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Conserved domains on  [gi|15598899|ref|NP_252393|]
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chemotaxis sensor/effector fusion protein [Pseudomonas aeruginosa PAO1]

Protein Classification

hybrid sensor histidine kinase/response regulator( domain architecture ID 14294233)

two-component hybrid sensor histidine kinase/response regulator that may function in chemotaxis by relaying sensory signals from chemoreceptors to flagellar motors

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
6-630 1.84e-168

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 497.40  E-value: 1.84e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   6 MRDASLLELFRLEAEAQTQVLNAGLMALERSPTQADQLEACMRAAHSLKGAARIVGLDAGVRVAHVMEDCLVEAQDGRLL 85
Cdd:COG0643   1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  86 LQSEHIDALLQGCDLLLRIGtppagDAGWAEGAGREEIDGLVLRLEGLVRSGLPLARAELPATTPGLPEAVPEAPPaasa 165
Cdd:COG0643  81 LTPELIDLLLEALDALRALL-----DALEAGGEPPADISALLARLDASEEAIEEVVADEVEISPPAPAALEPAPAA---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 166 aasddnDEEPAGQAGGEQAEERRSRVLRVTAERLDRLLDissksLVEfqrikpladslqrlrrlqssasraldvvrETVQ 245
Cdd:COG0643 152 ------APPAEAAAAAAEAAAAASETVRVDVERLDRLMN-----LVG-----------------------------ELVI 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 246 etaldpqAQAMLGEARQLIGEcqqmlvQHIADLDEFAWQGGQRAQVLYDAALASRMRPFADVLSGQARMVRDLGRSLGKQ 325
Cdd:COG0643 192 -------TRARLEQLAEELED------ESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKE 258
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 326 VRLLVEGESTQVDRDVLEKLEAPLTHLLRNAVDHGIEAPETRLAAGKPAEGRITIRARHHAGMLVLELSDDGGGIDLQRL 405
Cdd:COG0643 259 VELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKI 338
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 406 RETVLNRQFATAETVAQLSEEELLAFLFLPGFSMREQVTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPL 485
Cdd:COG0643 339 RAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 486 TLSVVRSLVVEIGEEAYAFPLAHIERMCELEAEEIVQLEGRQHFWYEGRHVGLVSAAQLLQRPESSRTEGAIPVVVVRDR 565
Cdd:COG0643 419 TLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSG 498
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598899 566 DAVYGVAVERFVGERTLVVMPLDPRLGKVRDVSAGALLDDGSPVLILDVEDLLHSVGKLLSSGRL 630
Cdd:COG0643 499 GRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARARARAAAA 563
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
648-748 1.15e-42

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: 150.22  E-value: 1.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNAL---------RSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQ 718
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                        90       100       110
                ....*....|....*....|....*....|
gi 15598899 719 SLPVMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd19924  81 NIPVILNSSLSGEFSRARGKKVGADAYLAK 110
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
6-630 1.84e-168

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 497.40  E-value: 1.84e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   6 MRDASLLELFRLEAEAQTQVLNAGLMALERSPTQADQLEACMRAAHSLKGAARIVGLDAGVRVAHVMEDCLVEAQDGRLL 85
Cdd:COG0643   1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  86 LQSEHIDALLQGCDLLLRIGtppagDAGWAEGAGREEIDGLVLRLEGLVRSGLPLARAELPATTPGLPEAVPEAPPaasa 165
Cdd:COG0643  81 LTPELIDLLLEALDALRALL-----DALEAGGEPPADISALLARLDASEEAIEEVVADEVEISPPAPAALEPAPAA---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 166 aasddnDEEPAGQAGGEQAEERRSRVLRVTAERLDRLLDissksLVEfqrikpladslqrlrrlqssasraldvvrETVQ 245
Cdd:COG0643 152 ------APPAEAAAAAAEAAAAASETVRVDVERLDRLMN-----LVG-----------------------------ELVI 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 246 etaldpqAQAMLGEARQLIGEcqqmlvQHIADLDEFAWQGGQRAQVLYDAALASRMRPFADVLSGQARMVRDLGRSLGKQ 325
Cdd:COG0643 192 -------TRARLEQLAEELED------ESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKE 258
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 326 VRLLVEGESTQVDRDVLEKLEAPLTHLLRNAVDHGIEAPETRLAAGKPAEGRITIRARHHAGMLVLELSDDGGGIDLQRL 405
Cdd:COG0643 259 VELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKI 338
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 406 RETVLNRQFATAETVAQLSEEELLAFLFLPGFSMREQVTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPL 485
Cdd:COG0643 339 RAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 486 TLSVVRSLVVEIGEEAYAFPLAHIERMCELEAEEIVQLEGRQHFWYEGRHVGLVSAAQLLQRPESSRTEGAIPVVVVRDR 565
Cdd:COG0643 419 TLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSG 498
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598899 566 DAVYGVAVERFVGERTLVVMPLDPRLGKVRDVSAGALLDDGSPVLILDVEDLLHSVGKLLSSGRL 630
Cdd:COG0643 499 GRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
307-484 1.50e-84

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 265.60  E-value: 1.50e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 307 VLSGQARMVRDLGRSLGKQVRLLVEGESTQVDRDVLEKLEAPLTHLLRNAVDHGIEAPETRLAAGKPAEGRITIRARHHA 386
Cdd:cd16916   1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 387 GMLVLELSDDGGGIDLQRLRETVLNRQFATAETVAQLSEEELLAFLFLPGFSMREQVTEVSGRGVGLDAVQHMVRQLRGG 466
Cdd:cd16916  81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160
                       170
                ....*....|....*...
gi 15598899 467 VRMEQRQGQGALFHVEVP 484
Cdd:cd16916 161 IEVESEPGQGTTFTIRLP 178
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
30-643 1.43e-60

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 216.52  E-value: 1.43e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   30 LMALERSPTQADQLEACMRAAHSLKGAARIVGLDAGVRVAHVMEDCLVEAQDGRLLLQSEHIDALLQGCDLL-------- 101
Cdd:PRK10547  25 LLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMqeqldayk 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  102 ----------------LR-------IGTPPAGDA---------GWAEGAGREEIDGLVLRLEGLVRSGLPLARAELP--A 147
Cdd:PRK10547 105 tsqepdaasfeyicqaLRqlaleakGETPSAVTRlsvvaiqekSEPQDESPRSQSGLRIILSRLKAGEVDLLEEELGnlG 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  148 TTPGLPEAVPEAPPAASAAASDDN---------DEEpagQAGGEQAEERRSRVLRVTAERLDRLLDISSKSLVEFQRIKP 218
Cdd:PRK10547 185 TLTDVVKGADSLEATLPGSVAEDDitavlcfviEAD---QITFETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQA 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  219 LADSLQRLRRLQSSASRALDVVRETVQetaldpqaqamlgearQLI---GE---CQQMLVQHIADLDEFAW--------Q 284
Cdd:PRK10547 262 PAGRVEREKTARSSESTSIRVAVEKVD----------------QLInlvGElviTQSMLAQRSSELDPVNHgdlitsmgQ 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  285 GGQRAQVLYDAALASRMRPFADVLSGQARMVRDLGRSLGKQVRLLVEGESTQVDRDVLEKLEAPLTHLLRNAVDHGIEAP 364
Cdd:PRK10547 326 LQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELP 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  365 ETRLAAGKPAEGRITIRARHHAGMLVLELSDDGGGIDLQRLRETVLNRQFATAETvaqLSEEELLAFLFLPGFSMREQVT 444
Cdd:PRK10547 406 EKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSEN---MSDEEVGMLIFAPGFSTAEQVT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  445 EVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPLTLSVVRSLVVEIGEEAYAFPLAHIERMCELEAEEIVQLE 524
Cdd:PRK10547 483 DVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREEDLHPLA 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  525 GRQH-FWYEGRHVGLVSAAQL--LQRPESSRTEGAIpvVVVRDRDAVYGVAVERFVGERTLVVMPLDPRLGKVRDVSAGA 601
Cdd:PRK10547 563 GGERvLEVRGEYLPLVELWKVfdVAGAKTEATQGIV--VILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAAT 640
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 15598899  602 LLDDGSPVLILDVEdllhsvgkllssgRLERIDRSRRQAGGA 643
Cdd:PRK10547 641 ILGDGSVALIVDVS-------------ALQALNREQRMANTA 669
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
648-748 1.15e-42

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: 150.22  E-value: 1.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNAL---------RSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQ 718
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                        90       100       110
                ....*....|....*....|....*....|
gi 15598899 719 SLPVMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd19924  81 NIPVILNSSLSGEFSRARGKKVGADAYLAK 110
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
643-769 9.25e-34

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 125.73  E-value: 9.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 643 AQRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPV 722
Cdd:COG0784   3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPI 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15598899 723 MVVSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAVVVLIGEAQG 769
Cdd:COG0784  83 IALTAYADEEDRERALEAGADDYLTK-PVDPEELLEALRRLLARASA 128
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
648-760 4.31e-25

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: 100.30  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMVVSY 727
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 15598899   728 KDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSK-PFDPDELLAAI 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
346-486 1.07e-19

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 85.01  E-value: 1.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899    346 EAPLTHLLRNAVDHGIEAPetrlaagkPAEGRITIRARHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlse 425
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYT--------PEGGRITVTLERDGDHVEITVEDNGPGIP------------------------ 50
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598899    426 EELLAFLFLPGFSMREQVTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPLT 486
Cdd:smart00387  51 PEDLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PRK10610 PRK10610
chemotaxis protein CheY;
647-748 4.05e-19

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 83.87  E-value: 4.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGY-DVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                         90       100
                 ....*....|....*....|...
gi 15598899  726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10610  87 TAEAKKENIIAAAQAGASGYVVK 109
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
646-700 5.52e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.05  E-value: 5.52e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15598899    646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMP 700
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
346-486 3.05e-11

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 60.84  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   346 EAPLTHLLRNAVDHGIEApetrlaAGKPAEGRITIrarHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlse 425
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKH------AAKAGEITVTL---SEGGELTLTVEDNGIGIP------------------------ 49
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598899   426 EELLAFLFLPGFsmREQVTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPLT 486
Cdd:pfam02518  50 PEDLPRIFEPFS--TADKRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
647-748 1.67e-08

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 56.34  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   647 RILVVDDSltvRE----LERKLLLGRGYDVA-VAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLP 721
Cdd:TIGR02875   4 RIVIADDN---KEfcnlLKEYLAAQPDMEVVgVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARPR 80
                          90       100
                  ....*....|....*....|....*..
gi 15598899   722 VMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:TIGR02875  81 VIMLSAFGQEKITQRAVALGADYYVLK 107
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
6-630 1.84e-168

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 497.40  E-value: 1.84e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   6 MRDASLLELFRLEAEAQTQVLNAGLMALERSPTQADQLEACMRAAHSLKGAARIVGLDAGVRVAHVMEDCLVEAQDGRLL 85
Cdd:COG0643   1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  86 LQSEHIDALLQGCDLLLRIGtppagDAGWAEGAGREEIDGLVLRLEGLVRSGLPLARAELPATTPGLPEAVPEAPPaasa 165
Cdd:COG0643  81 LTPELIDLLLEALDALRALL-----DALEAGGEPPADISALLARLDASEEAIEEVVADEVEISPPAPAALEPAPAA---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 166 aasddnDEEPAGQAGGEQAEERRSRVLRVTAERLDRLLDissksLVEfqrikpladslqrlrrlqssasraldvvrETVQ 245
Cdd:COG0643 152 ------APPAEAAAAAAEAAAAASETVRVDVERLDRLMN-----LVG-----------------------------ELVI 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 246 etaldpqAQAMLGEARQLIGEcqqmlvQHIADLDEFAWQGGQRAQVLYDAALASRMRPFADVLSGQARMVRDLGRSLGKQ 325
Cdd:COG0643 192 -------TRARLEQLAEELED------ESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKE 258
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 326 VRLLVEGESTQVDRDVLEKLEAPLTHLLRNAVDHGIEAPETRLAAGKPAEGRITIRARHHAGMLVLELSDDGGGIDLQRL 405
Cdd:COG0643 259 VELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKI 338
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 406 RETVLNRQFATAETVAQLSEEELLAFLFLPGFSMREQVTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPL 485
Cdd:COG0643 339 RAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 486 TLSVVRSLVVEIGEEAYAFPLAHIERMCELEAEEIVQLEGRQHFWYEGRHVGLVSAAQLLQRPESSRTEGAIPVVVVRDR 565
Cdd:COG0643 419 TLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSG 498
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598899 566 DAVYGVAVERFVGERTLVVMPLDPRLGKVRDVSAGALLDDGSPVLILDVEDLLHSVGKLLSSGRL 630
Cdd:COG0643 499 GRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
307-484 1.50e-84

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 265.60  E-value: 1.50e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 307 VLSGQARMVRDLGRSLGKQVRLLVEGESTQVDRDVLEKLEAPLTHLLRNAVDHGIEAPETRLAAGKPAEGRITIRARHHA 386
Cdd:cd16916   1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 387 GMLVLELSDDGGGIDLQRLRETVLNRQFATAETVAQLSEEELLAFLFLPGFSMREQVTEVSGRGVGLDAVQHMVRQLRGG 466
Cdd:cd16916  81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160
                       170
                ....*....|....*...
gi 15598899 467 VRMEQRQGQGALFHVEVP 484
Cdd:cd16916 161 IEVESEPGQGTTFTIRLP 178
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
30-643 1.43e-60

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 216.52  E-value: 1.43e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   30 LMALERSPTQADQLEACMRAAHSLKGAARIVGLDAGVRVAHVMEDCLVEAQDGRLLLQSEHIDALLQGCDLL-------- 101
Cdd:PRK10547  25 LLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMqeqldayk 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  102 ----------------LR-------IGTPPAGDA---------GWAEGAGREEIDGLVLRLEGLVRSGLPLARAELP--A 147
Cdd:PRK10547 105 tsqepdaasfeyicqaLRqlaleakGETPSAVTRlsvvaiqekSEPQDESPRSQSGLRIILSRLKAGEVDLLEEELGnlG 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  148 TTPGLPEAVPEAPPAASAAASDDN---------DEEpagQAGGEQAEERRSRVLRVTAERLDRLLDISSKSLVEFQRIKP 218
Cdd:PRK10547 185 TLTDVVKGADSLEATLPGSVAEDDitavlcfviEAD---QITFETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQA 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  219 LADSLQRLRRLQSSASRALDVVRETVQetaldpqaqamlgearQLI---GE---CQQMLVQHIADLDEFAW--------Q 284
Cdd:PRK10547 262 PAGRVEREKTARSSESTSIRVAVEKVD----------------QLInlvGElviTQSMLAQRSSELDPVNHgdlitsmgQ 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  285 GGQRAQVLYDAALASRMRPFADVLSGQARMVRDLGRSLGKQVRLLVEGESTQVDRDVLEKLEAPLTHLLRNAVDHGIEAP 364
Cdd:PRK10547 326 LQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELP 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  365 ETRLAAGKPAEGRITIRARHHAGMLVLELSDDGGGIDLQRLRETVLNRQFATAETvaqLSEEELLAFLFLPGFSMREQVT 444
Cdd:PRK10547 406 EKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSEN---MSDEEVGMLIFAPGFSTAEQVT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  445 EVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPLTLSVVRSLVVEIGEEAYAFPLAHIERMCELEAEEIVQLE 524
Cdd:PRK10547 483 DVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREEDLHPLA 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  525 GRQH-FWYEGRHVGLVSAAQL--LQRPESSRTEGAIpvVVVRDRDAVYGVAVERFVGERTLVVMPLDPRLGKVRDVSAGA 601
Cdd:PRK10547 563 GGERvLEVRGEYLPLVELWKVfdVAGAKTEATQGIV--VILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAAT 640
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 15598899  602 LLDDGSPVLILDVEdllhsvgkllssgRLERIDRSRRQAGGA 643
Cdd:PRK10547 641 ILGDGSVALIVDVS-------------ALQALNREQRMANTA 669
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
648-748 1.15e-42

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: 150.22  E-value: 1.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNAL---------RSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQ 718
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                        90       100       110
                ....*....|....*....|....*....|
gi 15598899 719 SLPVMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd19924  81 NIPVILNSSLSGEFSRARGKKVGADAYLAK 110
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
643-769 9.25e-34

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 125.73  E-value: 9.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 643 AQRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPV 722
Cdd:COG0784   3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPI 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15598899 723 MVVSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAVVVLIGEAQG 769
Cdd:COG0784  83 IALTAYADEEDRERALEAGADDYLTK-PVDPEELLEALRRLLARASA 128
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
645-763 8.74e-33

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: 124.64  E-value: 8.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 645 RKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMV 724
Cdd:COG3706   1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598899 725 VSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAVVVL 763
Cdd:COG3706  81 LTALDDEEDRARALEAGADDYLTK-PFDPEELLARVDLV 118
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
645-764 9.74e-29

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: 113.90  E-value: 9.74e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 645 RKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqSLPVMV 724
Cdd:COG0745   1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPS--DIPIIM 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598899 725 VSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAVVVLI 764
Cdd:COG0745  79 LTARDDEEDRVRGLEAGADDYLTK-PFDPEELLARIRALL 117
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
644-760 1.74e-26

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: 108.33  E-value: 1.74e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 644 QRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVM 723
Cdd:COG3437   5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVI 84
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15598899 724 VVSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:COG3437  85 FLTALADPEDRERALEAGADDYLTK-PFDPEELLARV 120
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
648-760 4.31e-25

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: 100.30  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMVVSY 727
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 15598899   728 KDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSK-PFDPDELLAAI 110
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
646-760 1.20e-24

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: 99.30  E-value: 1.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:cd17562   1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:cd17562  81 TTESSDEKKQEGKAAGATGWLVK-PFDPEQLLEVV 114
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
649-748 1.73e-24

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: 98.25  E-value: 1.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 649 LVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMVVSYK 728
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTAK 78
                        90       100
                ....*....|....*....|
gi 15598899 729 DREEDRRRGLDAGADYYLAK 748
Cdd:cd17574  79 DEEEDKVLGLELGADDYITK 98
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
649-748 4.97e-24

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: 96.91  E-value: 4.97e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 649 LVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqSLPVMVVSYK 728
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPP--DIPVIVLTAK 78
                        90       100
                ....*....|....*....|
gi 15598899 729 DREEDRRRGLDAGADYYLAK 748
Cdd:cd00156  79 ADEEDAVRALELGADDYLVK 98
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
647-748 1.24e-23

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: 96.64  E-value: 1.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGY-DVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:cd19923   2 KVLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                        90       100
                ....*....|....*....|...
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd19923  82 TAEAKKENVIAAAQAGVNNYIVK 104
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
648-748 2.54e-23

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 95.23  E-value: 2.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSR-LQSLPVMVVS 726
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGgGRRTPIIALT 80
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17546  81 ANALEEDREKCLEAGMDDYLSK 102
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
648-748 1.51e-22

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 92.83  E-value: 1.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVSY 727
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd19927  81 KGMTSDRIKGYNAGCDGYLSK 101
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
648-748 7.22e-22

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: 90.58  E-value: 7.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqSLPVMVVSY 727
Cdd:cd19935   1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGK--QTPVLMLTA 78
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd19935  79 RDSVEDRVKGLDLGADDYLVK 99
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
647-748 2.96e-21

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: 89.06  E-value: 2.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLL-LGRGYD-VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqSLPVMV 724
Cdd:COG4753   1 KVLIVDDEPLIREGLKRILeWEAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDP--DTKIII 78
                        90       100
                ....*....|....*....|....
gi 15598899 725 VSYKDREEDRRRGLDAGADYYLAK 748
Cdd:COG4753  79 LSGYSDFEYAQEAIKLGADDYLLK 102
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
648-748 1.53e-20

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: 87.51  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVSY 727
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17580  81 YGQPEDRERALEAGFDAHLVK 101
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
647-748 1.89e-20

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 86.78  E-value: 1.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVS 726
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17538  81 ALDDREDRIRGLEAGADDFLSK 102
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
644-760 4.35e-20

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: 93.49  E-value: 4.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 644 QRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqSLPVM 723
Cdd:COG2204   1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDP--DLPVI 78
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15598899 724 VVSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:COG2204  79 LLTGYGDVETAVEAIKAGAFDYLTK-PFDLEELLAAV 114
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
346-486 1.07e-19

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 85.01  E-value: 1.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899    346 EAPLTHLLRNAVDHGIEAPetrlaagkPAEGRITIRARHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlse 425
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYT--------PEGGRITVTLERDGDHVEITVEDNGPGIP------------------------ 50
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598899    426 EELLAFLFLPGFSMREQVTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPLT 486
Cdd:smart00387  51 PEDLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PRK10610 PRK10610
chemotaxis protein CheY;
647-748 4.05e-19

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 83.87  E-value: 4.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGY-DVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                         90       100
                 ....*....|....*....|...
gi 15598899  726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10610  87 TAEAKKENIIAAAQAGASGYVVK 109
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
647-748 6.49e-19

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: 82.97  E-value: 6.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVS 726
Cdd:cd17548   1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17548  81 AYAMKGDREKILEAGCDGYISK 102
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
648-748 8.08e-19

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: 82.82  E-value: 8.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqSLPVMVVSY 727
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGN--DLPILVLTA 78
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17627  79 RDSVSDRVAGLDAGADDYLVK 99
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
649-748 1.26e-18

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: 81.94  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 649 LVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVSYK 728
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                        90       100
                ....*....|....*....|
gi 15598899 729 DREEDRRRGLDAGADYYLAK 748
Cdd:cd19937  81 GEEFDKVLGLELGADDYITK 100
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
649-764 1.35e-18

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: 81.88  E-value: 1.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 649 LVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMVVSYK 728
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEG--IETPVLLLTAL 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598899 729 DREEDRRRGLDAGADYYLAKaSFHDEALLDAVVVLI 764
Cdd:cd17625  79 DAVEDRVKGLDLGADDYLPK-PFSLAELLARIRALL 113
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
646-748 1.85e-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: 81.53  E-value: 1.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:cd17618   1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                        90       100
                ....*....|....*....|...
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17618  81 TARGEEEDKVRGLEAGADDYITK 103
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
648-748 2.19e-18

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: 81.60  E-value: 2.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVSY 727
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17598  81 LSDPRDVIRGLECGADNFITK 101
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
648-764 3.47e-18

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: 80.79  E-value: 3.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqSLPVMVVSY 727
Cdd:cd19934   1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLILTA 78
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15598899 728 KDREEDRRRGLDAGADYYLAKaSFHDEALLDAVVVLI 764
Cdd:cd19934  79 RDSWQDKVEGLDAGADDYLTK-PFHIEELLARLRALI 114
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
648-748 7.66e-18

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: 79.13  E-value: 7.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqsLPVMVVSY 727
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA---VPVIVLSA 77
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17620  78 RDEESDKIAALDAGADDYLTK 98
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
648-744 1.13e-17

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 78.71  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVSY 727
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                        90
                ....*....|....*...
gi 15598899 728 KDREEDRRRGLDAGA-DY 744
Cdd:cd19920  81 LTDTEDKVKGFELGAvDY 98
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
647-748 4.20e-17

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: 77.87  E-value: 4.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGY-DVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                        90       100
                ....*....|....*....|...
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17551  82 TADTDREVRLRALEAGATDFLTK 104
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
647-760 7.72e-17

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: 77.46  E-value: 7.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDS-----LTVRELERkllLGRGYDVAVAVDGMDGWNALRSE-------HFDLLITDIDMPRMDGIELVTLVRRD 714
Cdd:cd17557   1 TILLVEDNpgdaeLIQEAFKE---AGVPNELHVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKAD 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15598899 715 SRLQSLPVMVVSYKDREEDRRRGLDAGADYYLAK-ASFhdEALLDAV 760
Cdd:cd17557  78 PDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKpVDF--EEFVEAI 122
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
648-748 2.10e-16

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 75.60  E-value: 2.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMVVSY 727
Cdd:cd17624   1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQG--QSLPVLILTA 78
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17624  79 RDGVDDRVAGLDAGADDYLVK 99
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
648-760 5.85e-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: 74.47  E-value: 5.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRE-LERKLLLGRGYD-VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMVV 725
Cdd:cd17535   1 VLIVDDHPLVREgLRRLLESEPDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIVL 78
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAKASfHDEALLDAV 760
Cdd:cd17535  79 TAHDDPEYVLRALKAGAAGYLLKDS-SPEELIEAI 112
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
646-733 8.06e-16

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: 73.79  E-value: 8.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRrdSRLQSLPVMVV 725
Cdd:cd17554   1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR--EKKPDLPVIIC 78

                ....*....
gi 15598899 726 S-YKDREED 733
Cdd:cd17554  79 TaYSEYKSD 87
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
8-103 1.15e-15

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 72.80  E-value: 1.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   8 DASLLELFRLEAEAQTQVLNAGLMALErsptQADQLEACMRAAHSLKGAARIVGLDAGVRVAHVMEDCLVEAQDGRLLLq 87
Cdd:cd00088   1 MEELLELFLEEAEELLEELERALLELE----DAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDGLEVT- 75
                        90
                ....*....|....*.
gi 15598899  88 SEHIDALLQGCDLLLR 103
Cdd:cd00088  76 PELIDLLLDALDALKA 91
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
646-748 2.09e-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: 2.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLqsLPVMVV 725
Cdd:cd17555   1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPD--TPVIVV 78
                        90       100
                ....*....|....*....|...
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17555  79 SGAGVMSDAVEALRLGAWDYLTK 101
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
647-754 5.97e-15

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: 71.78  E-value: 5.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRsEHFD--LLITDIDMPRMDGIELVTLVRRDSRLQSLPVMV 724
Cdd:cd17544   2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLE-QHPDikLVITDYNMPEMDGFELVREIRKKYSRDQLAIIG 80
                        90       100       110
                ....*....|....*....|....*....|
gi 15598899 725 VSYKDREEDRRRGLDAGADYYLAKASFHDE 754
Cdd:cd17544  81 ISASGDNALSARFIKAGANDFLTKPFLPEE 110
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
645-760 1.27e-14

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 71.54  E-value: 1.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 645 RKRILVVDDSLTVRELERKLL--LGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPV 722
Cdd:COG4565   3 MIRVLIVEDDPMVAELLRRYLerLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDVDV 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598899 723 MVVSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:COG4565  81 IVITAARDPETVREALRAGVVDYLIK-PFTFERLREAL 117
orf27 CHL00148
Ycf27; Reviewed
644-748 4.12e-14

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 72.83  E-value: 4.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  644 QRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVM 723
Cdd:CHL00148   5 SKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES---DVPII 81
                         90       100
                 ....*....|....*....|....*
gi 15598899  724 VVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:CHL00148  82 MLTALGDVSDRITGLELGADDYVVK 106
PRK15479 PRK15479
transcriptional regulator TctD;
647-748 4.88e-14

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 72.06  E-value: 4.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMVVS 726
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRK--RGQTLPVLLLT 79
                         90       100
                 ....*....|....*....|..
gi 15598899  727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK15479  80 ARSAVADRVKGLNVGADDYLPK 101
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
648-760 5.01e-14

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: 68.90  E-value: 5.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYD---VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMV 724
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIDWEELGfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRE--LYPDIKIII 78
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15598899 725 VS-YKDREedrRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:cd17536  79 LSgYDDFEy-aQKAIRLGVVDYLLK-PVDEEELEEAL 113
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
647-748 9.53e-14

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: 68.15  E-value: 9.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDsrLQSLPVMVVS 726
Cdd:cd17615   1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLT 78
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17615  79 AKDSVEDRIAGLTAGGDDYVTK 100
pleD PRK09581
response regulator PleD; Reviewed
647-748 1.05e-13

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 74.17  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLT-VRELERKLLLgRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:PRK09581   4 RILVVDDIPAnVKLLEAKLLA-EYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMV 82
                         90       100
                 ....*....|....*....|...
gi 15598899  726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK09581  83 TALDDPEDRVRGLEAGADDFLTK 105
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
648-748 1.33e-13

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: 67.72  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVSY 727
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17623  78 RGDDIDRILGLELGADDYLPK 98
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
647-748 1.47e-13

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 67.49  E-value: 1.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVS 726
Cdd:cd17626   2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES---GVPIVMLT 78
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17626  79 AKSDTVDVVLGLESGADDYVAK 100
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
647-748 1.60e-13

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 74.62  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDsltvRELERKLL---LGR-GYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPV 722
Cdd:PRK10841 803 MILVVDD----HPINRRLLadqLGSlGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLG--LTLPV 876
                         90       100
                 ....*....|....*....|....*.
gi 15598899  723 MVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10841 877 IGVTANALAEEKQRCLEAGMDSCLSK 902
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
647-760 1.77e-13

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: 67.80  E-value: 1.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGY--DVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIElvtLVRRDSRLQSLPVMV 724
Cdd:cd17541   2 RVLIVDDSAVMRKLLSRILESDPDieVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLE---ALRRIMAERPTPVVM 78
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598899 725 VSYKDREEDRR--RGLDAGADYYLAKASFHDEALLDAV 760
Cdd:cd17541  79 VSSLTEEGAEItlEALELGAVDFIAKPSGGISLDLEEI 116
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
648-748 2.10e-13

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: 66.70  E-value: 2.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVSY 727
Cdd:cd19936   1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS---TLPVIFLTS 77
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd19936  78 KDDEIDEVFGLRMGADDYITK 98
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
487-617 3.45e-13

CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. Activated by the chemotaxis receptor a histidine phosphoryl group from CheA is passed directly to an aspartate in the response regulator CheY. This signalling mechanism is modulated by the methyl accepting chemotaxis proteins (MCPs). MCPs form a highly interconnected, tightly packed array within the membrane that is organized, at least in part, through interactions with CheW and CheA. The CheA regulatory domain belongs to the family of CheW_like proteins and has been proposed to mediate interaction with the kinase regulator CheW.


Pssm-ID: 238373 [Multi-domain]  Cd Length: 132  Bit Score: 67.20  E-value: 3.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 487 LSVVRSLVVEIGEEAYAFPLAHIERMCELEAEEIVQLEGRQHFW-YEGRHVGLVSAAQLLQRPESSRTEGAIPVVVVRDR 565
Cdd:cd00731   1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGGKEVInVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRTG 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15598899 566 DAVYGVAVERFVGERTLVVMPLDPRLGKVRDVSAGALLDDGSPVLILDVEDL 617
Cdd:cd00731  81 GRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
648-748 5.35e-13

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: 66.11  E-value: 5.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRS--EHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVV 725
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLREnkDEFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                        90       100
                ....*....|....*....|...
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17584  78 SADGSTSTVMKGLAHGACDYLLK 100
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
648-748 6.26e-13

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: 65.91  E-value: 6.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVSY 727
Cdd:cd17614   1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS---NVPIIMLTA 77
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17614  78 KDSEVDKVLGLELGADDYVTK 98
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
648-748 6.76e-13

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: 65.55  E-value: 6.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVS- 726
Cdd:cd17594   2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS---DVPIIIISg 78
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17594  79 DRRDEIDRVVGLELGADDYLAK 100
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
305-486 1.52e-12

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 68.01  E-value: 1.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 305 ADVLSGQARMVRDLGRSLGKQVRLLVEGESTQV--DRDVLEKLeapLTHLLRNAVDHGieapetrlaagkPAEGRITIRA 382
Cdd:COG2205  94 AELLEEAVEELRPLAEEKGIRLELDLPPELPLVyaDPELLEQV---LANLLDNAIKYS------------PPGGTITISA 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 383 RHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlseEELLAFLFLPgFSMREQVTEVSGRGVGLDAVQHMVRQ 462
Cdd:COG2205 159 RREGDGVRISVSDNGPGIP------------------------EEELERIFER-FYRGDNSRGEGGTGLGLAIVKRIVEA 213
                       170       180
                ....*....|....*....|....
gi 15598899 463 LRGGVRMEQRQGQGALFHVEVPLT 486
Cdd:COG2205 214 HGGTIWVESEPGGGTTFTVTLPLA 237
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
644-748 1.76e-12

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 71.30  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   644 QRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVM 723
Cdd:PRK09959  957 EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPIW 1034
                          90       100
                  ....*....|....*....|....*
gi 15598899   724 VVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK09959 1035 GLTANAQANEREKGLSCGMNLCLFK 1059
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
12-101 1.89e-12

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 63.81  E-value: 1.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899     12 LELFRLEAEAQTQVLNAGLMALERSPTQADqLEACMRAAHSLKGAARIVGLDAGVRVAHVMEDCLVEAQDGRLLLQSEHI 91
Cdd:smart00073   3 LELFREELAEFLQSLEEGLLELEKALDAQD-VNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDLL 81
                           90
                   ....*....|
gi 15598899     92 DALLQGCDLL 101
Cdd:smart00073  82 DLLLELVDVL 91
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
647-748 2.15e-12

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: 64.33  E-value: 2.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqsLPVMVVS 726
Cdd:cd17619   2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE---VGIILVT 78
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17619  79 GRDDEVDRIVGLEIGADDYVTK 100
ompR PRK09468
osmolarity response regulator; Provisional
642-748 2.19e-12

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 67.69  E-value: 2.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  642 GAQRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDG--MDgwNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQS 719
Cdd:PRK09468   2 MQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAeqMD--RLLTRESFHLMVLDLMLPGEDGLSICRRLRSQN--NP 77
                         90       100
                 ....*....|....*....|....*....
gi 15598899  720 LPVMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK09468  78 TPIIMLTAKGEEVDRIVGLEIGADDYLPK 106
PRK10643 PRK10643
two-component system response regulator PmrA;
647-769 2.34e-12

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 66.98  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMVVS 726
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKK--YTLPVLILT 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 15598899  727 YKDREEDRRRGLDAGADYYLAKaSFHDEALLDAVVVLIGEAQG 769
Cdd:PRK10643  80 ARDTLEDRVAGLDVGADDYLVK-PFALEELHARIRALIRRHQG 121
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
646-760 2.36e-12

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: 64.22  E-value: 2.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDVAV-AVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMV 724
Cdd:cd17542   1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKID--PNAKVIM 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598899 725 VSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:cd17542  79 CSAMGQEEMVKEAIKAGAKDFIVK-PFQPERVLEAV 113
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
647-748 2.75e-12

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 63.93  E-value: 2.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVS 726
Cdd:cd19939   1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS---HVPILMLT 77
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd19939  78 ARTEEMDRVLGLEMGADDYLCK 99
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
646-700 5.52e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.05  E-value: 5.52e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15598899    646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMP 700
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
647-748 8.50e-12

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: 62.40  E-value: 8.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVS 726
Cdd:cd19938   1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVT 77
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd19938  78 ARVEEIDRLLGLELGADDYICK 99
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
648-748 1.90e-11

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 61.23  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVSY 727
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17602  81 KDGLVDRIRAKMAGASGYLTK 101
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
646-742 2.87e-11

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 61.41  E-value: 2.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLL-LGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMV 724
Cdd:cd17552   2 KRILVIDDEEDIREVVQACLeKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVIL 81
                        90
                ....*....|....*...
gi 15598899 725 VSYKDREEDRRRGLDAGA 742
Cdd:cd17552  82 LTAKAQPSDRQRFASLGV 99
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
346-486 3.05e-11

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 60.84  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   346 EAPLTHLLRNAVDHGIEApetrlaAGKPAEGRITIrarHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlse 425
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKH------AAKAGEITVTL---SEGGELTLTVEDNGIGIP------------------------ 49
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598899   426 EELLAFLFLPGFsmREQVTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPLT 486
Cdd:pfam02518  50 PEDLPRIFEPFS--TADKRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
647-768 3.54e-11

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: 63.05  E-value: 3.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDV-AVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqsLPVMVV 725
Cdd:COG3707   5 RVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APVILL 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAKAsFHDEALLDAVVVLIGEAQ 768
Cdd:COG3707  82 TAYSDPELIERALEAGVSAYLVKP-LDPEDLLPALELALARFR 123
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
647-757 4.86e-11

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 63.28  E-value: 4.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEhFDLLITDIDMPRMDGIELVTLVRRDsrlQSLPVMVVS 726
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS-IDLLLLDVMMPKKNGIDTLKELRQT---HQTPVIMLT 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 15598899  727 YKDREEDRRRGLDAGADYYLAKaSFHDEALL 757
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPK-PFNDRELV 108
PRK11517 PRK11517
DNA-binding response regulator HprR;
647-748 6.95e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 62.61  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRrdsRLQSLPVMVVS 726
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR---TAKQTPVICLT 78
                         90       100
                 ....*....|....*....|..
gi 15598899  727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK11517  79 ARDSVDDRVRGLDSGANDYLVK 100
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
304-486 7.53e-11

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 64.16  E-value: 7.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 304 FADVLSGQARMVRDLGRSLGKQVRLLVEGESTQV--DRDVLEKLeapLTHLLRNAVDHGieapetrlaagkPAEGRITIR 381
Cdd:COG0642 184 LAELLEEVVELFRPLAEEKGIELELDLPDDLPTVrgDPDRLRQV---LLNLLSNAIKYT------------PEGGTVTVS 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 382 ARHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlseEELLAFLFLPGFSMREQvTEVSGRGVGLDAVQHMVR 461
Cdd:COG0642 249 VRREGDRVRISVEDTGPGIP------------------------PEDLERIFEPFFRTDPS-RRGGGTGLGLAIVKRIVE 303
                       170       180
                ....*....|....*....|....*
gi 15598899 462 QLRGGVRMEQRQGQGALFHVEVPLT 486
Cdd:COG0642 304 LHGGTIEVESEPGKGTTFTVTLPLA 328
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
648-726 1.26e-10

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: 59.05  E-value: 1.26e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqSLPVMVVS 726
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYP--DLPVIMIS 77
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
646-712 2.10e-10

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: 58.57  E-value: 2.10e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVR 712
Cdd:cd17569   1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVR 67
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
646-748 2.17e-10

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 61.66  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:PRK10161   3 RRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVML 82
                         90       100
                 ....*....|....*....|...
gi 15598899  726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10161  83 TARGEEEDRVRGLETGADDYITK 105
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
646-748 2.31e-10

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 58.70  E-value: 2.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLlGRGYDVAV--AVDGMDGWNALRSEHFDLLITDIDMPRMDGIElvTLVRRDSRLQSLPVM 723
Cdd:cd17593   1 MKVLICDDSSMARKQLARAL-PADWDVEItfAENGEEALEILREGRIDVLFLDLTMPVMDGYE--VLEALPVEQLETKVI 77
                        90       100
                ....*....|....*....|....*
gi 15598899 724 VVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17593  78 VVSGDVQPEAKERVLELGALAFLKK 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
648-748 2.50e-10

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: 58.18  E-value: 2.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSE--HFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEqnEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                        90       100
                ....*....|....*....|...
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17582  81 SSQDSVGVVFKCLSKGAADYLVK 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
349-485 2.86e-10

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 62.94  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 349 LTHLLRNAVDHGIEApetrLAAGKPAEGRITIRARHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlseEEL 428
Cdd:COG3290 282 LVTILGNLLDNAIEA----VEKLPEEERRVELSIRDDGDELVIEVEDSGPGIP------------------------EEL 333
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598899 429 LAFLFLPGFSMREQvtevSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPL 485
Cdd:COG3290 334 LEKIFERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPK 386
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
648-748 5.99e-10

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: 56.82  E-value: 5.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVSY 727
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS---NVPVIMVTA 77
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17621  78 KDSEIDKVVGLELGADDYVTK 98
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
493-617 8.83e-10

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 57.21  E-value: 8.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   493 LVVEIGEEAYAFPLAHIERMceLEAEEIVQLEGRQHF-----WYEGRHVGLVSAAQLLQRPESSRTEgAIPVVVVRDRDA 567
Cdd:pfam01584   2 LLFRLGGETFAIPISKVREI--LRPPPITPIPGAPGYvlgviNLRGEVLPVIDLRRLLGLPPTEPRE-RTRVVVVEVGGQ 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15598899   568 VYGVAVERFVGERTLVVMPLDPRLGKVRD---VSAGALLDDGSPVLILDVEDL 617
Cdd:pfam01584  79 VVGLLVDEVIGVLEIVIKQIEPPLGLGRVagyISGATILGDGRVVLILDVEAL 131
PRK15347 PRK15347
two component system sensor kinase;
647-748 3.65e-09

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 60.43  E-value: 3.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV- 725
Cdd:PRK15347 692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMIVa 771
                         90       100
                 ....*....|....*....|....
gi 15598899  726 -SYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK15347 772 lTANAAPEEIHRCKKAGMNHYLTK 795
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
648-748 4.02e-09

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 57.51  E-value: 4.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVSY 727
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWS---AIPVIVLSA 80
                         90       100
                 ....*....|....*....|.
gi 15598899  728 KDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10529  81 RSEESDKIAALDAGADDYLSK 101
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
647-748 4.05e-09

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 57.63  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRrdSRLQSLPVMVVS 726
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLR--SANKGMPILLLT 79
                         90       100
                 ....*....|....*....|..
gi 15598899  727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK09836  80 ALGTIEHRVKGLELGADDYLVK 101
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
648-748 8.45e-09

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: 54.29  E-value: 8.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVaVAVDgmDGWNAL--------------RSEHFDLLITDIDMPRMDGIELVTLVRR 713
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRV-TAVD--SGKRALeflgledeedssnfNEPKVNMIITDYCMPGMTGYDLLKKVKE 77
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598899 714 DSRLQSLPVMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17581  78 SSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLK 112
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
11-103 9.98e-09

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 52.74  E-value: 9.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899    11 LLELFRLEAEAQTQVLNAGLmalersptQADQLEACMRAAHSLKGAARIVGLDAGVRVAHVMEDCLveaQDGRLLLQSEH 90
Cdd:pfam01627   2 LLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGELPLDPEL 70
                          90
                  ....*....|...
gi 15598899    91 IDALLQGCDLLLR 103
Cdd:pfam01627  71 LEALRDLLEALRA 83
PRK11173 PRK11173
two-component response regulator; Provisional
644-748 1.08e-08

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 56.56  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  644 QRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIelvtLVRRDSRLQ-SLPV 722
Cdd:PRK11173   2 QTPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGL----LLARELREQaNVAL 77
                         90       100
                 ....*....|....*....|....*.
gi 15598899  723 MVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK11173  78 MFLTGRDNEVDKILGLEIGADDYITK 103
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
648-748 1.46e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 57.73  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIElvTLVRRDSRLQSLPVMVVSY 727
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIA--TLKEIKALNPAIPVLIMTA 85
                         90       100
                 ....*....|....*....|.
gi 15598899  728 KDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10365  86 YSSVETAVEALKTGALDYLIK 106
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
647-748 1.50e-08

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 53.00  E-value: 1.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLT-VRELERKLLLGRGYDV-AVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMV 724
Cdd:cd17561   3 KVLIADDNREfVQLLEEYLNSQPDMEVvGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIM 82
                        90       100
                ....*....|....*....|....
gi 15598899 725 VSYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17561  83 LTAFGQEDITQRAVELGASYYILK 106
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
647-748 1.67e-08

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 56.34  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899   647 RILVVDDSltvRE----LERKLLLGRGYDVA-VAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLP 721
Cdd:TIGR02875   4 RIVIADDN---KEfcnlLKEYLAAQPDMEVVgVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARPR 80
                          90       100
                  ....*....|....*....|....*..
gi 15598899   722 VMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:TIGR02875  81 VIMLSAFGQEKITQRAVALGADYYVLK 107
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
111-486 1.73e-08

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 57.12  E-value: 1.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 111 DAGWAEGAGREEIDGLVLRLEGLVRSGLPLARAELPATTPGLPEAVPEAPPAASAAASDDNDEEPAGQAGGEQAEERRSR 190
Cdd:COG4191   9 LLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 191 VLRVTAERLDRLLDISSKSLVE--FQRIKPLADSLQRLRRLQSSASRA---------------------------LDVVR 241
Cdd:COG4191  89 LLEALLLLLLAALDAEENAELEelERDITELERAEEELRELQEQLVQSeklaalgelaagiaheinnplaailgnAELLR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 242 ETVQETALDPQAQAMLGEARQLIGECQQMlvqhIADLDEFAWQGGQRAQVLydaalasrmrPFADVLSGQARMVRDLGRS 321
Cdd:COG4191 169 RRLEDEPDPEELREALERILEGAERAAEI----VRSLRAFSRRDEEEREPV----------DLNELIDEALELLRPRLKA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 322 LGKQVRLLVEGESTQV--DRDVLEKLeapLTHLLRNAVDhgieapetrlAAGKPAEGRITIRARHHAGMLVLELSDDGGG 399
Cdd:COG4191 235 RGIEVELDLPPDLPPVlgDPGQLEQV---LLNLLINAID----------AMEEGEGGRITISTRREGDYVVISVRDNGPG 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 400 IDlqrlretvlnrqfataetvaqlseEELLAFLFLPGFSMREqvtEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALF 479
Cdd:COG4191 302 IP------------------------PEVLERIFEPFFTTKP---VGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTF 354

                ....*..
gi 15598899 480 HVEVPLT 486
Cdd:COG4191 355 TITLPLA 361
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
646-756 2.50e-08

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: 52.66  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMVV 725
Cdd:cd19919   1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ--RHPDLPVIIM 78
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598899 726 S-YKDreedrrrgLDA-------GADYYLAKASFHDEAL 756
Cdd:cd19919  79 TaHSD--------LDSavsayqgGAFEYLPKPFDIDEAV 109
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
647-713 4.23e-08

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 51.73  E-value: 4.23e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEH-FDLLITDIDMPRMDGIELVTLVRR 713
Cdd:cd18160   1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARK 68
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
647-760 4.41e-08

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 54.82  E-value: 4.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLlgRGYD----VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRlqslPV 722
Cdd:COG3279   3 KILIVDDEPLARERLERLL--EKYPdlevVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDP----PP 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15598899 723 MVV---SYKDREEDrrrGLDAGADYYLAKAsFHDEALLDAV 760
Cdd:COG3279  77 PIIfttAYDEYALE---AFEVNAVDYLLKP-IDEERLAKAL 113
PRK10766 PRK10766
two-component system response regulator TorR;
646-748 5.59e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 54.27  E-value: 5.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVtlvrRDSRLQS-LPVMV 724
Cdd:PRK10766   3 YHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLT----RELRSRStVGIIL 78
                         90       100
                 ....*....|....*....|....
gi 15598899  725 VSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10766  79 VTGRTDSIDRIVGLEMGADDYVTK 102
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
648-748 5.88e-08

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: 51.00  E-value: 5.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVrrDSRLQSLPVMVVSY 727
Cdd:cd19926   1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHI--QQRLPQTPVAVITA 78
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd19926  79 YGSLDTAIEALKAGAFDFLTK 99
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
648-757 7.35e-08

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: 51.13  E-value: 7.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVSY 727
Cdd:cd18159   1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQIS---NVPIIFISS 77
                        90       100       110
                ....*....|....*....|....*....|
gi 15598899 728 KDREEDRRRGLDAGADYYLAKaSFHDEALL 757
Cdd:cd18159  78 RDDNMDQVMAINMGGDDYITK-PFDLDVLL 106
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
355-484 9.95e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 50.75  E-value: 9.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 355 NAVDHGIEApetrLAAGKPAEGRITIRARHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlseEELLAFLFL 434
Cdd:cd16915   7 NLIDNALDA----LAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIA------------------------PELRDKVFE 58
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15598899 435 PGFSMREQvtevSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVP 484
Cdd:cd16915  59 RGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
PRK10336 PRK10336
two-component system response regulator QseB;
647-748 1.04e-07

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 53.36  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQslPVMVVS 726
Cdd:PRK10336   2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQRE--PVLILT 79
                         90       100
                 ....*....|....*....|..
gi 15598899  727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10336  80 ARDALAERVEGLRLGADDYLCK 101
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
322-484 1.85e-07

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 54.53  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  322 LGKQVRLLVEGESTQVDRDVL------EKLEAPLTHLLRNAVDHGIEApetrlAAGKPaEGRITIRARHHAGMLVLELSD 395
Cdd:PRK11086 401 LGKISRARELGITLIISEDSQlpdsgdEDQVHELITILGNLIENALEA-----VGGEE-GGEISVSLHYRNGWLHCEVSD 474
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  396 DGGGIDlqrlretvlnrqfataetvaqlseEELLAFLFLPGFSmreqvTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQ 475
Cdd:PRK11086 475 DGPGIA------------------------PDEIDAIFDKGYS-----TKGSNRGVGLYLVKQSVENLGGSIAVESEPGV 525

                 ....*....
gi 15598899  476 GALFHVEVP 484
Cdd:PRK11086 526 GTQFFVQIP 534
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
352-486 2.25e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 53.87  E-value: 2.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 352 LLRNAVDHGIEApetrlaagKPAEGRITIRARHHAGMLVLELSDDGGGIDLQRLREtvLNRQFATAEtvaqlseeellaf 431
Cdd:COG2972 344 LVENAIEHGIEP--------KEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEK--LLEELSSKG------------- 400
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598899 432 lflpgfsmreqvtevSGRGVGLDAVQHMVRQLRG---GVRMEQRQGQGALFHVEVPLT 486
Cdd:COG2972 401 ---------------EGRGIGLRNVRERLKLYYGeeyGLEIESEPGEGTTVTIRIPLE 443
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
648-757 2.87e-07

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 49.72  E-value: 2.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERkLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIElVTLVRRDSRLQSlPVMVVSY 727
Cdd:cd17616   2 LLIEDDSATAQSIEL-MLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYE-VLRTLRLAKVKT-PILILSG 78
                        90       100       110
                ....*....|....*....|....*....|
gi 15598899 728 KDREEDRRRGLDAGADYYLAKaSFHDEALL 757
Cdd:cd17616  79 LADIEDKVKGLGFGADDYMTK-PFHKDELV 107
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
643-748 3.21e-07

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: 51.07  E-value: 3.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 643 AQRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPV 722
Cdd:COG4567   2 AEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE--RDPDARI 79
                        90       100
                ....*....|....*....|....*.
gi 15598899 723 MVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:COG4567  80 VVLTGYASIATAVEAIKLGADDYLAK 105
PLN03029 PLN03029
type-a response regulator protein; Provisional
648-748 3.90e-07

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 51.57  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGW--------------------NALRSEHFDLLITDIDMPRMDGIEL 707
Cdd:PLN03029  11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALkflglheddrsnpdtpsvspNSHQEVEVNLIITDYCMPGMTGYDL 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15598899  708 VTLVRRDSRLQSLPVMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PLN03029  91 LKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLK 131
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
647-726 5.92e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 52.46  E-value: 5.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLlgrGYD-----VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIelvTLVRRDSRLQSLP 721
Cdd:PRK00742   5 RVLVVDDSAFMRRLISEIL---NSDpdievVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGL---DALEKIMRLRPTP 78

                 ....*
gi 15598899  722 VMVVS 726
Cdd:PRK00742  79 VVMVS 83
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
672-760 6.93e-07

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: 48.42  E-value: 6.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 672 VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVrRDSRLQSLPVMVVSYKdREEDRRRGLDAGADYYLAKASF 751
Cdd:cd19930  27 VAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAEL-REELPDTKVLIVTTFG-RPGYFRRALAAGVDGYVLKDRP 104

                ....*....
gi 15598899 752 HDEaLLDAV 760
Cdd:cd19930 105 IEE-LADAI 112
PRK10693 PRK10693
two-component system response regulator RssB;
673-748 7.74e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 51.53  E-value: 7.74e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598899  673 AVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRrdSRLQSLPVMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10693   1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLR--NRGDQTPVLVISATENMADIAKALRLGVQDVLLK 74
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
646-760 8.43e-07

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: 48.56  E-value: 8.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDV-AVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRrdSRLQSLPVMV 724
Cdd:cd19932   1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT--SENIAPIVLL 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598899 725 VSYKDREEDRRRGlDAGADYYLAKaSFHDEALLDAV 760
Cdd:cd19932  79 TAYSQQDLVERAK-EAGAMAYLVK-PFSESDLIPAI 112
PRK13557 PRK13557
histidine kinase; Provisional
635-713 8.54e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 52.37  E-value: 8.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  635 RSRRQAGgaqRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSE-HFDLLITDIDMP-RMDGIELVTLVR 712
Cdd:PRK13557 408 RAIDRGG---TETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMPgGMNGVMLAREAR 484

                 .
gi 15598899  713 R 713
Cdd:PRK13557 485 R 485
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
647-708 8.66e-07

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 48.73  E-value: 8.66e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598899 647 RILVVDDSLTVRE-LERKLLLGRGYDV-AVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELV 708
Cdd:COG2197   3 RVLIVDDHPLVREgLRALLEAEPDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEAL 66
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
349-486 9.24e-07

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 51.89  E-value: 9.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 349 LTHLLRNAVDHGieapetrlaagkPAEGRITIRARHHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlseEEL 428
Cdd:COG5000 322 LINLLKNAIEAI------------EEGGEIEVSTRREDGRVRIEVSDNGPGIP------------------------EEV 365
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598899 429 LAFLFLPGFSMREqvtevSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPLT 486
Cdd:COG5000 366 LERIFEPFFTTKP-----KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
643-748 1.04e-06

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 50.35  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  643 AQRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPV 722
Cdd:PRK11083   1 MQQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLA--FHPALPV 78
                         90       100
                 ....*....|....*....|....*.
gi 15598899  723 MVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK11083  79 IFLTARSDEVDRLVGLEIGADDYVAK 104
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
643-748 1.10e-06

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 51.77  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  643 AQRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRrdSRLQSLPV 722
Cdd:PRK11361   2 TAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMR--SHETRTPV 79
                         90       100
                 ....*....|....*....|....*.
gi 15598899  723 MVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK11361  80 ILMTAYAEVETAVEALRCGAFDYVIK 105
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
647-748 1.38e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 50.07  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVS 726
Cdd:PRK10710  12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS---DIPIVMVT 88
                         90       100
                 ....*....|....*....|..
gi 15598899  727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK10710  89 AKIEEIDRLLGLEIGADDYICK 110
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
648-725 1.50e-06

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: 47.58  E-value: 1.50e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsrlQSLPVMVV 725
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQE----RSLPTSVI 74
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
646-760 1.53e-06

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: 47.40  E-value: 1.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDV-AVAVDGMDGWNALRSEHFDLLITDIDMP-RMDGIELVTLVRrdsRLQSLPVM 723
Cdd:cd17534   1 KKILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIR---EKFDIPVI 77
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598899 724 -VVSYKDrEEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:cd17534  78 fLTAYSD-EETLERAKETNPYGYLVK-PFNERELKAAI 113
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
648-748 1.86e-06

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: 46.73  E-value: 1.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMVVSY 727
Cdd:cd19928   1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKK--ARPDLPIIVMSA 78
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd19928  79 QNTLMTAVKAAERGAFEYLPK 99
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
647-760 2.04e-06

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 51.39  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVS 726
Cdd:PRK11107 669 TVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVT 748
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598899  727 YKDREEDRRRGLDAGADYYLAKASfhDEALLDAV 760
Cdd:PRK11107 749 AHAMAGERERLLSAGMDDYLAKPI--DEAMLKQV 780
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
648-748 2.20e-06

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: 47.04  E-value: 2.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMVVSY 727
Cdd:cd17573   1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKH--PSIVVIVLSD 78
                        90       100
                ....*....|....*....|.
gi 15598899 728 KDREEDRRRGLDAGADYYLAK 748
Cdd:cd17573  79 NPKTEQEIEAFKEGADDYIAK 99
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
349-486 2.43e-06

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 50.23  E-value: 2.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 349 LTHLLRNAVDHGieapetrlaagkPAEGRITIRAR----------HHAGMLVLELSDDGGGIDlqrlretvlnrqfatae 418
Cdd:COG3852 249 LLNLVRNAAEAM------------PEGGTITIRTRverqvtlgglRPRLYVRIEVIDNGPGIP----------------- 299
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598899 419 tvaqlseEELLAFLFLPGFSMREQvtevsGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPLT 486
Cdd:COG3852 300 -------EEILDRIFEPFFTTKEK-----GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
647-760 3.31e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 48.70  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLL-LGRGYDV-AVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMV 724
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLeLDPGFEVvAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILT 87
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15598899  725 VSykDREEDRRRGLDAGADYYLAKASfHDEALLDAV 760
Cdd:PRK10403  88 VS--DASSDVFALIDAGADGYLLKDS-DPEVLLEAI 120
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
349-485 3.64e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 46.26  E-value: 3.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 349 LTHLLRNAVdHGIEApetrlaagkpaEGRITIRARHHAGMLVLELSDDGGGIDLqrlretvlnrqfataetvaqlseeEL 428
Cdd:cd16943   8 LLNLLVNAA-QAMEG-----------RGRITIRTWAHVDQVLIEVEDTGSGIDP------------------------EI 51
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598899 429 LAFLFLPGFSMREQVTevsGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPL 485
Cdd:cd16943  52 LGRIFDPFFTTKPVGE---GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
PRK15369 PRK15369
two component system response regulator;
647-750 4.84e-06

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 48.15  E-value: 4.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDD-SLTVRELERKLLLGRGYDVAVAV-DGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMV 724
Cdd:PRK15369   5 KILLVDDhELIINGIKNMLAPYPRYKIVGQVdNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQ--RWPAMNILV 82
                         90       100
                 ....*....|....*....|....*.
gi 15598899  725 VSYKDREEDRRRGLDAGADYYLAKAS 750
Cdd:PRK15369  83 LTARQEEHMASRTLAAGALGYVLKKS 108
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
647-748 9.38e-06

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 49.17  E-value: 9.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDD-SLTVrELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:PRK11091 527 NILLVEDiELNV-IVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVA 605
                         90       100
                 ....*....|....*....|...
gi 15598899  726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK11091 606 LTANVLKDKKEYLDAGMDDVLSK 628
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
648-760 9.74e-06

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: 47.02  E-value: 9.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELV-TLVRRDSRlqsLPVMVVS 726
Cdd:COG4566   2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQeELAARGSP---LPVIFLT 78
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598899 727 YKDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:COG4566  79 GHGDVPMAVRAMKAGAVDFLEK-PFDDQALLDAV 111
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
647-748 1.29e-05

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: 45.06  E-value: 1.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlqSLPVMVVS 726
Cdd:cd17622   2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY---QGPILLLT 78
                        90       100
                ....*....|....*....|..
gi 15598899 727 YKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17622  79 ALDSDIDHILGLELGADDYVVK 100
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
647-760 1.41e-05

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 46.95  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLL-LGRGYD-VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIElvTLVR-RDSRLQSlPVM 723
Cdd:PRK10651   8 TILLIDDHPMLRTGVKQLIsMAPDITvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLE--TLDKlREKSLSG-RIV 84
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15598899  724 VVSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:PRK10651  85 VFSVSNHEEDVVTALKRGADGYLLK-DMEPEDLLKAL 120
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
646-760 1.63e-05

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: 44.85  E-value: 1.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSrlQSLPVMVV 725
Cdd:cd17553   1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVID--ENIRVIIM 78
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:cd17553  79 TAYGELDMIQESKELGALTHFAK-PFDIDEIRDAV 112
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
649-748 2.48e-05

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 46.04  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  649 LVVDDSLTVRELERKLLLGRGYDVAVAV-DGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMVVSY 727
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILAELtEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRK--RQYSGIIIIVSA 81
                         90       100
                 ....*....|....*....|.
gi 15598899  728 KDREEDRRRGLDAGADYYLAK 748
Cdd:PRK09958  82 KNDHFYGKHCADAGANGFVSK 102
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
647-748 3.34e-05

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 43.93  E-value: 3.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEH--FDLLITDIDMPRMDGIELVTLVR--RDSRLQSLPV 722
Cdd:cd19933   2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRklFGRRERPLIV 81
                        90       100
                ....*....|....*....|....*.
gi 15598899 723 MVVSYKDREEdRRRGLDAGADYYLAK 748
Cdd:cd19933  82 ALTANTDDST-REKCLSLGMNGVITK 106
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
647-740 3.40e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.80  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGR-GYDVA-VAVDGMDGWNALRSEHFDLLITDIDMPRMDGIElvtLVRRDSRLQSLPVMV 724
Cdd:PRK12555   2 RIGIVNDSPLAVEALRRALARDpDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVE---ATRRIMAERPCPILI 78
                         90
                 ....*....|....*.
gi 15598899  725 VSyKDREEDRRRGLDA 740
Cdd:PRK12555  79 VT-SLTERNASRVFEA 93
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
648-743 3.95e-05

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 43.10  E-value: 3.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSE-HFDLLITDIDMPR-MDGIELVTLVRRdsRLQSLPVMVV 725
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARR--RRPDLKVLLT 78
                        90
                ....*....|....*...
gi 15598899 726 SYKDREEDRRRGLDAGAD 743
Cdd:cd18161  79 SGYAENAIEGGDLAPGVD 96
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
646-748 4.02e-05

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: 43.20  E-value: 4.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 646 KRILVVDDSLTVRE-----LERklllgRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRR---DSRL 717
Cdd:cd17563   1 KSLLLVDDDEVFAErlaraLER-----RGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAlqpDARI 75
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15598899 718 ------QSLPVMVVSYKDreedrrrgldaGADYYLAK 748
Cdd:cd17563  76 vvltgyASIATAVEAIKL-----------GADDYLAK 101
PRK10816 PRK10816
two-component system response regulator PhoP;
647-754 4.91e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 45.50  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIelvTLVRR-DSRLQSLPVMVV 725
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGL---SLIRRwRSNDVSLPILVL 78
                         90       100
                 ....*....|....*....|....*....
gi 15598899  726 SYKDREEDRRRGLDAGADYYLAKaSFHDE 754
Cdd:PRK10816  79 TARESWQDKVEVLSAGADDYVTK-PFHIE 106
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
644-756 5.61e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 46.40  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  644 QRKRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVM 723
Cdd:PRK10923   2 QRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVI 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 15598899  724 VVSYKDREEDRRRGLDAGADYYLAKASFHDEAL 756
Cdd:PRK10923  80 IMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAV 112
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
648-760 5.99e-05

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: 42.97  E-value: 5.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELV-TLVRRDSrlqSLPV---- 722
Cdd:cd17537   3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQdELLARGS---NIPIifit 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15598899 723 ------MVVsykdreedrrRGLDAGADYYLAKaSFHDEALLDAV 760
Cdd:cd17537  80 ghgdvpMAV----------EAMKAGAVDFLEK-PFRDQVLLDAI 112
PRK13856 PRK13856
two-component response regulator VirG; Provisional
646-748 6.12e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 45.19  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  646 KRILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIElvtLVRRDSRLQSLPVMVV 725
Cdd:PRK13856   2 KHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLE---IVRSLATKSDVPIIII 78
                         90       100
                 ....*....|....*....|....
gi 15598899  726 SYKDREE-DRRRGLDAGADYYLAK 748
Cdd:PRK13856  79 SGDRLEEaDKVVALELGATDFIAK 102
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
304-485 7.73e-05

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 45.70  E-value: 7.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 304 FADVLSGQARMVRDLGRSLGKQVRLLVEGESTQV--DRDVLEKLeapLTHLLRNAVDHGieapetrlaagkPAEGRITIR 381
Cdd:COG5002 242 LAELLEEVVEELRPLAEEKGIELELDLPEDPLLVlgDPDRLEQV---LTNLLDNAIKYT------------PEGGTITVS 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 382 ARHHAGMLVLELSDDGGGI---DLQRLREtvlnrQFATAEtvaqlseeellaflflpgfsmREQVTEVSGRGVGLDAVQH 458
Cdd:COG5002 307 LREEDDQVRISVRDTGIGIpeeDLPRIFE-----RFYRVD---------------------KSRSRETGGTGLGLAIVKH 360
                       170       180
                ....*....|....*....|....*..
gi 15598899 459 MVRQLRGGVRMEQRQGQGALFHVEVPL 485
Cdd:COG5002 361 IVEAHGGRIWVESEPGKGTTFTITLPL 387
PRK15115 PRK15115
response regulator GlrR; Provisional
647-726 9.99e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 45.60  E-value: 9.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  647 RILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMVVS 726
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQK--VQPGMPVIILT 84
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
345-483 1.13e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 42.06  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 345 LEAPLTHLLRNAVDhgieapetrlAAGKPAEGRITIRARHHAGMLVLELSDDGGGIdlqrlretvlnrqfataetvaqls 424
Cdd:cd16976   1 IQQVLMNLLQNALD----------AMGKVENPRIRIAARRLGGRLVLVVRDNGPGI------------------------ 46
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598899 425 EEELLAFLFLPGFSMREqvtevSGRGVGLD-AVQHMVRQLRGG-VRMEQRQGQGALFHVEV 483
Cdd:cd16976  47 AEEHLSRVFDPFFTTKP-----VGKGTGLGlSISYGIVEEHGGrLSVANEEGAGARFTFDL 102
CheW smart00260
Two component signalling adaptor domain;
484-618 1.59e-04

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 42.23  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899    484 PLTLSVvrslvveIGEEAYAFPLAHIERMceLEAEEIVQLEGRQHFW-----YEGRHVGLVSAAQLLQrPESSRTEGAIP 558
Cdd:smart00260   5 PLTFAI-------GKDETYAIPIAAVREI--LRPPPITPIPGAPGYVlgvinLRGEVLPVVDLRRLLG-LPPEPPTDETR 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598899    559 VVVVRDRDAVYGVAVERFVGERTLVVMPLDPR----LGKVRDVSAGALLDDGSPVLILDVEDLL 618
Cdd:smart00260  75 VIVVETGDRKVGLVVDSVLGVREVVVKSIEPPppvsLSNAPGISGATILGDGRVVLILDVDKLL 138
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
648-726 1.78e-04

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: 42.09  E-value: 1.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVR-RDSrlqSLPVMVVS 726
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIReLDP---DLPVILIT 77
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
647-759 2.29e-04

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: 41.46  E-value: 2.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLG-RGYDV-AVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMV 724
Cdd:cd19925   2 NVLIVEDDPMVAEIHRAYVEQvPGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA--AGHDVDVIV 79
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598899 725 VSYKDREEDRRRGLDAGADYYLAKaSFHDEALLDA 759
Cdd:cd19925  80 VTAANDVETVREALRLGVVDYLIK-PFTFERLRQR 113
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
647-760 2.71e-04

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: 41.58  E-value: 2.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLlGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRdsRLQSLPVMVVS 726
Cdd:cd17596   2 TILVVDDEVRSLEALRRTL-EEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRE--RWPEVVRIIIS 78
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598899 727 YKDREEDRRRGL-DAGADYYLAKaSFHDEALLDAV 760
Cdd:cd17596  79 GYTDSEDIIAGInEAGIYQYLTK-PWHPDQLLLTV 112
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
648-748 3.67e-04

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: 40.79  E-value: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLL-LGRGYDV-AVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:cd19931   1 VLLIDDHPLLRKGIKQLIeLDPDFTVvGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                        90       100
                ....*....|....*....|...
gi 15598899 726 SykDREEDRRRGLDAGADYYLAK 748
Cdd:cd19931  81 S--DAEDDVVTALRAGADGYLLK 101
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
352-401 6.41e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain.


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 39.73  E-value: 6.41e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15598899 352 LLRNAVDHGIEapetrlaaGKPAEGRITIRARHHAGMLVLELSDDGGGID 401
Cdd:cd16956   9 IVENAVKHGLS--------GLLDGGRVEITARLDGQHLLLEVEDNGGGMD 50
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
276-769 7.17e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 43.32  E-value: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  276 ADLDEFAWQGGQRAQVLYDAALASRMRPFADVLSGQARMVRDLGRSLGKQVRLLVEGESTQVDRDVLEKLEAPLTHLLRN 355
Cdd:COG3321  861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  356 AVDHGIEAPETRLAAGKPAEGRITIRARHHAGMLVLELSDDGGGIDLQRLRETVLNRQFATAETVAQLSEEELLAFLFLP 435
Cdd:COG3321  941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  436 GFSMREQVTEVSGRGVGLDAVQHMVRQLRGGVRM-----EQRQGQGALFHVEVPLTLSVVRSLVVEIGEEAYAFPLAHIE 510
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAaaaaaALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  511 RMCELEAEEIVQLEGRQHFWYEGRHVGLVSAAQLLQRPESSRTEGAIPVVVVRDRDAVYGVAVERFVGERTLVVMPLDPR 590
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALA 1180
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  591 LgkVRDVSAGALLDDGSPVLILDVEDLLHSVGKLLSSGRLERIDRSRRQAGGAQRKRILVVDDSLTVRELERKLLLGRGY 670
Cdd:COG3321 1181 L--AAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAA 1258
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  671 DVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVSYKDREEDRRRGLDAGADYYLAKAS 750
Cdd:COG3321 1259 LAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVA 1338
                        490
                 ....*....|....*....
gi 15598899  751 FHDEALLDAVVVLIGEAQG 769
Cdd:COG3321 1339 AALALAAAAAAAAAAAAAA 1357
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
343-485 8.29e-04

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 42.65  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  343 EKLEAPLTHLLRNAVdhgiEApetrlaagKPAEGRITIRARHHA-GMLVLELSDDGGGIDlqrlretvlnrqfataetva 421
Cdd:PRK11360 499 ELLKQVLLNILINAV----QA--------ISARGKIRIRTWQYSdGQVAVSIEDNGCGID-------------------- 546
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598899  422 qlseEELLAFLFLPGFSmreqvTEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPL 485
Cdd:PRK11360 547 ----PELLKKIFDPFFT-----TKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
648-716 8.59e-04

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: 39.83  E-value: 8.59e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598899 648 ILVVDDSLTVRElERKLLLGRGYD---VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSR 716
Cdd:cd17532   1 ALIVDDEPLARE-ELRYLLEEHPDieiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAK 71
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
493-617 8.93e-04

CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 238331  Cd Length: 136  Bit Score: 39.95  E-value: 8.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 493 LVVEIGEEAYAFPLAHIErMCELEAEEIVQLEGRQHFW----YEGRHVGLVSAAQLLQRPESSRTEGAIPVVVVRDRDAV 568
Cdd:cd00588   5 LLFRVGDELYAIPIAVVE-EILPLPPITRVPNAPDYVLgvinLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVGDRK 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598899 569 YGVAVERFVGERTLVVMPLDPRLGKVRD----VSAGALLDDGSPVLILDVEDL 617
Cdd:cd00588  84 VGLVVDSVLGVLEVVIKDIEPPPDVGSSnapgISGATILGDGRVVLILDVDKL 136
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
325-407 9.65e-04

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 39.90  E-value: 9.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 325 QVRLLVEG--ESTQVDRDVLEKLEAPLTHLLRNAVDHGieapetrlaAGKPAEGRITIRARHHAGMLVLELSDDGGGIDL 402
Cdd:COG2172  13 LARRAVRAllRELGLDEDDADDLVLAVSEAVTNAVRHA---------YGGDPDGPVEVELELDPDGLEIEVRDEGPGFDP 83

                ....*
gi 15598899 403 QRLRE 407
Cdd:COG2172  84 EDLPD 88
PRK11697 PRK11697
two-component system response regulator BtsR;
647-708 1.09e-03

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 41.37  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598899  647 RILVVDDSLTVRElERKLLLGRGYDVAV---AVDGMDGWNALRSEHFDLLITDIDMPRMDGIELV 708
Cdd:PRK11697   3 KVLIVDDEPLARE-ELRELLQEEGDIEIvgeCSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELV 66
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
648-748 1.59e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 38.79  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTVRELERKLL----LGRGydVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVrRDSRLQSLPVM 723
Cdd:cd17565   1 FYIVDDDKNIIKILSDIIedddLGEV--VGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKL-KDTGSNGKFIM 77
                        90       100
                ....*....|....*....|....*
gi 15598899 724 VVSYKDrEEDRRRGLDAGADYYLAK 748
Cdd:cd17565  78 ISQVSD-KEMIGKAYQAGIEFFINK 101
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
373-484 2.21e-03

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 38.51  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 373 PAEGRITIRAR----------HHAGM-----LVLELSDDGGGIDlqrlretvlnrqfataetvaqlseEELLAFLFLPGF 437
Cdd:cd16919  17 PEGGRLTIETSnqrvdadyalNYRDLipgnyVCLEVSDTGSGMP------------------------AEVLRRAFEPFF 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15598899 438 SMREqvtEVSGRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVP 484
Cdd:cd16919  73 TTKE---VGKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
fixJ PRK09390
response regulator FixJ; Provisional
650-726 3.15e-03

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 39.60  E-value: 3.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598899  650 VVDDSLTVRELERKLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIElvtLVRRDSRLQS-LPVMVVS 726
Cdd:PRK09390   8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIE---LLRRLKARGSpLPVIVMT 82
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
305-485 3.19e-03

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 40.93  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  305 ADVLSGQARMVRDLGRSLGKQVRLLVEGESTQVDRDVlEKLEAPLTHLLRNAVDhgieapetrlaaGKPAEGRITIRARH 384
Cdd:PRK10364 310 NDLINHSLQLVSQDANSREIQLRFTANDTLPEIQADP-DRLTQVLLNLYLNAIQ------------AIGQHGVISVTASE 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  385 HAGMLVLELSDDGGGIDLQRLREtvlnrqfataetvaqlseeellafLFLPGFSmreqvTEVSGRGVGLDAVQHMVRQLR 464
Cdd:PRK10364 377 SGAGVKISVTDSGKGIAADQLEA------------------------IFTPYFT-----TKAEGTGLGLAVVHNIVEQHG 427
                        170       180
                 ....*....|....*....|.
gi 15598899  465 GGVRMEQRQGQGALFHVEVPL 485
Cdd:PRK10364 428 GTIQVASQEGKGATFTLWLPV 448
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
647-708 3.76e-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: 3.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598899 647 RILVVDDSLTVRELERKLLLGRGYD-VAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELV 708
Cdd:cd17530   2 RVLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFL 64
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
374-485 4.48e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 37.47  E-value: 4.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 374 AEGRITIRAR-----HHAGMLVLELSDDGGGIDlqrlretvlnrqfataetvaqlseEELLAFLFLPgFSmreQVtEVS- 447
Cdd:cd16922  17 EEGEVTLRVSleeeeEDGVQLRFSVEDTGIGIP------------------------EEQQARLFEP-FS---QA-DSSt 67
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15598899 448 -----GRGVGLDAVQHMVRQLRGGVRMEQRQGQGALFHVEVPL 485
Cdd:cd16922  68 trkygGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
pleD PRK09581
response regulator PleD; Reviewed
630-746 5.11e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 39.88  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  630 LERIDRSRRQAGGaqrkRILVVDDSltVRELER-KLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELV 708
Cdd:PRK09581 144 LMIMAYANKDEDG----RILLVDDD--VSQAERiANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLC 217
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15598899  709 TLVRRDSRLQSLPVMVVSYKDREEDRRRGLDAGADYYL 746
Cdd:PRK09581 218 SQLRSKERTRYVPILLLVDEDDDPRLVKALELGVNDYL 255
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
648-748 5.53e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 39.09  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899  648 ILVVDDSLTVReLERKLLLGRGYDVAVAVDGMDGWNA---LRSEHFDLLITDIDMPRMDGIelvTLVRRDSRLQS-LPVM 723
Cdd:PRK09935   6 VIIMDTHPIIR-MSIEVLLQKNSELQIVLKTDDYRITidyLRTRPVDLIIMDIDLPGTDGF---TFLKRIKQIQStVKVL 81
                         90       100
                 ....*....|....*....|....*
gi 15598899  724 VVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:PRK09935  82 FLSSKSECFYAGRAIQAGANGFVSK 106
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
648-748 7.58e-03

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 37.32  E-value: 7.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSLTV-----RELERKLllGRGYDVAVAVDGMDGWNAL-----RSEHFDLLITDIDMPRMDGIELVTLVrRDSRL 717
Cdd:cd17595   3 ILTVDDDPQVlravaRDLRRQY--GKDYRVLRADSGAEALDALkelklRGEAVALFLVDQRMPEMDGVEFLEKA-MELFP 79
                        90       100       110
                ....*....|....*....|....*....|.
gi 15598899 718 QSLPVMVVSYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17595  80 EAKRVLLTAYADTDAAIRAINDVQLDYYLLK 110
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
648-746 8.36e-03

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 36.91  E-value: 8.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 648 ILVVDDSltVRELER-KLLLGRGYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVVS 726
Cdd:cd17539   1 VLLVDDR--PSSAERiAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVA 78
                        90       100
                ....*....|....*....|
gi 15598899 727 YKDREEDRRRGLDAGADYYL 746
Cdd:cd17539  79 DPGDRGRLIRALEIGVNDYL 98
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
647-748 9.33e-03

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 37.00  E-value: 9.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598899 647 RILVVDDSLTVRELERKLLLGR-GYDVAVAVDGMDGWNALRSEHFDLLITDIDMPRMDGIELVTLVRRDSRLQSLPVMVV 725
Cdd:cd17575   2 MVLLVDDQAIIGEAVRRALADEeDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVL 81
                        90       100
                ....*....|....*....|...
gi 15598899 726 SYKDREEDRRRGLDAGADYYLAK 748
Cdd:cd17575  82 STKEEPEVKSEAFALGANDYLVK 104
 
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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