRERGND----VMEIARAFLARQCTRMGRAPlsfahDAEQAIRHYPWPGNVRELENAIERAVILSESQEIH----- 386
Cdd:PRK11388 491 TIPPLRMRREDipalVNNKLRSLEKRFSTRLKIDD-----DALARLVSYRWPGNDFELRSVIENLALSSDNGRIRlsdlp 565
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920  387 ADLLGIDielddleddfaadlglgPAGAAASNHEPTeDLSLEDyFQHFVLEHQDHMTE---TELARKLGISRKCLWERRQ 463
Cdd:PRK11388 566 EHLFTEQ-----------------ATDDVSATRLST-SLSLAE-LEKEAIINAAQVCGgriQEMAALLGIGRTTLWRKMK 626

                 ....
gi 15599920  464 RLGI 467
Cdd:PRK11388 627 QHGI 630
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
163-389 2.54e-47

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: 171.17  E-value: 2.54e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 163 IRKVAPtdstVLIQGESGTGKELVARALHNLSK---RAKAPLISVNCAaipeTL----IESELFGHEKGAFTGASAGRAG 235
Cdd:COG4650 205 IRSRAP----ILLTGPTGAGKSQLARRIYELKKarhQVSGRFVEVNCA----TLrgdgAMSALFGHVKGAFTGAVSDRAG 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 236 LVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISL 315
Cdd:COG4650 277 LLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTF 356
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 316 KLPALRERGNDV-----MEIARaFLARQCTRMG------RAPLSFAHDAEQairhyPWPGNVRELENAIERAVILSESQE 384
Cdd:COG4650 357 RLPGLAERREDIepnldYELAR-FAREQGRRVRfnkearARYLAFATSPEA-----LWSGNFRDLNASVTRMATLAEGGR 430

                ....*
gi 15599920 385 IHADL 389
Cdd:COG4650 431 ITVAL 435
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
173-373 2.62e-41

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: 157.58  E-value: 2.62e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 173 VLIQGESGTGKELVARALHNLSKRAK-----APLISVNCAAI---PETLIeSELFGHEKGAFTGASAGRAGLVEAADGGT 244
Cdd:COG1221 133 TLILGPTGVGKSFFAELMYEYAIEIGvlpedAPFVVFNCADYannPQLLM-SQLFGYVKGAFTGADKDKEGLIEKADGGI 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 245 LFLDEIGELPLEAQARLLRVLQEGEIRRVG-SVQSQKVDVRLIAATHRDL-KTLAKTgqF-RedlyyRLHVIsLKLPALR 321
Cdd:COG1221 212 LFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPeSSLLKT--FlR-----RIPMV-IKLPSLE 283
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15599920 322 ERG-NDVMEIARAFLARQCTRMGRaPLSFAHDAEQAIRHYPWPGNVRELENAI 373
Cdd:COG1221 284 ERSlEERLELIKHFFKEEAKRLNK-PIKVSKEVLKALLLYDCPGNIGQLKSDI 335
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
156-313 2.09e-27

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 107.23  E-value: 2.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 156 MQELYSKIRKVA--PTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEkgaftgASAGR 233
Cdd:cd00009   3 QEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920 234 AGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVgsvqsQKVDVRLIAATHRDLKtlaktGQFREDLYYRLHVI 313
Cdd:cd00009  77 FELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRI-----DRENVRVIGATNRPLL-----GDLDRALYDRLDIR 146
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1-130 2.25e-27

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 108.50  E-value: 2.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMT 76
Cdd:COG0745   1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRrlraRPSDIPIIMLT 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKdrqenRSAAPVSANGG 130
Cdd:COG0745  81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR-----RRAAEVLRVGD 129
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
5-99 3.19e-27

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 104.62  E-value: 3.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLIMTSYAS 80
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLrklrELPPDIPVIVLTAKAD 80
                        90
                ....*....|....*....
gi 15599920  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd00156  81 EEDAVRALELGADDYLVKP 99
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-118 8.05e-27

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: 104.55  E-value: 8.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLA------EGIPVLI 74
Cdd:COG0784   5 GKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIralprlPDIPIIA 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15599920  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQE 118
Cdd:COG0784  85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
150-320 1.27e-24

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 98.95  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   150 IGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESelfghekgaftga 229
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   230 sagraglveaADGGTLFLDEIGELPLEAQARLLRVLQEGEirrvgsvqsqKVDVRLIAATHRDLKTLAKTGQFREDLYYR 309
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 15599920   310 LHVISLKLPAL 320
Cdd:pfam14532 128 LSALRLHVPPL 138
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1-149 4.07e-24

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: 100.24  E-value: 4.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL------AEGIPVLI 74
Cdd:COG3437   6 APTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLlradpsTRDIPVIF 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599920  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRsaapvsANGGKAGGERGASPAVADGEIGI 149
Cdd:COG3437  86 LTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQR------ELDDLVLYLKLAAPLHDIGKIGI 154
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1-109 4.86e-24

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 98.44  E-value: 4.86e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL------AEGIPVLI 74
Cdd:COG3706   1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRlradprTADIPIIF 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:COG3706  81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
3-124 7.69e-24

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: 98.06  E-value: 7.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLA----EGIPVLIMTSY 78
Cdd:COG4567   6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALrerdPDARIVVLTGY 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAP 124
Cdd:COG4567  86 ASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENPM 131
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
3-108 8.33e-24

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 95.59  E-value: 8.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSY 78
Cdd:cd17563   2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPplraLQPDARIVVLTGY 81
                        90       100       110
                ....*....|....*....|....*....|
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQA 108
Cdd:cd17563  82 ASIATAVEAIKLGADDYLAKPADADEILAA 111
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
4-110 1.55e-23

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: 94.91  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920     4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSYA 79
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKrirrRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 15599920    80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVA 110
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
4-121 3.54e-23

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: 94.48  E-value: 3.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTiPSF-DMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSY 78
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALS-PDFpGVVISDIRMPGMDGLELLAqireLDPDLPVILITGH 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQ---ENRS 121
Cdd:cd17549  80 GDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRlvlENRR 125
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
3-123 2.50e-22

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 94.40  E-value: 2.50e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK-LAE---GIPVLIMTSY 78
Cdd:COG4566   1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEeLAArgsPLPVIFLTGH 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAA 123
Cdd:COG4566  81 GDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAER 125
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1-114 8.46e-21

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: 87.54  E-value: 8.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMT 76
Cdd:COG5803   2 MKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKeikeIDPDIPVIMMT 81
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:COG5803  82 AYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-121 4.20e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 86.18  E-value: 4.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLI 74
Cdd:COG4565   3 MIRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLrelrARGPDVDVIV 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15599920  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRS 121
Cdd:COG4565  83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
4-99 1.17e-19

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: 83.67  E-value: 1.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTS 77
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEaireLDPDTKIIILSG 81
                        90       100
                ....*....|....*....|..
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKP 99
Cdd:COG4753  82 YSDFEYAQEAIKLGADDYLLKP 103
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
4-111 7.23e-19

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: 81.94  E-value: 7.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI-KLAE---GIPVLIMTSYA 79
Cdd:cd19919   3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLaQIKQrhpDLPVIIMTAHS 82
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVAR 111
Cdd:cd19919  83 DLDSAVSAYQGGAFEYLPKPFDIDEAVALVER 114
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
4-114 1.71e-18

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: 81.00  E-value: 1.71e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAE----GIPVLIMTSYA 79
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKekypDLPVIMISGHG 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:cd17550  81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
4-114 1.77e-18

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: 81.23  E-value: 1.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQY---QVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMT 76
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIDWEELgfeVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEkireLYPDIKIIILS 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15599920  77 SYAS---LRSAvdsMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:cd17536  81 GYDDfeyAQKA---IRLGVVDYLLKPVDEEELEEALEKAKE 118
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
2-112 2.05e-18

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: 80.76  E-value: 2.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK------LAEGIPVLIM 75
Cdd:cd17618   1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRrlkrdeMTRDIPIIML 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599920  76 TSYASLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17618  81 TARGEEEDKVRGLEAGADDYITKPFSPREL---VARI 114
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
4-109 2.47e-18

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 80.53  E-value: 2.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTE-LIKLAEGIPV---LIMTSYA 79
Cdd:cd17569   3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAElLKRVRERYPDtvrILLTGYA 82
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599920  80 SLRSAVDSMKMGAVD-YIAKPFDHDEMLQAV 109
Cdd:cd17569  83 DLDAAIEAINEGEIYrFLTKPWDDEELKETI 113
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
5-99 2.92e-18

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: 79.76  E-value: 2.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSYAS 80
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRrlreKGSDIPIIMLTAKDE 80
                        90
                ....*....|....*....
gi 15599920  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd17574  81 EEDKVLGLELGADDYITKP 99
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
2-109 7.93e-18

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 79.17  E-value: 7.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI-KLAE---GIPVLIMTS 77
Cdd:cd17537   1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQdELLArgsNIPIIFITG 80
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17537  81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAI 112
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
4-117 1.27e-17

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: 78.78  E-value: 1.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG----IPVLIMTSYA 79
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQErslpTSVIVITAHG 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQ 117
Cdd:cd17572  81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRK 118
fixJ PRK09390
response regulator FixJ; Provisional
2-127 1.38e-17

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 80.82  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTS 77
Cdd:PRK09390   4 GVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRrlkaRGSPLPVIVMTG 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15599920   78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSA 127
Cdd:PRK09390  84 HGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEAAKSEAVAA 133
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1-124 6.19e-17

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 79.86  E-value: 6.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLER-NQYQ-VSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLI 74
Cdd:COG3279   1 MMKILIVDDEPLARERLERLLEKyPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARqlreLDPPPPIIF 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15599920  75 MTSYASLrsAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAP 124
Cdd:COG3279  81 TTAYDEY--ALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEA 128
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
4-113 1.80e-16

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: 75.24  E-value: 1.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTS 77
Cdd:cd17535   1 VLIVDDHPLVREGLRRLLESEPdiEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRrlrrRYPDLKVIVLTA 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17535  81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
2-113 2.11e-16

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: 75.03  E-value: 2.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAE--GIPVLIM 75
Cdd:cd17562   1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKelrkLPAykFTPILML 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15599920  76 TSYASlrsavDSMKM-----GAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17562  81 TTESS-----DEKKQegkaaGATGWLVKPFDPEQLLEVVKKVL 118
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
2-111 1.03e-15

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: 73.00  E-value: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTS 77
Cdd:cd17555   1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKqitkESPDTPVIVVSG 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEML-QAVAR 111
Cdd:cd17555  81 AGVMSDAVEALRLGAWDYLTKPIEDLAVLeHAVRR 115
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
4-116 2.42e-15

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 71.93  E-value: 2.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK--LAEG--IPVLIMTSYA 79
Cdd:cd19934   1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRrwRSEGraTPVLILTARD 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFdHDEMLQAVARILKDR 116
Cdd:cd19934  81 SWQDKVEGLDAGADDYLTKPF-HIEELLARLRALIRR 116
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
4-111 2.96e-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: 2.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL--AEG--IPVLIMTSYA 79
Cdd:cd17624   1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRwrRQGqsLPVLILTARD 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEM---LQAVAR 111
Cdd:cd17624  81 GVDDRVAGLDAGADDYLVKPFALEELlarLRALLR 115
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
4-100 4.15e-15

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 71.00  E-value: 4.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTE---LIK---LAEGIPVLIMTS 77
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEvcrRLKadpATRHIPVIFLTA 80
                        90       100
                ....*....|....*....|...
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPF 100
Cdd:cd19920  81 LTDTEDKVKGFELGAVDYITKPF 103
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
4-113 6.70e-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: 71.05  E-value: 6.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSYA 79
Cdd:cd17553   3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKrmkvIDENIRVIIMTAYG 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17553  83 ELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
4-113 9.21e-15

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: 70.39  E-value: 9.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQ-VSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSY 78
Cdd:cd17542   3 VLIVDDAAFMRMMLKDILTKAGYEvVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKeikkIDPNAKVIMCSAM 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17542  83 GQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
5-112 1.00e-14

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 70.33  E-value: 1.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL--AEGI--PVLIMTSYAS 80
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSlrEEGIetPVLLLTALDA 80
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599920  81 LRSAVDSMKMGAVDYIAKPFDHDEMLqavARI 112
Cdd:cd17625  81 VEDRVKGLDLGADDYLPKPFSLAELL---ARI 109
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
2-129 3.13e-14

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


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 71.98  E-value: 3.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920     2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK------LAEGIPVLIM 75
Cdd:TIGR02154   3 RRILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRrlrrrpETRAIPIIML 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15599920    76 TSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSANG 129
Cdd:TIGR02154  83 TARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLRRIRPQLSDEVIEVGD 136
PRK10643 PRK10643
two-component system response regulator PmrA;
4-121 3.74e-14

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 71.61  E-value: 3.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLIMTSYA 79
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLrrwrQKKYTLPVLILTARD 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEmLQAVARILKDRQENRS 121
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPFALEE-LHARIRALIRRHQGQG 123
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
4-109 7.70e-14

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: 67.49  E-value: 7.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPG---TELIKLAEG----IPVLIMT 76
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGleaTRRIRELEGggrrTPIIALT 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17546  81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
4-99 1.17e-13

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: 66.79  E-value: 1.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAE----GIPVLIMTSYA 79
Cdd:cd19926   1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQqrlpQTPVAVITAYG 80
                        90       100
                ....*....|....*....|
gi 15599920  80 SLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19926  81 SLDTAIEALKAGAFDFLTKP 100
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
2-112 1.36e-13

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: 66.86  E-value: 1.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLIMTS 77
Cdd:cd17554   1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLrkirEKKPDLPVIICTA 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  78 YASLRSavDSMKMGAVDYIAKPFDHDEMLQAVARI 112
Cdd:cd17554  81 YSEYKS--DFSSWAADAYVVKSSDLTELKETIKRL 113
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
5-114 2.71e-13

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 66.14  E-value: 2.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   5 LIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL------AEGIPVLIMTSY 78
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRIlrsdpkTSSIPIIMLTAK 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:cd19937  81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVLR 116
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
4-113 5.42e-13

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 65.42  E-value: 5.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEG---IPVLIMTS 77
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELcrkIKSDPDlkdIPVILLTT 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17598  81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
4-99 5.94e-13

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: 64.49  E-value: 5.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG---IPVLIMTSYAS 80
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREwsaVPVIVLSARDE 80
                        90
                ....*....|....*....
gi 15599920  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd17620  81 ESDKIAALDAGADDYLTKP 99
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
2-106 6.13e-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: 65.10  E-value: 6.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSY 78
Cdd:cd17619   1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLtreLREQSEVGIILVTGR 80
                        90       100
                ....*....|....*....|....*...
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEML 106
Cdd:cd17619  81 DDEVDRIVGLEIGADDYVTKPFNPRELL 108
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
2-112 6.66e-13

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: 65.16  E-value: 6.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   2 AHILIVEDETIIRSALRRLLERNQY-QVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLA------EGIPVLI 74
Cdd:cd17551   1 MRILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLralpglEDVPIVM 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599920  75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLqavARI 112
Cdd:cd17551  81 ITADTDREVRLRALEAGATDFLTKPFDPVELL---ARV 115
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
4-105 1.10e-12

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: 64.57  E-value: 1.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQE--RYTIPSFDMVVSDLRLPGAPG---TELIKLAEGIPVLIMTSY 78
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSmlRENKDEFDLVITDVHMPDMDGfefLELIRLEMDLPVIMMSAD 80
                        90       100
                ....*....|....*....|....*..
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEM 105
Cdd:cd17584  81 GSTSTVMKGLAHGACDYLLKPVSIEDL 107
orf27 CHL00148
Ycf27; Reviewed
3-130 1.11e-12

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 67.43  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSYA 79
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVcqeIRKESDVPIIMLTALG 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEmLQAVARILKDRQENRSAAPVSANGG 130
Cdd:CHL00148  88 DVSDRITGLELGADDYVVKPFSPKE-LEARIRSVLRRTNKKSFSSKIPNSS 137
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-104 1.25e-12

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 64.46  E-value: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEA----QERytiPSFDMVVSDLRLPGAPGTELIKlaegipvLIMTSY 78
Cdd:cd17544   2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEAlevlEQH---PDIKLVITDYNMPEMDGFELVR-------EIRKKY 71
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599920  79 ASLR------SAVDS-------MKMGAVDYIAKPFDHDE 104
Cdd:cd17544  72 SRDQlaiigiSASGDnalsarfIKAGANDFLTKPFLPEE 110
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
4-113 1.31e-12

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: 64.28  E-value: 1.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQ-VSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL--AEG----IPVLIMT 76
Cdd:cd19923   3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTirADGalshLPVLMVT 82
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd19923  83 AEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
3-109 2.14e-12

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 63.62  E-value: 2.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG---IPVLIMTSYA 79
Cdd:cd17594   1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRArsdVPIIIISGDR 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599920  80 SLRSAVD-SMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17594  81 RDEIDRVvGLELGADDYLAKPFGLRELLARV 111
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
4-114 2.37e-12

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 66.28  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK------LAEGIPVLIMTS 77
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKhlkresMTRDIPVVMLTA 84
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15599920   78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
4-111 3.19e-12

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: 62.94  E-value: 3.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG------IPVLIMTS 77
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEdpatrdIPVIALTA 81
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVAR 111
Cdd:cd17548  82 YAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
172-292 3.34e-12

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 63.93  E-value: 3.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    172 TVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIES---ELFGHEKGAFTGASAGRAG--LVEAADGGTLF 246
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 15599920    247 LDEIGELPLEAQARLLRVLQEgeiRRVGSVQSQKVDVRLIAATHRD 292
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTNDE 126
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
4-113 6.80e-12

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 62.30  E-value: 6.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPG---TELIKLAEGIPVLIMTSYAS 80
Cdd:cd18159   1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGfywCREIRQISNVPIIFISSRDD 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599920  81 LRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd18159  81 NMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
4-109 6.89e-12

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: 62.09  E-value: 6.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL------AEGIPVLIMTS 77
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRlrelpwLANTPAIALTG 80
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17580  81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
4-99 1.16e-11

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 61.06  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSYAS 80
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVcrqLRARSNVPVIMVTAKDS 80
                        90
                ....*....|....*....
gi 15599920  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd17621  81 EIDKVVGLELGADDYVTKP 99
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
4-112 1.56e-11

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: 61.24  E-value: 1.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG----IPVLIMTSYA 79
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAagndLPILVLTARD 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLqavARI 112
Cdd:cd17627  81 SVSDRVAGLDAGADDYLVKPFALEELL---ARV 110
ompR PRK09468
osmolarity response regulator; Provisional
3-112 1.79e-11

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 63.84  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG----IPVLIMTSY 78
Cdd:PRK09468   7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSqnnpTPIIMLTAK 86
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15599920   79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLqavARI 112
Cdd:PRK09468  87 GEEVDRIVGLEIGADDYLPKPFNPRELL---ARI 117
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
4-109 1.81e-11

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: 60.88  E-value: 1.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSE-AGSVQEAQERYTIPSFDMVVSDLRLPGAP-GTEL---IKLAEGIPVLIMTSY 78
Cdd:cd17534   3 ILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKGDMdGIEAareIREKFDIPVIFLTAY 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599920  79 AS---LRSAvdsMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17534  83 SDeetLERA---KETNPYGYLVKPFNERELKAAI 113
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
4-117 1.83e-11

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 61.01  E-value: 1.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLER-NQYQ-VSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLIMTS 77
Cdd:cd17532   1 ALIVDDEPLAREELRYLLEEhPDIEiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAkklsKLAKPPLIVFVTA 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15599920  78 YASLrsAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQ 117
Cdd:cd17532  81 YDEY--AVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
PRK10766 PRK10766
two-component system response regulator TorR;
3-113 5.63e-11

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 62.36  E-value: 5.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSYA 79
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLtreLRSRSTVGIILVTGRT 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:PRK10766  84 DSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
3-114 7.57e-11

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: 59.31  E-value: 7.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSYA 79
Cdd:cd19939   1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVcreVREHSHVPILMLTART 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:cd19939  81 EEMDRVLGLEMGADDYLCKPFSPRELLARVRALLR 115
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
3-100 7.57e-11

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: 58.66  E-value: 7.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEG---IPVLIMT 76
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVcrrLKEDPEtrhIPVIMIT 80
                        90       100
                ....*....|....*....|....
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPF 100
Cdd:cd17538  81 ALDDREDRIRGLEAGADDFLSKPI 104
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-122 1.13e-10

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: 60.74  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQYQV-SEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG---IPVLIMT 76
Cdd:COG3707   3 GLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEerpAPVILLT 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15599920  77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSA 122
Cdd:COG3707  83 AYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRAL 128
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
4-109 1.20e-10

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 58.58  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQV-SEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTE---LIKLAEGIPVLIMTSYA 79
Cdd:cd19932   3 VLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEaakIITSENIAPIVLLTAYS 82
                        90       100       110
                ....*....|....*....|....*....|
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd19932  83 QQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
4-99 1.42e-10

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: 57.84  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL--AEGI--PVLIMTSYA 79
Cdd:cd19935   1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRlrAAGKqtPVLMLTARD 80
                        90       100
                ....*....|....*....|
gi 15599920  80 SLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19935  81 SVEDRVKGLDLGADDYLVKP 100
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
4-99 1.48e-10

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: 58.16  E-value: 1.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI-KLAEG-----IPVLIMTS 77
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLgKLRKNadfdtIPVIFLTA 80
                        90       100
                ....*....|....*....|..
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19927  81 KGMTSDRIKGYNAGCDGYLSKP 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
3-56 1.53e-10

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: 56.42  E-value: 1.53e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15599920      3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLP 56
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1-125 1.71e-10

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 60.97  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQ----EAQERYTipsfDMVVSDLRLPGAPGTELI---KLAEGIPVL 73
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQrgllEAATRKP----DLIILDLGLPDGDGIEFIrdlRQWSAIPVI 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15599920   74 IMTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPV 125
Cdd:PRK10529  77 VLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATPAPDPL 128
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
4-112 1.83e-10

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 57.83  E-value: 1.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG----IPVLIMTSYA 79
Cdd:cd17573   1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEkhpsIVVIVLSDNP 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17573  81 KTEQEIEAFKEGADDYIAKPFDFKVL---VARI 110
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-130 3.72e-10

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 59.98  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMT 76
Cdd:PRK11083   3 QPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRqllaFHPALPVIFLT 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599920   77 SyaslRSA-VD---SMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSANGG 130
Cdd:PRK11083  83 A----RSDeVDrlvGLEIGADDYVAKPFSPREVAARVRTILRRVKKFAAPSPVIRIGH 136
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
3-111 4.27e-10

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: 57.25  E-value: 4.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK--LAEGIPV-LIMTS 77
Cdd:cd19925   2 NVLIVEDDPMVAEIHRAYVEQVPGftVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRelRAAGHDVdVIVVT 81
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  78 YASLRSAV-DSMKMGAVDYIAKPFDHDEMLQAVAR 111
Cdd:cd19925  82 AANDVETVrEALRLGVVDYLIKPFTFERLRQRLER 116
PRK14084 PRK14084
DNA-binding response regulator;
4-128 5.17e-10

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 59.77  E-value: 5.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGtelIKLAEGI-----PVLIMT 76
Cdd:PRK14084   3 ALIVDDEPLARNELTYLLNEIGGfeEINEAENVKETLEALLINQYDIIFLDINLMDESG---IELAAKIqkmkePPAIIF 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15599920   77 SYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSAN 128
Cdd:PRK14084  80 ATAHDQFAVKAFELNATDYILKPFEQKRIEQAVNKVRATKAKDDNNASAIAN 131
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
4-114 5.33e-10

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: 56.66  E-value: 5.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSYAS 80
Cdd:cd17614   1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVcreVRKTSNVPIIMLTAKDS 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599920  81 LRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:cd17614  81 EVDKVLGLELGADDYVTKPFSNRELLARVKANLR 114
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1-65 6.19e-10

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: 57.21  E-value: 6.19e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599920   1 MAHILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK 65
Cdd:COG2197   1 MIRVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALR 67
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
4-112 8.62e-10

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: 56.26  E-value: 8.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEGI----PVLIMTSYA 79
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAkvktPILILSGLA 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599920  80 SLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17616  81 DIEDKVKGLGFGADDYMTKPFHKDEL---VARI 110
PRK11173 PRK11173
two-component response regulator; Provisional
3-121 2.10e-09

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 57.72  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK-LAEGIPVLIMtsYASL 81
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLAReLREQANVALM--FLTG 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15599920   82 R-SAVD---SMKMGAVDYIAKPFDHDEmLQAVARILKDRQENRS 121
Cdd:PRK11173  83 RdNEVDkilGLEIGADDYITKPFNPRE-LTIRARNLLSRTMNLG 125
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-114 2.19e-09

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


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 54.88  E-value: 2.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERN-QYQVSEAGSVQEAQERYTIPS-FDMVVSDLRLPGAPGTELIK--LAEGIPVLIMTSY 78
Cdd:cd19921   1 KVLIVEDSKTFSKVLKHLIAQElGLEVDVAETLAEAKALLEEGDdYFAALVDLNLPDAPNGEAVDlvLEKGIPVIVLTGS 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599920  79 --ASLRSAVdsMKMGAVDYIAKpfDHDEMLQAVARILK 114
Cdd:cd19921  81 fdEDKRETL--LSKGVVDYVLK--DSRYSYDYVVKLVR 114
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
4-99 2.84e-09

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: 54.33  E-value: 2.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQE--RYTIPSFDMVVSDLRLPGAPGTELIKL------AEGIPVLIM 75
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDvlEDEQNEIDLILTEVDLPVSSGFKLLSYimrhkiCKNIPVIMM 80
                        90       100
                ....*....|....*....|....
gi 15599920  76 TSYASLRSAVDSMKMGAVDYIAKP 99
Cdd:cd17582  81 SSQDSVGVVFKCLSKGAADYLVKP 104
PRK10610 PRK10610
chemotaxis protein CheY;
5-114 2.96e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 54.98  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    5 LIVEDETIIRSALRRLL-ERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL--AEG----IPVLIMTS 77
Cdd:PRK10610   9 LVVDDFSTMRRIVRNLLkELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTirADGamsaLPVLMVTA 88
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15599920   78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:PRK10610  89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
4-114 3.47e-09

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 56.86  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL----AEGIPVLIMTSYA 79
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMlrsaNKGMPILLLTALG 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:PRK09836  83 TIEHRVKGLELGADDYLVKPFAFAELLARVRTLLR 117
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
2-112 5.20e-09

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: 54.01  E-value: 5.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   2 AHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTE---LIKLAEGIPVLIMTSY 78
Cdd:cd17626   1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEvcrQIRAESGVPIVMLTAK 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17626  81 SDTVDVVLGLESGADDYVAKPFKPKEL---VARI 111
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
4-100 5.97e-09

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: 53.27  E-value: 5.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTI-PSFDMVVSDLRLPGAPGTELIKLAEGI----PVLIMTSY 78
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQgKDIDIVVTDIVMPEMDGIELAREARKIdpdvKILFISGG 81
                        90       100
                ....*....|....*....|..
gi 15599920  79 ASLRSAVDSMKMGAVDYIAKPF 100
Cdd:cd18160  82 AAAAPELLSDAVGDNATLKKPF 103
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
4-100 6.30e-09

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 53.50  E-value: 6.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYT-IPSFDMVVSDLRLPGAP-GTELIKLAE----GIPVLIMTS 77
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLEsGPDIDLLVTDVIMPGGMnGSQLAEEARrrrpDLKVLLTSG 80
                        90       100
                ....*....|....*....|...
gi 15599920  78 YASLRSAVDSMKMGaVDYIAKPF 100
Cdd:cd18161  81 YAENAIEGGDLAPG-VDVLSKPF 102
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
4-123 9.32e-09

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: 53.91  E-value: 9.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLErNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEGI---PV-LIMTSYA 79
Cdd:cd17596   3 ILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERwpeVVrIIISGYT 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15599920  80 SLRSAVDSMKMGAV-DYIAKPFDHDEMLQAV---ARILKDRQENRSAA 123
Cdd:cd17596  82 DSEDIIAGINEAGIyQYLTKPWHPDQLLLTVrnaARLFELQRENERLS 129
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
4-99 1.00e-08

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: 53.15  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEA---------QERYTIPSFDMVVSDLRLPGAPGTELIKLAEG----- 69
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEAlnklenlakEGNDLSKELDLIITDIEMPKMDGYELTFELRDdprla 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599920  70 -IPVLIMTSYASLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19924  81 nIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
4-99 1.17e-08

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: 52.51  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLIMTSYA 79
Cdd:cd19928   1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIprikKARPDLPIIVMSAQN 80
                        90       100
                ....*....|....*....|
gi 15599920  80 SLRSAVDSMKMGAVDYIAKP 99
Cdd:cd19928  81 TLMTAVKAAERGAFEYLPKP 100
PRK10816 PRK10816
two-component system response regulator PhoP;
4-111 1.43e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 55.13  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL----AEGIPVLIMTSYA 79
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRwrsnDVSLPILVLTARE 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEM---LQAVAR 111
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPFHIEEVmarMQALMR 117
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
4-112 1.52e-08

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: 52.74  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEA--QERYTIPsfDMVVSDLRLPGAPGTELI-KLAE---GIPVLIMTS 77
Cdd:cd17615   2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEAlaAAREFRP--DAVVLDIMLPDMDGLEVLrRLRAdgpDVPVLFLTA 79
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17615  80 KDSVEDRIAGLTAGGDDYVTKPFSLEEV---VARL 111
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
4-112 1.61e-08

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: 52.69  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEG---IPVLIMTSYAS 80
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKtsqVPVLMLTARGD 80
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599920  81 LRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:cd17623  81 DIDRILGLELGADDYLPKPFNPREL---VARI 109
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
3-113 1.64e-08

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 52.38  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQE--RYTIPsfDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTS 77
Cdd:cd19938   1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPyvRHTPP--DLILLDLMLPGTDGLTLcreIRRFSDVPIIMVTA 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd19938  79 RVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
173-323 1.77e-08

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 53.07  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   173 VLIQGESGTGK-ELVARALHNLSKRakapliSVNCAAIPETLIESELFGH-----EKGAFTGASAGRAglveAADGGTLF 246
Cdd:pfam07728   2 VLLVGPPGTGKtELAERLAAALSNR------PVFYVQLTRDTTEEDLFGRrnidpGGASWVDGPLVRA----AREGEIAV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   247 LDEIGELPLEAQARLLRVLQEGEIR---RVGSVQSQKVDVRLIAATHrdlktlaktgqfreDLYYRLHVISlklPALRER 323
Cdd:pfam07728  72 LDEINRANPDVLNSLLSLLDERRLLlpdGGELVKAAPDGFRLIATMN--------------PLDRGLNELS---PALRSR 134
PRK10336 PRK10336
two-component system response regulator QseB;
4-112 1.82e-08

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 54.90  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIMTSYA 79
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILRewreKGQREPVLILTARD 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFdhdEMLQAVARI 112
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPF---ALIEVAARL 112
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
3-112 4.17e-08

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 51.65  E-value: 4.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDE----TIIRSALRRLLERNQYQVSEAGsvQEA------QERYTI-PSFDMVVSDLRLPGAPGTELikLAE--- 68
Cdd:cd17557   1 TILLVEDNpgdaELIQEAFKEAGVPNELHVVRDG--EEAldflrgEGEYADaPRPDLILLDLNMPRMDGFEV--LREika 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15599920  69 -----GIPVLIMTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARI 112
Cdd:cd17557  77 dpdlrRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSL 125
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1-112 7.71e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 53.27  E-value: 7.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQErYTIPSFDMVVSDLRLPGAPGTELIK---LAEGIPVLIMTS 77
Cdd:PRK10955   1 MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALD-LLDDSIDLLLLDVMMPKKNGIDTLKelrQTHQTPVIMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15599920   78 YASLRSAVDSMKMGAVDYIAKPFDHDEMlqaVARI 112
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDREL---VARI 111
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
4-116 9.20e-08

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: 50.47  E-value: 9.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERN-QYQV-SEAGSVQEAQERYTIPSFDMVVSDLRLPGAPG---TELIKLAEGIPVLIMTSY 78
Cdd:cd17541   3 VLIVDDSAVMRKLLSRILESDpDIEVvGTARDGEEALEKIKELKPDVITLDIEMPVMDGleaLRRIMAERPTPVVMVSSL 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15599920  79 ASLRSAV--DSMKMGAVDYIAKPFDH-DEMLQAVARILKDR 116
Cdd:cd17541  83 TEEGAEItlEALELGAVDFIAKPSGGiSLDLEEIAEELIEK 123
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
4-99 1.31e-07

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: 50.06  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQE-----------RYTIPSFDMVVSDLRLPGAPGTELIK------- 65
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEflgledeedssNFNEPKVNMIITDYCMPGMTGYDLLKkvkessa 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599920  66 LAEgIPVLIMTSYASLRSAVDSMKMGAVDYIAKP 99
Cdd:cd17581  81 LKE-IPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
3-113 2.34e-07

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: 49.47  E-value: 2.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   3 HILIVEDETIIRSALRRLLER-NQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPG-TELIKLAE-----GIPVLIM 75
Cdd:cd17552   3 RILVIDDEEDIREVVQACLEKlAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGlATLKKLQAnpetqSIPVILL 82
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599920  76 TSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17552  83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
PRK15479 PRK15479
transcriptional regulator TctD;
4-121 6.78e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 50.11  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI----KLAEGIPVLIMTSYA 79
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLqrlrKRGQTLPVLLLTARS 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15599920   80 SLRSAVDSMKMGAVDYIAKPFDHDEmLQAVARILKDRQENRS 121
Cdd:PRK15479  83 AVADRVKGLNVGADDYLPKPFELEE-LDARLRALLRRSAGQV 123
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
4-99 2.71e-06

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 45.90  E-value: 2.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSYAS 80
Cdd:cd19936   1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELlqrLRQKSTLPVIFLTSKDD 80
                        90
                ....*....|....*....
gi 15599920  81 LRSAVDSMKMGAVDYIAKP 99
Cdd:cd19936  81 EIDEVFGLRMGADDYITKP 99
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
4-113 2.78e-06

phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response regulators; This subfamily is composed of stand-alone response regulators (RRs) containing the PFxFATG[G/Y] motif; RRs with such a motif are also called ''FAT GUY'' response regulators. Included in this subfamily are Sphingomonas melonis SdrG, Sinorhizobium meliloti Sma0114, and Erythrobacter litoralis EL_LovR. SdrG is involved in the control of the general stress response. Sma0114 is part of the Sma0113/Sma0114 two-component system (TCS) that is involved in catabolite repression and polyhydroxy butyrate synthesis. EL_LovR is involved in a light-regulated TCS. PFxFATG[G/Y] RRs are typically associated with histidine-tryptophan-glutamate (HWE) histidine kinases that constitute a subclass of the larger histidine kinase superfamily characterized by an altered ATP binding site, which lacks the F-box that is normally an integral component of the ATP lid. The PFxFATG[G/Y] motif is involved in conformational changes after phosphorylation that results in the activation of the RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 45.92  E-value: 2.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQ-VSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL--IKLAEGIPVLIMTSYAS 80
Cdd:cd17586   1 VLVLEDEPLIAMNLEDALEDLGGKeVVTAATCAEALRSLADGPIDIAILDVNLGGETSIPVadALKRRAIPFIFATGYGD 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599920  81 lRSAVDSMKMGaVDYIAKPFDHDEMLQAVARIL 113
Cdd:cd17586  81 -SHGIDSRLID-VPVLRKPFDADSALAALAMLL 111
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
4-101 2.82e-06

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: 46.22  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSYAS 80
Cdd:cd17622   3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLcrdLRPKYQGPILLLTALDS 82
                        90       100
                ....*....|....*....|.
gi 15599920  81 LRSAVDSMKMGAVDYIAKPFD 101
Cdd:cd17622  83 DIDHILGLELGADDYVVKPVE 103
PRK09483 PRK09483
response regulator; Provisional
1-109 3.61e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 47.79  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    1 MAHILIVEDETIIRSALRRLLE--RNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTE----LIKLAEGIPVLI 74
Cdd:PRK09483   1 MINVLLVDDHELVRAGIRRILEdiKGIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEatrkILRYTPDVKIIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15599920   75 MTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:PRK09483  81 LTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAI 115
PRK13435 PRK13435
response regulator; Provisional
4-125 3.83e-06

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 46.58  E-value: 3.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVS-EAGSVQEAQE--RYTIPSFDMVvsDLRLP-GAPGTELI-KLAE--GIPVLIMT 76
Cdd:PRK13435   8 VLIVEDEALIALELEKLVEEAGHEVVgIAMSSEQAIAlgRRRQPDVALV--DVHLAdGPTGVEVArRLSAdgGVEVVFMT 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15599920   77 syASLRSAVDSMKmGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPV 125
Cdd:PRK13435  86 --GNPERVPHDFA-GALGVIAKPYSPRGVARALSYLSARRVGDRASGPT 131
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1-112 5.93e-06

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 47.50  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    1 MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK---LAEGIPVLIMtS 77
Cdd:PRK13856   1 MKHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRslaTKSDVPIIII-S 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15599920   78 YASLRSA--VDSMKMGAVDYIAKPFDHDEMLqavARI 112
Cdd:PRK13856  80 GDRLEEAdkVVALELGATDFIAKPFGTREFL---ARI 113
PRK11517 PRK11517
DNA-binding response regulator HprR;
4-109 1.18e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 46.43  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK---LAEGIPVLIMTSYAS 80
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQtlrTAKQTPVICLTARDS 82
                         90       100
                 ....*....|....*....|....*....
gi 15599920   81 LRSAVDSMKMGAVDYIAKPFDHDEMLQAV 109
Cdd:PRK11517  83 VDDRVRGLDSGANDYLVKPFSFSELLARV 111
PLN03029 PLN03029
type-a response regulator protein; Provisional
3-120 1.27e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 46.18  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    3 HILIVEDETIIRSALRRLLERNQYQVS--EAGSV--------QEAQERYTIPS----------FDMVVSDLRLPGAPGTE 62
Cdd:PLN03029  10 HVLAVDDSLIDRKLIEKLLKTSSYQVTtvDSGSKalkflglhEDDRSNPDTPSvspnshqeveVNLIITDYCMPGMTGYD 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599920   63 LIKLAE------GIPVLIMTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK-----DRQENR 120
Cdd:PLN03029  90 LLKKIKessslrNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKtksknQKQENQ 158
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
4-107 1.61e-05

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: 43.79  E-value: 1.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLER-NQYQVSEAGSVQEAQERYTIPSFDMVVSDLRL-PGAPGTEL---IKLAEGIP---VLIM 75
Cdd:cd17589   1 FLIVDDQPTFRSMLKSMLRSlGVTRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLleeLRHKKLISpstVFIM 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599920  76 TSYASLRSAVdsmkMGAV-----DYIAKPFDHDEMLQ 107
Cdd:cd17589  81 VTGESSRAMV----LSALelepdDYLLKPFTVSELRE 113
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
2-113 1.93e-05

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 45.64  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    2 AHILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIK----LAEGIPVLIM 75
Cdd:PRK09935   4 ASVIIMDTHPIIRMSIEVLLQKNSelQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKrikqIQSTVKVLFL 83
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15599920   76 TSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARIL 113
Cdd:PRK09935  84 SSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMIL 121
PRK15369 PRK15369
two component system response regulator;
4-98 2.42e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 45.45  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLE-RNQYQVseAGSVQEAQERY-----TIPsfDMVVSDLRLPGAPGTELI-KLAEGIP---VL 73
Cdd:PRK15369   6 ILLVDDHELIINGIKNMLApYPRYKI--VGQVDNGLEVYnacrqLEP--DIVILDLGLPGMNGLDVIpQLHQRWPamnIL 81
                         90       100
                 ....*....|....*....|....*
gi 15599920   74 IMTSYASLRSAVDSMKMGAVDYIAK 98
Cdd:PRK15369  82 VLTARQEEHMASRTLAAGALGYVLK 106
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
4-114 2.64e-05

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: 43.41  E-value: 2.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQ--YQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPG----TELIKLAEGIPVLIMTS 77
Cdd:cd19930   1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGlevaAELREELPDTKVLIVTT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15599920  78 YAS---LRSAVDSmkmGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:cd19930  81 FGRpgyFRRALAA---GVDGYVLKDRPIEELADAIRTVHA 117
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
4-114 2.78e-05

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 43.49  E-value: 2.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQY--QVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKL--AEGIP--VLIMTS 77
Cdd:cd19931   1 VLLIDDHPLLRKGIKQLIELDPDftVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKAlrEEGVSarIVILTV 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599920  78 YASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:cd19931  81 SDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
4-114 1.44e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 43.14  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    4 ILIVEDETIIRSALRRLLERNQYQVS--EAGSVQEAQERYTIPsfDMVVSDLRLPGAPGTEL---IKLAEGIPVLIMTSY 78
Cdd:PRK10710  13 ILIVEDEPKLGQLLIDYLQAASYATTllSHGDEVLPYVRQTPP--DLILLDLMLPGTDGLTLcreIRRFSDIPIVMVTAK 90
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15599920   79 ASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILK 114
Cdd:PRK10710  91 IEEIDRLLGLEIGADDYICKPYSPREVVARVKTILR 126
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
173-291 1.45e-04

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 41.42  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   173 VLIQGESGTGKELVARAlhnLSKRAKAPLISVNCaaipetlieSELFGHEKGAFTGASAGRAGLVEAADGGTLFLDEI-- 250
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKA---VAKELGAPFIEISG---------SELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIda 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15599920   251 ---------GELPLEAQARLLRVLQEgeirrvgsVQSQKVDVRLIAATHR 291
Cdd:pfam00004  69 lagsrgsggDSESRRVVNQLLTELDG--------FTSSNSKVIVIAATNR 110
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
4-109 4.26e-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: 39.92  E-value: 4.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLERNQYQV-SEAGSVQEAQERYTIPSFDMVVSDLRLP-GAPGTEL---IKLAEGIPVLIMTSY 78
Cdd:cd17540   3 VLIIEDEPLIAMDLEQIVEDLGHQVvGIARTRDEAVALARRERPDLILADIQLAdGSSGIDAvneILTTHDVPVIFVTAY 82
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599920  79 --ASLRSAvdsmKMGAVDYIAKPFDHDEMLQAV 109
Cdd:cd17540  83 peRLLTGE----RPEPTFLITKPFDPEMVKAAI 111
PRK13557 PRK13557
histidine kinase; Provisional
3-113 4.57e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 42.74  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    3 HILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERY-TIPSFDMVVSDLRLPGA-PGTELIKLAE----GIPVLIMT 76
Cdd:PRK13557 417 TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPGGmNGVMLAREARrrqpKIKVLLTT 496
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15599920   77 SYAslRSAVDSMKMGA--VDYIAKPFDHDEMLQAVARIL 113
Cdd:PRK13557 497 GYA--EASIERTDAGGseFDILNKPYRRAELARRVRMVL 533
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
4-111 2.21e-03

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: 38.19  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920   4 ILIVEDETIIRSALRRLLER-NQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI-KLAE---GIPVLIMTSY 78
Cdd:cd17530   3 VLVLDDDPFQCMMAATILEDlGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLrHLAEshsNAAVILMSGL 82
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599920  79 -ASLRSAVDSMK----MGAVDYIAKPFDHDEMLQAVAR 111
Cdd:cd17530  83 dGGILESAETLAgangLNLLGTLSKPFSPEELTELLTK 120
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
5-109 2.35e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 39.11  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    5 LIVEDETIIRSALRRLLERNQYQV-SEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI-----KLAEGIPVLIMTS- 77
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEIlAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLetlrkRQYSGIIIIVSAKn 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15599920   78 --YASLRSAvdsmKMGAVDYIAKPFDHDEMLQAV 109
Cdd:PRK09958  84 dhFYGKHCA----DAGANGFVSKKEGMNNIIAAI 113
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
424-471 3.01e-03

RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the presumed domain. The domain is found in algal minus dominance proteins as well as plant proteins involved in nitrogen-controlled development.


Pssm-ID: 460427  Cd Length: 49  Bit Score: 35.56  E-value: 3.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15599920   424 DLSLEDYFQHFvlehqdHMTETELARKLGISRKCLWERRQRLGIPR---RK 471
Cdd:pfam02042   1 SITLEDLSQYF------HLPIKEAAKELGVSLTTLKRICRRLGIPRwphRK 45
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
4-113 3.46e-03

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 40.10  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920     4 ILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELI-KLAE---GIPVLIMTSYA 79
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTrKLREqnsSLPIWGLTANA 1040
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15599920    80 SLRSAVDSMKMGAVDYIAKPF------DHDEMLQAVARIL 113
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLtldvlkTHLSQLHQVAHIA 1080
PRK10430 PRK10430
two-component system response regulator DcuR;
1-100 4.25e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 38.94  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599920    1 MAHILIVEDETIIRSALRRLLErnqyQVS------EAGSVQEAQERYTIP--SFDMVVSDLRLPGAPGTELI----KLAE 68
Cdd:PRK10430   1 MINVLIVDDDAMVAELNRRYVA----QIPgfqccgTASTLEQAKEIIFNSdtPIDLILLDIYMQQENGLDLLpvlhEAGC 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 15599920   69 GIPVLIMTSYASLRSAVDSMKMGAVDYIAKPF 100
Cdd:PRK10430  77 KSDVIVISSAADAATIKDSLHYGVVDYLIKPF 108
 
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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