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Conserved domains on  [gi|1800169395|ref|WP_160247160|]
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hybrid sensor histidine kinase/response regulator transcription factor [Phocaeicola sartorii]

Protein Classification

hybrid sensor histidine kinase/response regulator transcription factor( domain architecture ID 15525797)

two-component hybrid sensor histidine kinase/response regulator transcription factor containing a ligand-binding periplasmic sensor domain, a Y_Y_Y domain, and an AraC family helix-turn-helix (HTH) DNA-binding domain; receives the signal from the sensor partner in a two-component system through its receiver (REC) domain and functions as a protein kinase that phosphorylates a target protein in response to various signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
22-1066 6.56e-108

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


:

Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 364.31  E-value: 6.56e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395   22 SAPVANTYYFSNLSLKDGLSQLSVLKIYQDSKGYMWFGTRNGLNKYDGNRMVVYKHLDSDSLSLVDNHITAIVEDRKNCL 101
Cdd:COG3292     15 FAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNYIRALLEDSDGRL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  102 WVGTSRGLNRLDLKTDRITPYAGKNfSLLDSGVRSLFIDSNDRLWVGTSKGLYLFVHEADTFQSVDLDGkikgefisvit 181
Cdd:COG3292     95 WIGTDGGLSRYDPKTDKFTRYPLDP-GLPNNSIRSIAEDSDGNIWVGTSNGLYRYDPKTGKFKRFTLDG----------- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  182 etsdhqlligtehkglyvcdlnlklishyaktegnasLPDNNISDIHEDSRKQLWVstnyggvskvdlstgtsvhyttan 261
Cdd:COG3292    163 -------------------------------------LPSNTITSLAEDADGNLWV------------------------ 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  262 sklttdnirclaEADGTLFIGTF-DGLYTIDLTDNQLKgRSNAALEKGTLSHFSIYSICVDNSGNVWVGTYSGGVNYFSK 340
Cdd:COG3292    182 ------------DSDGNLWIGTDgNGLYRLDPNTGKFE-HITHDPDPNSLSSNSIYSLFEDREGNLWVGTYGGGLNYLDP 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  341 YNNRFvfheptnalnmlmgvygamacqpphclyiateggglldyhlesntyqyYLYDTSSSQQYSRNIIKSVMQEKD--- 417
Cdd:COG3292    249 NNSKF------------------------------------------------KSYRHNDPNGLSGNSVRSIAEDSDgnl 280
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  418 --YIWCGTTQGSIYRFDTRSKRFSLYYAFPLHQSTsVYSILRTQDNNLWLATSkpEVGLVKLTEErkmQNRFELADSGRI 495
Cdd:COG3292    281 wiRLWIGTYGGGLFRLDPKTGKFKRYNPNGLPSNS-VYSILEDSDGNLWIGTS--GGGLYRYDPK---TGKFTKFSEDNG 354
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  496 WTPGSSRCLLELEKGVLLVGSrNNGLYKYDENKRECTVFsKNGKGANHLPADYVTSLVRTKSGQIWVGTFGGGLSLFDQE 575
Cdd:COG3292    355 LSNNFIRSILEDSDGNLWVGT-NGGLYRLDPKTGKFTNF-THDPDKNGLSSNYINSIFEDSDGRLWIGTDGGGLYRYDPK 432
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  576 KGIVKYITKKEGLLDDEVCMVVEDRNGDLWmstnscisryNPKTDEVYNYYMDNGIGaqefsphsgmllpdgnicfsaNN 655
Cdd:COG3292    433 TGKFKHFTTKDGLPSNTIYSILEDDNGNLW----------NFNSASNLGLLSLLGGL---------------------LG 481
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  656 GFITFDPANLQINSFLPPLVLTTLAVNN-RVVNPTGEGILQMVLDDTEKIELNYNQNNITIGYCALNYVCSDLNQYAYRL 734
Cdd:COG3292    482 GLNLGNAIKLPLSNLGLLLTLLLLGINLsLVRSLISLLTLLLLALLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLL 561
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  735 KGYDKDWNYVGNRKEAYYTNLGPGKYVFEVKASNNDGIWNDEIRTLSIIVHPPYWMTWYAYLFYAFSFFGICFLVMYYII 814
Cdd:COG3292    562 LLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLL 641
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  815 KKKNLEQALVYEHLKQQQAEEFHQTKMRMFTNFSHELRTPLTLIISPLQELLRRNEFNTGIRNKLDLIYNNSQRLLLLVN 894
Cdd:COG3292    642 LLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLLLALKLLLLLLLILLLLLLLLGL 721
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  895 QLMDLRKNQAGKMQLKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAG 974
Cdd:COG3292    722 LLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETV 801
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  975 GEIVLSVAKLKLKDVPAGQRKELESLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSI 1054
Cdd:COG3292    802 SEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLLGLLLLLLLEILLLSLVELLLELLEGIILALD 881
                         1050
                   ....*....|..
gi 1800169395 1055 VRLHHGTIRVEN 1066
Cdd:COG3292    882 LLLGSLSLVILL 893
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1117-1301 1.59e-43

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: 157.43  E-value: 1.59e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1117 KYTVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVIL 1195
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREGYeVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPS--DIPIIM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREKLRSLYGKKFSPEAIGVEIVSGTDRFTQKFFEVIERN 1275
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDLLDLAAREVTRDGEPVELTPKEFRLLELL 158
                          170       180
                   ....*....|....*....|....*.
gi 1800169395 1276 IANPELNidlicrevgLSRTNLYRKL 1301
Cdd:COG0745    159 MRNPGRV---------VSREQLLEEV 175
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1281-1369 2.69e-25

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 106.79  E-value: 2.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1281 LNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCFKSVYGCSPT 1360
Cdd:COG2207    169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                   ....*....
gi 1800169395 1361 EFLMEHKKE 1369
Cdd:COG2207    249 EYRKRLRAR 257
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
22-1066 6.56e-108

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 364.31  E-value: 6.56e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395   22 SAPVANTYYFSNLSLKDGLSQLSVLKIYQDSKGYMWFGTRNGLNKYDGNRMVVYKHLDSDSLSLVDNHITAIVEDRKNCL 101
Cdd:COG3292     15 FAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNYIRALLEDSDGRL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  102 WVGTSRGLNRLDLKTDRITPYAGKNfSLLDSGVRSLFIDSNDRLWVGTSKGLYLFVHEADTFQSVDLDGkikgefisvit 181
Cdd:COG3292     95 WIGTDGGLSRYDPKTDKFTRYPLDP-GLPNNSIRSIAEDSDGNIWVGTSNGLYRYDPKTGKFKRFTLDG----------- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  182 etsdhqlligtehkglyvcdlnlklishyaktegnasLPDNNISDIHEDSRKQLWVstnyggvskvdlstgtsvhyttan 261
Cdd:COG3292    163 -------------------------------------LPSNTITSLAEDADGNLWV------------------------ 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  262 sklttdnirclaEADGTLFIGTF-DGLYTIDLTDNQLKgRSNAALEKGTLSHFSIYSICVDNSGNVWVGTYSGGVNYFSK 340
Cdd:COG3292    182 ------------DSDGNLWIGTDgNGLYRLDPNTGKFE-HITHDPDPNSLSSNSIYSLFEDREGNLWVGTYGGGLNYLDP 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  341 YNNRFvfheptnalnmlmgvygamacqpphclyiateggglldyhlesntyqyYLYDTSSSQQYSRNIIKSVMQEKD--- 417
Cdd:COG3292    249 NNSKF------------------------------------------------KSYRHNDPNGLSGNSVRSIAEDSDgnl 280
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  418 --YIWCGTTQGSIYRFDTRSKRFSLYYAFPLHQSTsVYSILRTQDNNLWLATSkpEVGLVKLTEErkmQNRFELADSGRI 495
Cdd:COG3292    281 wiRLWIGTYGGGLFRLDPKTGKFKRYNPNGLPSNS-VYSILEDSDGNLWIGTS--GGGLYRYDPK---TGKFTKFSEDNG 354
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  496 WTPGSSRCLLELEKGVLLVGSrNNGLYKYDENKRECTVFsKNGKGANHLPADYVTSLVRTKSGQIWVGTFGGGLSLFDQE 575
Cdd:COG3292    355 LSNNFIRSILEDSDGNLWVGT-NGGLYRLDPKTGKFTNF-THDPDKNGLSSNYINSIFEDSDGRLWIGTDGGGLYRYDPK 432
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  576 KGIVKYITKKEGLLDDEVCMVVEDRNGDLWmstnscisryNPKTDEVYNYYMDNGIGaqefsphsgmllpdgnicfsaNN 655
Cdd:COG3292    433 TGKFKHFTTKDGLPSNTIYSILEDDNGNLW----------NFNSASNLGLLSLLGGL---------------------LG 481
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  656 GFITFDPANLQINSFLPPLVLTTLAVNN-RVVNPTGEGILQMVLDDTEKIELNYNQNNITIGYCALNYVCSDLNQYAYRL 734
Cdd:COG3292    482 GLNLGNAIKLPLSNLGLLLTLLLLGINLsLVRSLISLLTLLLLALLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLL 561
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  735 KGYDKDWNYVGNRKEAYYTNLGPGKYVFEVKASNNDGIWNDEIRTLSIIVHPPYWMTWYAYLFYAFSFFGICFLVMYYII 814
Cdd:COG3292    562 LLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLL 641
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  815 KKKNLEQALVYEHLKQQQAEEFHQTKMRMFTNFSHELRTPLTLIISPLQELLRRNEFNTGIRNKLDLIYNNSQRLLLLVN 894
Cdd:COG3292    642 LLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLLLALKLLLLLLLILLLLLLLLGL 721
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  895 QLMDLRKNQAGKMQLKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAG 974
Cdd:COG3292    722 LLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETV 801
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  975 GEIVLSVAKLKLKDVPAGQRKELESLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSI 1054
Cdd:COG3292    802 SEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLLGLLLLLLLEILLLSLVELLLELLEGIILALD 881
                         1050
                   ....*....|..
gi 1800169395 1055 VRLHHGTIRVEN 1066
Cdd:COG3292    882 LLLGSLSLVILL 893
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1117-1301 1.59e-43

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: 157.43  E-value: 1.59e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1117 KYTVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVIL 1195
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREGYeVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPS--DIPIIM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREKLRSLYGKKFSPEAIGVEIVSGTDRFTQKFFEVIERN 1275
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDLLDLAAREVTRDGEPVELTPKEFRLLELL 158
                          170       180
                   ....*....|....*....|....*.
gi 1800169395 1276 IANPELNidlicrevgLSRTNLYRKL 1301
Cdd:COG0745    159 MRNPGRV---------VSREQLLEEV 175
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
816-1236 3.50e-36

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 149.16  E-value: 3.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  816 KKNLEQ-----------------ALVYEHLK-QQQAEEFHQTKMRMFTNFSHELRTPLTLIISPLqELLRRNEFNTGIRN 877
Cdd:TIGR02956  422 KESLEQlvaqrtqelaetnerlnAEVKNHAKaRAEAEEANRAKSAFLATMSHEIRTPLNGILGTL-ELLGDTGLTSQQQQ 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  878 KLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEvGIVAWF--DKSL 955
Cdd:TIGR02956  501 YLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPE-QLPNWWqgDGPR 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  956 FEKVVFNLLSNAFKYTQAgGEIVLSVaklklkdvpagqrkeleSLSEDTELvhLF-VSDTGKGIPEEEMKNIFAPFYQIE 1034
Cdd:TIGR02956  580 IRQVLINLVGNAIKFTDR-GSVVLRV-----------------SLNDDSSL--LFeVEDTGCGIAEEEQATLFDAFTQAD 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1035 DRKAkdVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRrvyteEEIDREAADRVVMDVIPSttapevfgl 1114
Cdd:TIGR02956  640 GRRR--SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR-----GKPAEDSATLTVIDLPPQ--------- 703
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1115 ekkyTVLLVEDNeEVRSYVRECLDPHF--FVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGH-I 1191
Cdd:TIGR02956  704 ----RVLLVEDN-EVNQMVAQGFLTRLghKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNeV 778
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1800169395 1192 PVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILAS 1236
Cdd:TIGR02956  779 KFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAG 823
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1121-1220 2.91e-33

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: 124.06  E-value: 2.91e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1121 LLVEDNEEVRSYVRECLDP-HFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghIPVILMTAR 1199
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKeGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1800169395 1200 SMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
848-1227 5.20e-31

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 131.99  E-value: 5.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  848 SHELRTPLTLIISpLQELLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDICSFVMEIYCAF 927
Cdd:PRK11091   291 SHELRTPLNGIVG-LSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLS 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  928 NQIASGKEIRFRYE-GGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGeIVLSVAklklkdvpagqrkeleslSEDTEL 1006
Cdd:PRK11091   370 GLQAEQKGLRFDLEpLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGG-VTVRVR------------------YEEGDM 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1007 VHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVA-GTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRrvy 1085
Cdd:PRK11091   431 LTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPA--- 507
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1086 teeeIDREAADRVVMDVIPSTtapevfglekKYTVLLVED---NEEVRSYVRECLDPHFFVleADNGETAFEIVLDKYPD 1162
Cdd:PRK11091   508 ----VAEEVEDAFDEDDMPLP----------ALNILLVEDielNVIVARSVLEKLGNSVDV--AMTGKEALEMFDPDEYD 571
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800169395 1163 IVVSDIMMPRKDGLELC-TLIKEDLRTGHIPVILMTArSMVMHIKEGFSAGADDYIVKPFNMDVLI 1227
Cdd:PRK11091   572 LVLLDIQLPDMTGLDIArELRERYPREDLPPLVALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALT 636
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
952-1080 2.05e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 116.21  E-value: 2.05e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395   952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTL-------------------ERDGDHVEITVEDNGPGIPPEDLEKIFEPFF 62
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1800169395  1032 QiEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPI 1080
Cdd:smart00387   63 R-TDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPL 110
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1120-1231 4.09e-30

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: 115.33  E-value: 4.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTA 1198
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
956-1078 2.33e-28

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 110.00  E-value: 2.33e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  956 FEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIed 1035
Cdd:cd00075      1 LEQVLSNLLDNALKYSPPGGTIEISL-------------------RQEGDGVVLEVEDNGPGIPEEDLERIFERFYRG-- 59
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1800169395 1036 RKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLF 1078
Cdd:cd00075     60 DKSREGGGTGLGLAIVRRIVEAHGGRITVESEPGGGTTFTVTL 102
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
952-1082 1.57e-25

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: 102.45  E-value: 1.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslsEDTELVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEITVTL--------------------SEGGELTLTVEDNGIGIPPEDLPRIFEPFS 61
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1800169395 1032 QIEDRKAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDR 1082
Cdd:pfam02518   62 TADKRGGG---GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1281-1369 2.69e-25

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 106.79  E-value: 2.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1281 LNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCFKSVYGCSPT 1360
Cdd:COG2207    169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                   ....*....
gi 1800169395 1361 EFLMEHKKE 1369
Cdd:COG2207    249 EYRKRLRAR 257
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
842-1074 2.83e-24

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 109.46  E-value: 2.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  842 RMF-TNFSHELRTPLTLIISPLQELlrrnefNTG-IRNK------LDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAK 913
Cdd:NF033092   373 REFvANVSHELRTPLTTMRSYLEAL------ADGaWKDPelaprfLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKEW 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  914 DDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLsvaklklkdvpagq 993
Cdd:NF033092   447 VNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGTITF-------------- 512
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  994 rkeleSLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGAT 1073
Cdd:NF033092   513 -----RLLETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTT 587

                   .
gi 1800169395 1074 F 1074
Cdd:NF033092   588 I 588
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
1119-1234 3.45e-24

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


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 102.41  E-value: 3.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMT 1197
Cdd:TIGR02154    4 RILVVEDEPAIRELIAYNLEKAGYdVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPIIMLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:TIGR02154   84 ARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVL 120
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1280-1363 4.03e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 97.24  E-value: 4.03e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  1280 ELNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCFKSVYGCSP 1359
Cdd:smart00342    1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                    ....
gi 1800169395  1360 TEFL 1363
Cdd:smart00342   81 SEYR 84
pleD PRK09581
response regulator PleD; Reviewed
1141-1231 3.19e-21

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 98.43  E-value: 3.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1141 FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:PRK09581    27 YTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKP 106
                           90
                   ....*....|.
gi 1800169395 1221 FNMDVLIYRIR 1231
Cdd:PRK09581   107 INDVALFARVK 117
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
831-1079 8.75e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.20  E-value: 8.75e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  831 QQAEEFHQT-KMR--MFTNFSHELRTPLTLI---ISPLQELLRRNEfntgiRNKLDLIYNNSQRLLLLVNQLMDLRKNQA 904
Cdd:NF012163   228 QLASTLEKNeQMRrdFMADISHELRTPLAVLraeLEAIQDGIRKFT-----PESLDSLQAEVGTLTKLVDDLHDLSMSDE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  905 GKMQLKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVaWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVAKl 984
Cdd:NF012163   303 GALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSSLV-FGDRDRLMQLFNNLLENSLRYTDSGGSLHISASQ- 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  985 klkdVPAGqrkeleslsedtelVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRV 1064
Cdd:NF012163   381 ----RPKE--------------VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHA 442
                          250
                   ....*....|....*
gi 1800169395 1065 ENNARGGATFHVLFP 1079
Cdd:NF012163   443 AHSPLGGLRIVVTLP 457
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
831-1104 1.35e-19

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 93.94  E-value: 1.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  831 QQAEEFHQTKMRMFTNFSHELRTPLTlIISPLQELL--RRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQ 908
Cdd:NF040691   262 RQLEELSRLQQRFVSDVSHELRTPLT-TIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAE 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  909 LKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQaGGEIVLSVAklklkd 988
Cdd:NF040691   341 LDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGE-GKPVVVTVA------ 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  989 vpagqrkeleslSEDTElVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNA 1068
Cdd:NF040691   414 ------------QDDTA-VAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRP 480
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1800169395 1069 RGGATFHVLFPidrrvyteeeidREAADRVVMDVIP 1104
Cdd:NF040691   481 GQGSQFRLTLP------------RVAGDRLTTSPLP 504
HTH_18 pfam12833
Helix-turn-helix domain;
1286-1363 2.21e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.79  E-value: 2.21e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800169395 1286 ICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLE-SDYSVSEISTCVGFNSHAYFTQCFKSVYGCSPTEFL 1363
Cdd:pfam12833    1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEdTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
1120-1231 1.39e-16

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 80.30  E-value: 1.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNE---EVRSYV--RECLDPHFfvleADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKedlRTGHIPVI 1194
Cdd:NF040689     1 ILVVDDDPalaEMLGIVlrAEGFETVF----CADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIR---AESGVPII 73
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1195 LMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:NF040689    74 MLTAKSDTVDVVRGLEAGADDYVVKPFKPKELVARIR 110
resp_reg_YycF NF040534
response regulator YycF;
1143-1231 2.01e-14

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 74.37  E-value: 2.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1143 VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCtliKEDLRTGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFN 1222
Cdd:NF040534    27 VFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVC---REVRKKYDMPIIMLTAKDSEIDKVLGLELGADDYVTKPFS 103

                   ....*....
gi 1800169395 1223 MDVLIYRIR 1231
Cdd:NF040534   104 TRELIARVK 112
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1118-1171 1.89e-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: 62.97  E-value: 1.89e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1800169395  1118 YTVLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMP 1171
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLeKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
1259-1362 3.78e-08

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 56.58  E-value: 3.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1259 SGTDRFTQKFFEVIERNIANPELNIDLICREVGLSRTNLYRkLKAITELSPVELIRNKRLEVAARLL--LESDYSVSEIS 1336
Cdd:PRK09685   193 PRRERQFQKVVALIDQSIQEEILRPEWIAGELGISVRSLYR-LFAEQGLVVAQYIRNRRLDRCADDLrpAADDEKITSIA 271
                           90       100
                   ....*....|....*....|....*.
gi 1800169395 1337 TCVGFNSHAYFTQCFKSVYGCSPTEF 1362
Cdd:PRK09685   272 YKWGFSDSSHFSTAFKQRFGVSPGEY 297
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
22-1066 6.56e-108

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 364.31  E-value: 6.56e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395   22 SAPVANTYYFSNLSLKDGLSQLSVLKIYQDSKGYMWFGTRNGLNKYDGNRMVVYKHLDSDSLSLVDNHITAIVEDRKNCL 101
Cdd:COG3292     15 FAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNYIRALLEDSDGRL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  102 WVGTSRGLNRLDLKTDRITPYAGKNfSLLDSGVRSLFIDSNDRLWVGTSKGLYLFVHEADTFQSVDLDGkikgefisvit 181
Cdd:COG3292     95 WIGTDGGLSRYDPKTDKFTRYPLDP-GLPNNSIRSIAEDSDGNIWVGTSNGLYRYDPKTGKFKRFTLDG----------- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  182 etsdhqlligtehkglyvcdlnlklishyaktegnasLPDNNISDIHEDSRKQLWVstnyggvskvdlstgtsvhyttan 261
Cdd:COG3292    163 -------------------------------------LPSNTITSLAEDADGNLWV------------------------ 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  262 sklttdnirclaEADGTLFIGTF-DGLYTIDLTDNQLKgRSNAALEKGTLSHFSIYSICVDNSGNVWVGTYSGGVNYFSK 340
Cdd:COG3292    182 ------------DSDGNLWIGTDgNGLYRLDPNTGKFE-HITHDPDPNSLSSNSIYSLFEDREGNLWVGTYGGGLNYLDP 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  341 YNNRFvfheptnalnmlmgvygamacqpphclyiateggglldyhlesntyqyYLYDTSSSQQYSRNIIKSVMQEKD--- 417
Cdd:COG3292    249 NNSKF------------------------------------------------KSYRHNDPNGLSGNSVRSIAEDSDgnl 280
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  418 --YIWCGTTQGSIYRFDTRSKRFSLYYAFPLHQSTsVYSILRTQDNNLWLATSkpEVGLVKLTEErkmQNRFELADSGRI 495
Cdd:COG3292    281 wiRLWIGTYGGGLFRLDPKTGKFKRYNPNGLPSNS-VYSILEDSDGNLWIGTS--GGGLYRYDPK---TGKFTKFSEDNG 354
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  496 WTPGSSRCLLELEKGVLLVGSrNNGLYKYDENKRECTVFsKNGKGANHLPADYVTSLVRTKSGQIWVGTFGGGLSLFDQE 575
Cdd:COG3292    355 LSNNFIRSILEDSDGNLWVGT-NGGLYRLDPKTGKFTNF-THDPDKNGLSSNYINSIFEDSDGRLWIGTDGGGLYRYDPK 432
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  576 KGIVKYITKKEGLLDDEVCMVVEDRNGDLWmstnscisryNPKTDEVYNYYMDNGIGaqefsphsgmllpdgnicfsaNN 655
Cdd:COG3292    433 TGKFKHFTTKDGLPSNTIYSILEDDNGNLW----------NFNSASNLGLLSLLGGL---------------------LG 481
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  656 GFITFDPANLQINSFLPPLVLTTLAVNN-RVVNPTGEGILQMVLDDTEKIELNYNQNNITIGYCALNYVCSDLNQYAYRL 734
Cdd:COG3292    482 GLNLGNAIKLPLSNLGLLLTLLLLGINLsLVRSLISLLTLLLLALLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLL 561
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  735 KGYDKDWNYVGNRKEAYYTNLGPGKYVFEVKASNNDGIWNDEIRTLSIIVHPPYWMTWYAYLFYAFSFFGICFLVMYYII 814
Cdd:COG3292    562 LLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLL 641
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  815 KKKNLEQALVYEHLKQQQAEEFHQTKMRMFTNFSHELRTPLTLIISPLQELLRRNEFNTGIRNKLDLIYNNSQRLLLLVN 894
Cdd:COG3292    642 LLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLLLALKLLLLLLLILLLLLLLLGL 721
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  895 QLMDLRKNQAGKMQLKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAG 974
Cdd:COG3292    722 LLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETV 801
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  975 GEIVLSVAKLKLKDVPAGQRKELESLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSI 1054
Cdd:COG3292    802 SEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLLGLLLLLLLEILLLSLVELLLELLEGIILALD 881
                         1050
                   ....*....|..
gi 1800169395 1055 VRLHHGTIRVEN 1066
Cdd:COG3292    882 LLLGSLSLVILL 893
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
830-1080 1.61e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 224.79  E-value: 1.61e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  830 QQQAEEFHQTKMRMFTNFSHELRTPLTLIISPLQELLRRNEFNTG-IRNKLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQ 908
Cdd:COG2205      6 LEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEeRRELLEIIRESAERLLRLIEDLLDLSRLESGKLS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  909 LKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkd 988
Cdd:COG2205     86 LELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISA------- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  989 vpagqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRkaKDVAGTGIGLSLTQSIVRLHHGTIRVENNA 1068
Cdd:COG2205    159 ------------RREGDGVRISVSDNGPGIPEEELERIFERFYRGDNS--RGEGGTGLGLAIVKRIVEAHGGTIWVESEP 224
                          250
                   ....*....|..
gi 1800169395 1069 RGGATFHVLFPI 1080
Cdd:COG2205    225 GGGTTFTVTLPL 236
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
831-1080 7.99e-64

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 220.55  E-value: 7.99e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  831 QQAEEFHQTKMRMFTNFSHELRTPLTLIISPLQELLRrnEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLK 910
Cdd:COG0642    101 LLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLE--ELDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELE 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  911 IAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvp 990
Cdd:COG0642    179 PEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSV--------- 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  991 agqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEdrKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARG 1070
Cdd:COG0642    250 ----------RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTD--PSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGK 317
                          250
                   ....*....|
gi 1800169395 1071 GATFHVLFPI 1080
Cdd:COG0642    318 GTTFTVTLPL 327
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
832-1082 6.17e-59

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 208.64  E-value: 6.17e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  832 QAEEFHQTKMRMFTNFSHELRTPLTLIISPLQELLRRNEFNTGIRNK-LDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLK 910
Cdd:COG5002    157 ELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEERREyLEIILEEAERLSRLVNDLLDLSRLESGELKLE 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  911 IAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvp 990
Cdd:COG5002    237 KEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSL--------- 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  991 agqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARG 1070
Cdd:COG5002    308 ----------REEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGK 377
                          250
                   ....*....|..
gi 1800169395 1071 GATFHVLFPIDR 1082
Cdd:COG5002    378 GTTFTITLPLAR 389
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1117-1301 1.59e-43

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: 157.43  E-value: 1.59e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1117 KYTVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVIL 1195
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREGYeVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPS--DIPIIM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREKLRSLYGKKFSPEAIGVEIVSGTDRFTQKFFEVIERN 1275
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDLLDLAAREVTRDGEPVELTPKEFRLLELL 158
                          170       180
                   ....*....|....*....|....*.
gi 1800169395 1276 IANPELNidlicrevgLSRTNLYRKL 1301
Cdd:COG0745    159 MRNPGRV---------VSREQLLEEV 175
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1117-1230 4.12e-40

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: 146.59  E-value: 4.12e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1117 KYTVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVIL 1195
Cdd:COG3706      1 PARILVVDDDPTNRKLLRRLLEAAGYeVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRI 1230
Cdd:COG3706     81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1115-1243 2.55e-37

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: 140.30  E-value: 2.55e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1115 EKKYTVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPV 1193
Cdd:COG3437      4 GQAPTVLIVDDDPENLELLRQLLRTLGYdVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPV 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1194 ILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREKLRSL 1243
Cdd:COG3437     84 IFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQREL 133
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1116-1239 6.40e-37

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: 135.36  E-value: 6.40e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1116 KKYTVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVI 1194
Cdd:COG0784      4 GGKRILVVDDNPDNRELLRRLLERLGYeVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPII 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1800169395 1195 LMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREK 1239
Cdd:COG0784     84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
829-1083 7.29e-37

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 143.45  E-value: 7.29e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  829 KQQQAEEFHQTKMR----MFTNFSHELRTPLTLIISPLQeLLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQA 904
Cdd:COG3852    120 KRLERELRRAEKLAavgeLAAGLAHEIRNPLTGIRGAAQ-LLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRP 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  905 GKMQLKiakdDICSFVMEIYCAF-NQIASGKEIRFRYEGG--EVgivaWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSV 981
Cdd:COG3852    199 PEREPV----NLHEVLERVLELLrAEAPKNIRIVRDYDPSlpEV----LGDPDQLIQVLLNLVRNAAEAMPEGGTITIRT 270
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  982 AKLKLkDVPAGQRKELEslsedtelVHLFVSDTGKGIPEEEMKNIFAPFYQiedRKAKdvaGTGIGLSLTQSIVRLHHGT 1061
Cdd:COG3852    271 RVERQ-VTLGGLRPRLY--------VRIEVIDNGPGIPEEILDRIFEPFFT---TKEK---GTGLGLAIVQKIVEQHGGT 335
                          250       260
                   ....*....|....*....|..
gi 1800169395 1062 IRVENNARGGATFHVLFPIDRR 1083
Cdd:COG3852    336 IEVESEPGKGTTFRIYLPLEQA 357
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
816-1236 3.50e-36

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 149.16  E-value: 3.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  816 KKNLEQ-----------------ALVYEHLK-QQQAEEFHQTKMRMFTNFSHELRTPLTLIISPLqELLRRNEFNTGIRN 877
Cdd:TIGR02956  422 KESLEQlvaqrtqelaetnerlnAEVKNHAKaRAEAEEANRAKSAFLATMSHEIRTPLNGILGTL-ELLGDTGLTSQQQQ 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  878 KLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEvGIVAWF--DKSL 955
Cdd:TIGR02956  501 YLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPE-QLPNWWqgDGPR 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  956 FEKVVFNLLSNAFKYTQAgGEIVLSVaklklkdvpagqrkeleSLSEDTELvhLF-VSDTGKGIPEEEMKNIFAPFYQIE 1034
Cdd:TIGR02956  580 IRQVLINLVGNAIKFTDR-GSVVLRV-----------------SLNDDSSL--LFeVEDTGCGIAEEEQATLFDAFTQAD 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1035 DRKAkdVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRrvyteEEIDREAADRVVMDVIPSttapevfgl 1114
Cdd:TIGR02956  640 GRRR--SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR-----GKPAEDSATLTVIDLPPQ--------- 703
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1115 ekkyTVLLVEDNeEVRSYVRECLDPHF--FVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGH-I 1191
Cdd:TIGR02956  704 ----RVLLVEDN-EVNQMVAQGFLTRLghKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNeV 778
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1800169395 1192 PVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILAS 1236
Cdd:TIGR02956  779 KFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAG 823
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
819-1080 7.09e-36

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 140.32  E-value: 7.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  819 LEQALvyEHLKQQQAEEFHQTKM----RMFTNFSHELRTPLTLI---ISPLQELLRRNEFNTGIRNKLDLIYNNSQRLLL 891
Cdd:COG4191    119 LERAE--EELRELQEQLVQSEKLaalgELAAGIAHEINNPLAAIlgnAELLRRRLEDEPDPEELREALERILEGAERAAE 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  892 LVNQLMDL-RKNQAGKMQLKIAK--DDICSFVMeiycafNQIASgKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAF 968
Cdd:COG4191    197 IVRSLRAFsRRDEEEREPVDLNEliDEALELLR------PRLKA-RGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAI 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  969 kytQAggeivlsvaklklkdVPAGQRKELE-SLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQiedrkAKDVA-GTGI 1046
Cdd:COG4191    270 ---DA---------------MEEGEGGRITiSTRREGDYVVISVRDNGPGIPPEVLERIFEPFFT-----TKPVGkGTGL 326
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1800169395 1047 GLSLTQSIVRLHHGTIRVENNARGGATFHVLFPI 1080
Cdd:COG4191    327 GLSISYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
848-1080 1.61e-35

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: 140.87  E-value: 1.61e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  848 SHELRTPLT---LIISPLQELLRRN--EFNTGIRNKLDLIYNNSQRLLLLVNQLMDLrknqAGKMQLKIAKDDICSFVME 922
Cdd:COG5000    209 AHEIKNPLTpiqLSAERLRRKLADKleEDREDLERALDTIIRQVDRLKRIVDEFLDF----ARLPEPQLEPVDLNELLRE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  923 IYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslSE 1002
Cdd:COG5000    285 VLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVST-------------------RR 345
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800169395 1003 DTELVHLFVSDTGKGIPEEEMKNIFAPFYQiedRKAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPI 1080
Cdd:COG5000    346 EDGRVRIEVSDNGPGIPEEVLERIFEPFFT---TKPK---GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPL 417
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1121-1220 2.91e-33

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: 124.06  E-value: 2.91e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1121 LLVEDNEEVRSYVRECLDP-HFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghIPVILMTAR 1199
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKeGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1800169395 1200 SMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
848-1083 1.96e-31

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 130.29  E-value: 1.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  848 SHELRTPLTLIISPLQELLRR--NEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLrkNQAGKMQLKIAKDDICSFVMEIYC 925
Cdd:COG4251    290 SHDLREPLRKISGFSQLLEEDygDKLDEEGREYLERIRDAAERMQALIDDLLAY--SRVGRQELEFEPVDLNELLEEVLE 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  926 AFNQIASGKEIRFRYEGGevgIVAWFDKSLFEKVVFNLLSNAFKYTQAG--GEIVLSVaklklkdvpagqrkeleslSED 1003
Cdd:COG4251    368 DLEPRIEERGAEIEVGPL---PTVRGDPTLLRQVFQNLISNAIKYSRPGepPRIEIGA-------------------ERE 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1004 TELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKakDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRR 1083
Cdd:COG4251    426 GGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRD--EYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAPA 503
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1121-1220 4.01e-31

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: 117.71  E-value: 4.01e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1121 LLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVILMTAR 1199
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYeVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPP--DIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1800169395 1200 SMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
848-1227 5.20e-31

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 131.99  E-value: 5.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  848 SHELRTPLTLIISpLQELLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDICSFVMEIYCAF 927
Cdd:PRK11091   291 SHELRTPLNGIVG-LSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLS 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  928 NQIASGKEIRFRYE-GGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGeIVLSVAklklkdvpagqrkeleslSEDTEL 1006
Cdd:PRK11091   370 GLQAEQKGLRFDLEpLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGG-VTVRVR------------------YEEGDM 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1007 VHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVA-GTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRrvy 1085
Cdd:PRK11091   431 LTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPA--- 507
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1086 teeeIDREAADRVVMDVIPSTtapevfglekKYTVLLVED---NEEVRSYVRECLDPHFFVleADNGETAFEIVLDKYPD 1162
Cdd:PRK11091   508 ----VAEEVEDAFDEDDMPLP----------ALNILLVEDielNVIVARSVLEKLGNSVDV--AMTGKEALEMFDPDEYD 571
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800169395 1163 IVVSDIMMPRKDGLELC-TLIKEDLRTGHIPVILMTArSMVMHIKEGFSAGADDYIVKPFNMDVLI 1227
Cdd:PRK11091   572 LVLLDIQLPDMTGLDIArELRERYPREDLPPLVALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALT 636
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1119-1234 6.35e-31

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: 118.12  E-value: 6.35e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMT 1197
Cdd:cd17618      2 TILIVEDEPAIREMIAFNLERAGFdVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17618     82 ARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
952-1080 2.05e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 116.21  E-value: 2.05e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395   952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTL-------------------ERDGDHVEITVEDNGPGIPPEDLEKIFEPFF 62
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1800169395  1032 QiEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPI 1080
Cdd:smart00387   63 R-TDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPL 110
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1120-1231 4.09e-30

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: 115.33  E-value: 4.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTA 1198
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1116-1291 8.40e-30

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: 123.92  E-value: 8.40e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1116 KKYTVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVI 1194
Cdd:COG2204      1 SMARILVVDDDPDIRRLLKELLERAGYeVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDP--DLPVI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1195 LMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREKLRSLygkkfspeAIGVEIVsGTDRFTQKFFEVIER 1274
Cdd:COG2204     79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRREN--------AEDSGLI-GRSPAMQEVRRLIEK 149
                          170
                   ....*....|....*..
gi 1800169395 1275 nIANPELNIdLICREVG 1291
Cdd:COG2204    150 -VAPSDATV-LITGESG 164
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
726-1089 1.09e-29

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 125.09  E-value: 1.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  726 DLNQYAYRLKGYDKDwnyvgNRKEAYYTNLGPGKYVFEVKASNNDGIWNDEIRTLSIivhpPYWMTWYAYLFYAFSFFGI 805
Cdd:COG5809    165 YANPAACKLLGISIE-----ELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEV----RFWTKDGRWRLLEASGAPI 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  806 CF---LVMYYIIKKKNLEQaLVYEHLKQqqaeefHQTKMRMFTNF----SHELRTPLTLIISPLQeLLRRNeFNTGIRNK 878
Cdd:COG5809    236 KKngeVDGIVIIFRDITER-KKLEELLR------KSEKLSVVGELaagiAHEIRNPLTSLKGFIQ-LLKDT-IDEEQKTY 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  879 LDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKiakdDICSFVMEIYCAFNQIA--SGKEIRFRYEGGEVGIVAwfDKSLF 956
Cdd:COG5809    307 LDIMLSELDRIESIISEFLVLAKPQAIKYEPK----DLNTLIEEVIPLLQPQAllKNVQIELELEDDIPDILG--DENQL 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  957 EKVVFNLLSNAFKYTQAGGEIVLSVAKlklkdvpagqrkeleslsEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQiedR 1036
Cdd:COG5809    381 KQVFINLLKNAIEAMPEGGNITIETKA------------------EDDDKVVISVTDEGCGIPEERLKKLGEPFYT---T 439
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1800169395 1037 KAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRRVYTEEE 1089
Cdd:COG5809    440 KEK---GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSMN 489
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
956-1078 2.33e-28

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 110.00  E-value: 2.33e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  956 FEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIed 1035
Cdd:cd00075      1 LEQVLSNLLDNALKYSPPGGTIEISL-------------------RQEGDGVVLEVEDNGPGIPEEDLERIFERFYRG-- 59
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1800169395 1036 RKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLF 1078
Cdd:cd00075     60 DKSREGGGTGLGLAIVRRIVEAHGGRITVESEPGGGTTFTVTL 102
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
813-1226 4.23e-28

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 123.31  E-value: 4.23e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  813 IIKKKNLEQALVYEHLKQQQAEefhQTKMRMFTNFSHELRTPLTLIISPLqELLRRNEFNTGIR-NKLDLIYNNSQRLLL 891
Cdd:PRK09959   688 ITETRDLIHALEVERNKAINAT---VAKSQFLATMSHEIRTPISSIMGFL-ELLSGSGLSKEQRvEAISLAYATGQSLLG 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  892 LVNQLMDLRKNQAGKMQLKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGG-EVGIVAWFDKSLFEKVVFNLLSNAFKY 970
Cdd:PRK09959   764 LIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPDHYLVKIDPQAFKQVLSNLLSNALKF 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  971 TQAGGEIVLSvaklklkdvpagqrkELESLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEdrKAKDVAGTGIGLSL 1050
Cdd:PRK09959   844 TTEGAVKITT---------------SLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTS--AGRQQTGSGLGLMI 906
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1051 TQSIVRLHHGTIRVENNARGGATFHVLFPIdrrvyteEEIDREAAdrvvmdviPSTTAPEVFGLEKKYTVLLVEDNEEVR 1130
Cdd:PRK09959   907 CKELIKNMQGDLSLESHPGIGTTFTITIPV-------EISQQVAT--------VEAKAEQPITLPEKLSILIADDHPTNR 971
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1131 SYVRECLDP-HFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTARSMVMHIKEGF 1209
Cdd:PRK09959   972 LLLKRQLNLlGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLRE--QNSSLPIWGLTANAQANEREKGL 1049
                          410
                   ....*....|....*..
gi 1800169395 1210 SAGADDYIVKPFNMDVL 1226
Cdd:PRK09959  1050 SCGMNLCLFKPLTLDVL 1066
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1120-1221 1.43e-27

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: 107.98  E-value: 1.43e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTA 1198
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYrVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                           90       100
                   ....*....|....*....|...
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPF 1221
Cdd:cd19920     81 LTDTEDKVKGFELGAVDYITKPF 103
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1119-1221 5.45e-27

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: 106.43  E-value: 5.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMT 1197
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEGYeVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPF 1221
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
PRK15347 PRK15347
two component system sensor kinase;
831-1220 6.55e-27

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 119.36  E-value: 6.55e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  831 QQAEEFHQTKMRMFTNFSHELRTPLTLIISPLqELLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLK 910
Cdd:PRK15347   389 QRAEQANKRKSEHLTTISHEIRTPLNGVLGAL-ELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLS 467
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  911 IAKDDICSFVMEIYCAFNQIASGKEIRFR-YEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGeIVLSVAklklkdv 989
Cdd:PRK15347   468 LEETALLPLLDQAMLTIQGPAQSKSLTLRtFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG-IRLRVK------- 539
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  990 pagqrkeleslSEDTELVHLfVSDTGKGIPEEEMKNIFAPFYQIEDRKakdvAGTGIGLSLTQSIVRLHHGTIRVENNAR 1069
Cdd:PRK15347   540 -----------RHEQQLCFT-VEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFSTPG 603
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1070 GGATFHVLFPIDrrVYTEEEI-----------------------------DREAAD--------RVVMDVIPSTTAPEVf 1112
Cdd:PRK15347   604 VGSCFSLVLPLN--EYAPPEPlkgelsaplalhrqlsawgitcqpghqnpALLDPElaylpgrlYDLLQQIIQGAPNEP- 680
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1113 gLEK------KYTVLLVEDNEEVRSYV-RECLDPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKED 1185
Cdd:PRK15347   681 -VINlplqpwQLQILLVDDVETNRDIIgMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDD 759
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1800169395 1186 L--RTGHIPVILMTARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:PRK15347   760 PnnLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKP 796
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
846-1079 1.24e-26

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 115.18  E-value: 1.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  846 NFS----HELRTPLTLIISPLQELLRRNEFNTGIRnklDLIYNNS---QRLLLLVNQLMDLRKNQAGKMQLKIAKDDICS 918
Cdd:TIGR01386  243 QFSadlaHELRTPLTNLLGQTQVALSQPRTGEEYR---EVLESNLeelERLSRMVSDMLFLARADNGQLALERVRLDLAA 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  919 FVMEIYCAFNQIA--SGKEIRFRYEGGEVGivawfDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVAklklkdvpagqrke 996
Cdd:TIGR01386  320 ELAKVAEYFEPLAeeRGVRIRVEGEGLVRG-----DPQMFRRAISNLLSNALRHTPDGGTITVRIE-------------- 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  997 leslsEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVEnNARGGATFHV 1076
Cdd:TIGR01386  381 -----RRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAE-SPDGKTRFIL 454

                   ...
gi 1800169395 1077 LFP 1079
Cdd:TIGR01386  455 RFP 457
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1119-1220 1.06e-25

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 102.54  E-value: 1.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLD---PHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVIL 1195
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILEweaGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDP--DTKIII 78
                           90       100
                   ....*....|....*....|....*
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:COG4753     79 LSGYSDFEYAQEAIKLGADDYLLKP 103
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1120-1234 1.33e-25

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: 102.85  E-value: 1.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLD-PHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghIPVILMTA 1198
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRfEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGND--LPILVLTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17627     79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
952-1082 1.57e-25

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: 102.45  E-value: 1.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslsEDTELVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEITVTL--------------------SEGGELTLTVEDNGIGIPPEDLPRIFEPFS 61
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1800169395 1032 QIEDRKAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDR 1082
Cdd:pfam02518   62 TADKRGGG---GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1281-1369 2.69e-25

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 106.79  E-value: 2.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1281 LNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCFKSVYGCSPT 1360
Cdd:COG2207    169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                   ....*....
gi 1800169395 1361 EFLMEHKKE 1369
Cdd:COG2207    249 EYRKRLRAR 257
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1116-1242 5.00e-25

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 101.97  E-value: 5.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1116 KKYTVLLVEDNEEV----RSYVREcLDPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHI 1191
Cdd:COG4565      2 KMIRVLIVEDDPMVaellRRYLER-LPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGP--DV 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1800169395 1192 PVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREKLRS 1242
Cdd:COG4565     79 DVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1120-1234 6.73e-25

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: 100.86  E-value: 6.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTA 1198
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
956-1079 8.50e-25

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: 100.26  E-value: 8.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  956 FEKVVFNLLSNAFKYTQAGgEIVLSVaklklkdvpagqrkELESLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIED 1035
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEG-EVTLRV--------------SLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADS 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1800169395 1036 RKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16922     66 STTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
849-1082 2.08e-24

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 110.06  E-value: 2.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  849 HELRTPLTLIISPLQeLLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDL-RKNQAgkmqlKIAKDDICSFVMEIYCAF 927
Cdd:PRK11360   399 HEIRNPLTAIRGYVQ-IWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFsRPRES-----QWQPVSLNALVEEVLQLF 472
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  928 NQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkelESLSEDTelV 1007
Cdd:PRK11360   473 QTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRT----------------WQYSDGQ--V 534
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800169395 1008 HLFVSDTGKGIPEEEMKNIFAPFYQIedrKAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDR 1082
Cdd:PRK11360   535 AVSIEDNGCGIDPELLKKIFDPFFTT---KAK---GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINP 603
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
844-1070 2.67e-24

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 108.32  E-value: 2.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  844 FT---NFS----HELRTPLTLIISPLQELLRRNEfntgIRNKL-DLIYNN---SQRLLLLVNQLMDLRknQAGKMQLKIA 912
Cdd:PRK09835   259 FTrqsNFSadiaHEIRTPITNLITQTEIALSQSR----SQKELeDVLYSNleeLTRMAKMVSDMLFLA--QADNNQLIPE 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  913 KD--DICSFVMEIYCAFNQIASGKEIRFRYEGgeVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSvaklklkdvp 990
Cdd:PRK09835   333 KKmlDLADEVGKVFDFFEAWAEERGVELRFVG--DPCQVAGDPLMLRRAISNLLSNALRYTPAGEAITVR---------- 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  991 agqrkelesLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARG 1070
Cdd:PRK09835   401 ---------CQEVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDARG 471
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
842-1074 2.83e-24

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 109.46  E-value: 2.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  842 RMF-TNFSHELRTPLTLIISPLQELlrrnefNTG-IRNK------LDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAK 913
Cdd:NF033092   373 REFvANVSHELRTPLTTMRSYLEAL------ADGaWKDPelaprfLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKEW 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  914 DDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLsvaklklkdvpagq 993
Cdd:NF033092   447 VNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGTITF-------------- 512
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  994 rkeleSLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGAT 1073
Cdd:NF033092   513 -----RLLETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTT 587

                   .
gi 1800169395 1074 F 1074
Cdd:NF033092   588 I 588
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
1119-1234 3.45e-24

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


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 102.41  E-value: 3.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMT 1197
Cdd:TIGR02154    4 RILVVEDEPAIRELIAYNLEKAGYdVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPIIMLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:TIGR02154   84 ARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVL 120
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1119-1231 3.86e-24

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: 98.38  E-value: 3.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMT 1197
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:cd17548     81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1280-1363 4.03e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 97.24  E-value: 4.03e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  1280 ELNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCFKSVYGCSP 1359
Cdd:smart00342    1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                    ....
gi 1800169395  1360 TEFL 1363
Cdd:smart00342   81 SEYR 84
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
841-1078 8.63e-24

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 104.21  E-value: 8.63e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  841 MR--MFTNFSHELRTPLTLIISPLQELLRRNEFNTGIRNK-LDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDIC 917
Cdd:TIGR02966  113 MRrdFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWNRaLEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMP 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  918 SFVMEIYCAFNQIASGKEIRFRYE-GGEVGIVAwfDKSLFEKVVFNLLSNAFKYTQAGGEIVLsvaklklkdvpagqrke 996
Cdd:TIGR02966  193 ALLDHLRDEAEALSQGKNHQITFEiDGGVDVLG--DEDELRSAFSNLVSNAIKYTPEGGTITV----------------- 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  997 leSLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHV 1076
Cdd:TIGR02966  254 --RWRRDGGGAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSF 331

                   ..
gi 1800169395 1077 LF 1078
Cdd:TIGR02966  332 IF 333
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1120-1234 1.39e-23

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: 97.06  E-value: 1.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCtlikEDLRT-GHIPVILMT 1197
Cdd:cd17622      3 ILLVEDDPKLARLIADFLESHgFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLC----RDLRPkYQGPILLLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1198 ARSMVM-HIKeGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17622     79 ALDSDIdHIL-GLELGADDYVVKPVEPAVLLARLRALL 115
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1121-1234 3.62e-23

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: 95.75  E-value: 3.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1121 LLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELctlIKEdLRTGHI--PVILMT 1197
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEV---LKS-LREEGIetPVLLLT 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17625     77 ALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1120-1234 8.68e-23

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: 94.75  E-value: 8.68e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLrtgHIPVILMTA 1198
Cdd:cd19939      2 ILIVEDELELARLTRDYLIKAgLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS---HVPILMLTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd19939     79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
PRK09303 PRK09303
histidine kinase;
827-1082 2.46e-22

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 100.80  E-value: 2.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  827 HLKQQQAEEFHQTK-----MRMFtnfSHELRTPLT---LIISPLQelLRRNEFNTGIRNKL-----DLIYNNSQRLLLLV 893
Cdd:PRK09303   136 VLRQENETLLEQLKfkdrvLAML---AHDLRTPLTaasLALETLE--LGQIDEDTELKPALieqlqDQARRQLEEIERLI 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  894 NQLMDLRKNQAGKMQLKIAKDDICSFVMEIYcafnqiasgKEIRFRYEGGEVGIVA---------WFDKSLFEKVVFNLL 964
Cdd:PRK09303   211 TDLLEVGRTRWEALRFNPQKLDLGSLCQEVI---------LELEKRWLAKSLEIQTdipsdlpsvYADQERIRQVLLNLL 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  965 SNAFKYTQAGGEIVLSVaklklkdvpagqrkelesLSEDTELVHLFVSDTGKGIPEEEMKNIFapfyqiEDR----KAKD 1040
Cdd:PRK09303   282 DNAIKYTPEGGTITLSM------------------LHRTTQKVQVSICDTGPGIPEEEQERIF------EDRvrlpRDEG 337
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1800169395 1041 VAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDR 1082
Cdd:PRK09303   338 TEGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLPVYR 379
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1120-1227 4.59e-22

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: 92.53  E-value: 4.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTG-HIPVILMT 1197
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYeVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGrRTPIIALT 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLI 1227
Cdd:cd17546     81 ANALEEDREKCLEAGMDDYLSKPVKLDQLK 110
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
952-1079 5.30e-22

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 92.17  E-value: 5.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVAKLklkdvpagqrkeleslseDTELVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKF------------------RLNRFLLTVSDSGPGIPPNLREEIFERFR 62
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1032 QIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16925     63 QGDGSSTRAHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1121-1234 5.44e-22

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: 92.34  E-value: 5.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1121 LLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTAR 1199
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEgYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1800169395 1200 SMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd19937     81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1120-1238 5.66e-22

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: 92.40  E-value: 5.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF----VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVIL 1195
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIDWEELgfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYP--DIKIII 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1196 MTArsmvmH-----IKEGFSAGADDYIVKPFNMDVLIYRIRNILASRE 1238
Cdd:cd17536     79 LSG-----YddfeyAQKAIRLGVVDYLLKPVDEEELEEALEKAKEELD 121
PRK10490 PRK10490
sensor protein KdpD; Provisional
848-1096 7.29e-22

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 102.81  E-value: 7.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  848 SHELRTPLTLIISPLQELLrrnefntgirnkLDLIYNNS----------QRLL---LLVNQLMDLRKNQAGKMQLK---I 911
Cdd:PRK10490   672 SHDLRTPLTVLFGQAEILT------------LDLASEGSpharqaseirQQVLnttRLVNNLLDMARIQSGGFNLRkewL 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  912 AKDDIcsfvmeIYCAFNQIA---SGKEIRFRYEGGEVGIvaWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkd 988
Cdd:PRK10490   740 TLEEV------VGSALQMLEpglSGHPINLSLPEPLTLI--HVDGPLFERVLINLLENAVKYAGAQAEIGIDA------- 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  989 vpagqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQieDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNA 1068
Cdd:PRK10490   805 ------------HVEGERLQLDVWDNGPGIPPGQEQLIFDKFAR--GNKESAIPGVGLGLAICRAIVEVHGGTIWAENRP 870
                          250       260
                   ....*....|....*....|....*...
gi 1800169395 1069 RGGATFHVLFPIDrrvyTEEEIDREAAD 1096
Cdd:PRK10490   871 EGGACFRVTLPLE----TPPELEEFHED 894
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1120-1220 1.73e-21

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 90.51  E-value: 1.73e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTA 1198
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLeDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                           90       100
                   ....*....|....*....|..
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd19927     81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1118-1234 2.40e-21

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: 90.80  E-value: 2.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEVRSYVRECLDPHFF--VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHipVIL 1195
Cdd:cd17542      1 KKVLIVDDAAFMRMMLKDILTKAGYevVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK--VIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17542     79 CSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
pleD PRK09581
response regulator PleD; Reviewed
1141-1231 3.19e-21

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 98.43  E-value: 3.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1141 FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:PRK09581    27 YTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKP 106
                           90
                   ....*....|.
gi 1800169395 1221 FNMDVLIYRIR 1231
Cdd:PRK09581   107 INDVALFARVK 117
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1120-1233 6.85e-21

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: 89.50  E-value: 6.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEiVLDKYPDI--VVSDIMMPRKDGLELCTLIKEDLRTGHIPVI-- 1194
Cdd:cd17544      3 VLVVDDSATSRNHLRALLRRHNFqVLEAANGQEALE-VLEQHPDIklVITDYNMPEMDGFELVREIRKKYSRDQLAIIgi 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1800169395 1195 ------LMTARsmvmHIKegfsAGADDYIVKPFNMDVLIYRI-RNI 1233
Cdd:cd17544     82 sasgdnALSAR----FIK----AGANDFLTKPFLPEEFYCRVtQNL 119
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
831-1079 8.75e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.20  E-value: 8.75e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  831 QQAEEFHQT-KMR--MFTNFSHELRTPLTLI---ISPLQELLRRNEfntgiRNKLDLIYNNSQRLLLLVNQLMDLRKNQA 904
Cdd:NF012163   228 QLASTLEKNeQMRrdFMADISHELRTPLAVLraeLEAIQDGIRKFT-----PESLDSLQAEVGTLTKLVDDLHDLSMSDE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  905 GKMQLKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVaWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVAKl 984
Cdd:NF012163   303 GALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSSLV-FGDRDRLMQLFNNLLENSLRYTDSGGSLHISASQ- 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  985 klkdVPAGqrkeleslsedtelVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRV 1064
Cdd:NF012163   381 ----RPKE--------------VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHA 442
                          250
                   ....*....|....*
gi 1800169395 1065 ENNARGGATFHVLFP 1079
Cdd:NF012163   443 AHSPLGGLRIVVTLP 457
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1120-1234 1.40e-20

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: 88.31  E-value: 1.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCtlikEDLRTG--HIPVILM 1196
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLL----RRWRRQgqSLPVLIL 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17624     77 TARDGVDDRVAGLDAGADDYLVKPFALEELLARLRALL 114
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1120-1220 1.47e-20

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: 87.88  E-value: 1.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVL-DKYpDIVVSDIMMPRKDGLELCtlikEDLRTGHI--PVIL 1195
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLtEEGYAVDVAYDGEDGLHLALtNEY-DLIILDVMLPGLDGLEVL----RRLRAAGKqtPVLM 75
                           90       100
                   ....*....|....*....|....*
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd19935     76 LTARDSVEDRVKGLDLGADDYLVKP 100
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1120-1234 2.61e-20

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 91.40  E-value: 2.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEiVLDKYPDIVVSDIMMPRKDGLElcTLikEDLRTGH-IPVILMT 1197
Cdd:PRK10955     4 ILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQALD-LLDDSIDLLLLDVMMPKKNGID--TL--KELRQTHqTPVIMLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK10955    79 ARGSELDRVLGLELGADDYLPKPFNDRELVARIRAIL 115
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1120-1227 5.14e-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: 86.74  E-value: 5.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTA 1198
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                           90       100
                   ....*....|....*....|....*....
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLI 1227
Cdd:cd17580     81 YGQPEDRERALEAGFDAHLVKPVDPDELI 109
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
1114-1238 5.92e-20

Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 91.40  E-value: 5.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1114 LEKKYTVLLVEDNEEVRSYVRECLD--PHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGH 1190
Cdd:COG5801      1 MMEKIKVLIADDNREFCELLEEYLSsqPDMEVVgVAYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLREMNLEKR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1800169395 1191 IPVILMTA---RSMvmhIKEGFSAGADDYIVKPFNMDVLIYRIRNILASRE 1238
Cdd:COG5801     81 PKVIMLTAfgqEDI---TQRAVELGADYYILKPFDLDVLAERIRQLAGGKA 128
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1120-1234 9.28e-20

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: 86.24  E-value: 9.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF--VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMT 1197
Cdd:cd19923      3 VLVVDDFSTMRRIIKNLLKELGFnnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVT 82
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd19923     83 AEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
831-1104 1.35e-19

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 93.94  E-value: 1.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  831 QQAEEFHQTKMRMFTNFSHELRTPLTlIISPLQELL--RRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQ 908
Cdd:NF040691   262 RQLEELSRLQQRFVSDVSHELRTPLT-TIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAE 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  909 LKIAKDDICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQaGGEIVLSVAklklkd 988
Cdd:NF040691   341 LDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGE-GKPVVVTVA------ 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  989 vpagqrkeleslSEDTElVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNA 1068
Cdd:NF040691   414 ------------QDDTA-VAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRP 480
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1800169395 1069 RGGATFHVLFPidrrvyteeeidREAADRVVMDVIP 1104
Cdd:NF040691   481 GQGSQFRLTLP------------RVAGDRLTTSPLP 504
orf27 CHL00148
Ycf27; Reviewed
1113-1239 1.45e-19

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 89.39  E-value: 1.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1113 GLEKKYTVLLVEDNeevrSYVRECLDPH-----FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKedlR 1187
Cdd:CHL00148     2 MENSKEKILVVDDE----AYIRKILETRlsiigYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR---K 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1800169395 1188 TGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREK 1239
Cdd:CHL00148    75 ESDVPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNK 126
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1117-1235 2.20e-19

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 85.23  E-value: 2.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1117 KYTVLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghIPVIL 1195
Cdd:COG5803      2 MKKILIVDDQAGIRMLLKEVLkKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPD--IPVIM 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILA 1235
Cdd:COG5803     80 MTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
HTH_18 pfam12833
Helix-turn-helix domain;
1286-1363 2.21e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.79  E-value: 2.21e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800169395 1286 ICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLE-SDYSVSEISTCVGFNSHAYFTQCFKSVYGCSPTEFL 1363
Cdd:pfam12833    1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEdTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1119-1234 4.06e-19

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: 84.33  E-value: 4.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLD-PHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDlrTGHIPVILMT 1197
Cdd:cd17615      1 RVLVVDDEPNITELLSMALRyEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17615     79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL 115
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1120-1231 4.13e-19

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: 84.06  E-value: 4.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYV-----RECLDPHFfvleADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDlrtGHIPVI 1194
Cdd:cd17626      3 ILVVDDDAALAEMIgivlrGEGFDPAF----CGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE---SGVPIV 75
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1195 LMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:cd17626     76 MLTAKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1120-1231 4.14e-19

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: 84.26  E-value: 4.14e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghIPVILMTA 1198
Cdd:cd19934      1 LLLVEDDALLAAQLKEQLsDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--TPVLILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:cd19934     79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
962-1079 4.67e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 83.53  E-value: 4.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  962 NLLSNAFKYtqaggeivlSVAKLKLkdvpagqrkeleSLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDV 1041
Cdd:cd16949      7 NVLRNALRY---------SPSKILL------------DISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRES 65
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1042 AGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16949     66 GGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1119-1233 5.36e-19

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: 83.81  E-value: 5.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMT 1197
Cdd:cd17554      2 KILVVDDEENIRELYKEELeDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIICT 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSmvmHIKEGFSA-GADDYIVKPFNMDVLIYRIRNI 1233
Cdd:cd17554     80 AYS---EYKSDFSSwAADAYVVKSSDLTELKETIKRL 113
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1120-1234 5.68e-19

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: 83.89  E-value: 5.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLEA-DNGETAFEIVLDKYPDIVVSDIMMPRKDGLElctLIKEdLRTGH-IPVILMT 1197
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAaHDGEQGLAALLEGSPDLVVLDVMLPKMNGLD---VLKE-LRKTSqVPVLMLT 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17623     77 ARGDDIDRILGLELGADDYLPKPFNPRELVARIRAIL 113
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
842-1071 7.29e-19

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 91.53  E-value: 7.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  842 RMFTNFSHELRTPLTliisPLQ---ELLRRNEfntGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAgKMQLKIAKDDICS 918
Cdd:PRK09470   245 RLLSDISHELRTPLT----RLQlatALLRRRQ---GESKELERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANS 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  919 FVMEIY--CAFNQIASGKEIRFRYEGGEvgivaWF---DKSLFEKVVFNLLSNAFKYTQAggEIVLSvaklklkdvpagq 993
Cdd:PRK09470   317 LWSEVLedAKFEAEQMGKSLTVSAPPGP-----WPingNPNALASALENIVRNALRYSHT--KIEVA------------- 376
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800169395  994 rkelesLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGG 1071
Cdd:PRK09470   377 ------FSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEDSPLGG 448
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
954-1080 1.22e-18

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: 82.47  E-value: 1.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  954 SLFEKVVFNLLSNAFKYTQAGGEIVLSVAklklkdvpagqrkelesLSEDTELVHlfVSDTGKGIPEEEMKNIFAPFYQi 1033
Cdd:cd16943      2 SQLNQVLLNLLVNAAQAMEGRGRITIRTW-----------------AHVDQVLIE--VEDTGSGIDPEILGRIFDPFFT- 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1034 edrkAKDVA-GTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPI 1080
Cdd:cd16943     62 ----TKPVGeGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
Y_Y_Y pfam07495
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ...
721-785 1.92e-18

Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a family of two component regulators. However they are also found tandemly repeated in Swiss:Q891H4 without other signal conduction domains being present. It's named after the conserved tyrosines found in the alignment. The exact function is not known.


Pssm-ID: 400051 [Multi-domain]  Cd Length: 65  Bit Score: 80.47  E-value: 1.92e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800169395  721 NYVCSDLNQYAYRLKGYDKDWNYVGNRKEAYYTNLGPGKYVFEVKASNNDGIWNDEIRTLSIIVH 785
Cdd:pfam07495    1 NYDGPENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSYDDASLNFTIL 65
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1120-1234 2.86e-18

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 81.83  E-value: 2.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL--DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMT 1197
Cdd:cd17552      4 ILVIDDEEDIREVVQACLekLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17552     84 AKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
862-1083 3.86e-18

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 88.37  E-value: 3.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  862 LQELLRRN--EFntgiRNKLDLIY-----NNSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDICSFVMeiycAFNQIASGK 934
Cdd:COG3290    189 LAEALRAQrhDF----RNHLHTISgllqlGEYDEALEYIDEISEELQELIDSLLSRIGNPVLAALLL----GKAARARER 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  935 EIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEivlsvaklklkdvpagQRKELE-SLSEDTELVHLFVSD 1013
Cdd:COG3290    261 GIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIEAVEKLPE----------------EERRVElSIRDDGDELVIEVED 324
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1014 TGKGIPEEEMKNIFAPFYQIedrkaKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRR 1083
Cdd:COG3290    325 SGPGIPEELLEKIFERGFST-----KLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
849-1082 5.89e-18

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 88.75  E-value: 5.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  849 HELRTPLTLIISPLqELLR-------RNEFNTGIRNKldliynnSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDICSFVM 921
Cdd:PRK11100   265 HELKSPLAAIRGAA-ELLQedpppedRARFTGNILTQ-------SARLQQLIDRLLELARLEQRQELEVLEPVALAALLE 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  922 EIYCAFNQIASGKEIRFRYEGGEVGIVAwfDKSLFEKVVFNLLSNAFKYTQAGGEIVLSvaklklkdvpagqrkelesLS 1001
Cdd:PRK11100   337 ELVEAREAQAAAKGITLRLRPDDARVLG--DPFLLRQALGNLLDNAIDFSPEGGTITLS-------------------AE 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1002 EDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEdRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPID 1081
Cdd:PRK11100   396 VDGEQVALSVEDQGPGIPDYALPRIFERFYSLP-RPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRH 474

                   .
gi 1800169395 1082 R 1082
Cdd:PRK11100   475 F 475
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1114-1244 8.96e-18

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 87.98  E-value: 8.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1114 LEKKYTVLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKE-DLRTghi 1191
Cdd:PRK11361     1 MTAINRILIVDDEDNVRRMLSTAFALQgFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRShETRT--- 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1800169395 1192 PVILMTARSMVMHIKEGFSAGADDYIVKPFNMD---VLIYRIRNILASREKLRSLY 1244
Cdd:PRK11361    78 PVILMTAYAEVETAVEALRCGAFDYVIKPFDLDelnLIVQRALQLQSMKKEIRHLH 133
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
821-1178 1.53e-17

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 88.81  E-value: 1.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  821 QALVYEHLKQQ-QAEEFHQTKMRMFTNFSHELRTPLTLIISPLQeLLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDL 899
Cdd:PRK11466   424 QELVIEHRQARaEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQ-LLADNPALNAQRDDLRAITDSGESLLTILNDILDY 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  900 RKNQAGKMQLKIAKDDICSfvMEIYCAFNQIASGK----EIRFRYEGGEVgIVAWF--DKSLFEKVVFNLLSNAFKYTQA 973
Cdd:PRK11466   503 SAIEAGGKNVSVSDEPFEP--RPLLESTLQLMSGRvkgrPIRLATDIADD-LPTALmgDPRRIRQVITNLLSNALRFTDE 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  974 GgEIVLSvaklklkdvpagqrkeleSLSEDTELVhLFVSDTGKGIPEEEMKNIFAPFYQIEDRKakdvAGTGIGLSLTQS 1053
Cdd:PRK11466   580 G-SIVLR------------------SRTDGEQWL-VEVEDSGCGIDPAKLAEIFQPFVQVSGKR----GGTGLGLTISSR 635
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1054 IVRLHHGTIRVENNARGGATFHVLFPIDRRVYTEEEIDREAADRVvmdvipsttapevfGLEkkytVLLVEDNEEVRSYV 1133
Cdd:PRK11466   636 LAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAVRLD--------------GLR----LLLIEDNPLTQRIT 697
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1800169395 1134 RECLDPHFF-VLEADNGETAFEIVLDKYP-DIVVSDIMMPRKDGLEL 1178
Cdd:PRK11466   698 AEMLNTSGAqVVAVGNAAQALETLQNSEPfAAALVDFDLPDYDGITL 744
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1120-1234 1.94e-17

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: 79.39  E-value: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCtliKEDLRTGHIPVILMTA 1198
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEGYeVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVC---REVRKTSNVPIIMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17614     78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
828-1080 2.11e-17

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 87.09  E-value: 2.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  828 LKQQQAEEFHQTKM----RMFTNFSHELRTPLTLIISPLQ----ELLRRNEFNTGIRNKLDliynnsqRLLLLVNQLMDL 899
Cdd:COG5805    271 KKEAEELMARSEKLsiagQLAAGIAHEIRNPLTSIKGFLQllqpGIEDKEEYFDIMLSELD-------RIESIISEFLAL 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  900 RKNQAGKMQLKIAKDDICSFVMEIYCafNQIASGKEIRFRYEGGEVGIVAwfDKSLFEKVVFNLLSNAFKYTQAGGEIVL 979
Cdd:COG5805    344 AKPQAVNKEKENINELIQDVVTLLET--EAILHNIQIRLELLDEDPFIYC--DENQIKQVFINLIKNAIEAMPNGGTITI 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  980 SVAklklkdvpagqrkeleslSEDTElVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRkakdvaGTGIGLSLTQSIVRLHH 1059
Cdd:COG5805    420 HTE------------------EEDNS-VIIRVIDEGIGIPEERLKKLGEPFFTTKEK------GTGLGLMVSYKIIENHN 474
                          250       260
                   ....*....|....*....|.
gi 1800169395 1060 GTIRVENNARGGATFHVLFPI 1080
Cdd:COG5805    475 GTIDIDSKVGKGTTFTITLPL 495
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1119-1233 2.43e-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: 79.77  E-value: 2.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEE----VRSYVRECLDPHFfVLEADNGETAFEIVL--DKY-----PDIVVSDIMMPRKDGLELCTLIKEDLR 1187
Cdd:cd17557      1 TILLVEDNPGdaelIQEAFKEAGVPNE-LHVVRDGEEALDFLRgeGEYadaprPDLILLDLNMPRMDGFEVLREIKADPD 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1800169395 1188 TGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNI 1233
Cdd:cd17557     80 LRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSL 125
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
952-1079 3.36e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 78.66  E-value: 3.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVAKlklkdVPAGqrkeleslsedtelVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQ-----TPQE--------------VRLDVEDSAPGVSDDQLARLFERFY 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1032 QIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16946     62 RVESSRNRASGGSGLGLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
950-1071 6.75e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 77.83  E-value: 6.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  950 WFDKSLFEKVVFNLLSNAFKYTqaggeivlsvaklklkdvPAGQRKELESLSEDTELVHlfVSDTGKGIPEEEMKNIFAP 1029
Cdd:cd16940      8 QGDALLLFLLLRNLVDNAVRYS------------------PQGSRVEIKLSADDGAVIR--VEDNGPGIDEEELEALFER 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1800169395 1030 FYQIEDRKAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGG 1071
Cdd:cd16940     68 FYRSDGQNYG---GSGLGLSIVKRIVELHGGQIFLGNAQGGG 106
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
1270-1362 7.53e-17

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 83.28  E-value: 7.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1270 EVIERNIANPeLNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQ 1349
Cdd:COG4977    217 AWMEANLEEP-LSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRR 295
                           90
                   ....*....|...
gi 1800169395 1350 CFKSVYGCSPTEF 1362
Cdd:COG4977    296 AFRRRFGVSPSAY 308
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
1120-1237 1.06e-16

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: 77.92  E-value: 1.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghIPVILMTA 1198
Cdd:cd17549      1 VLLVDDDADVREALQQTLELAgFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPD--LPVILITG 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1800169395 1199 R---SM-VMHIKegfsAGADDYIVKPFNMDVLIYRIRNILASR 1237
Cdd:cd17549     79 HgdvPMaVEAMR----AGAYDFLEKPFDPERLLDVVRRALEKR 117
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1116-1243 1.15e-16

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 79.62  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1116 KKYTVLLVEDNEEVRSYVRECLDPHFF--VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtghIPV 1193
Cdd:COG3707      2 RGLRVLVVDDEPLRRADLREGLREAGYevVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APV 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1800169395 1194 ILMTARSMVMHIKEGFSAGADDYIVKPFN-------MDVLIYRIRNILASREKLRSL 1243
Cdd:COG3707     79 ILLTAYSDPELIERALEAGVSAYLVKPLDpedllpaLELALARFRELRALRRELAKL 135
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
1120-1231 1.39e-16

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 80.30  E-value: 1.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNE---EVRSYV--RECLDPHFfvleADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKedlRTGHIPVI 1194
Cdd:NF040689     1 ILVVDDDPalaEMLGIVlrAEGFETVF----CADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIR---AESGVPII 73
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1195 LMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:NF040689    74 MLTAKSDTVDVVRGLEAGADDYVVKPFKPKELVARIR 110
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1120-1234 1.51e-16

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: 76.94  E-value: 1.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDP-HFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLrtgHIPVILMTA 1198
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQIS---NVPIIFISS 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd18159     78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
1120-1235 1.54e-16

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: 76.77  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVILM-- 1196
Cdd:cd17550      1 ILIVDDEEDIRESLSGILeDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYP--DLPVIMIsg 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1800169395 1197 -----TArsmVMHIKEgfsaGADDYIVKPFNMDVLIYRIRNILA 1235
Cdd:cd17550     79 hgtieTA---VKATKL----GAYDFIEKPLSLDRLLLTIERALE 115
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1120-1220 2.59e-16

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: 76.26  E-value: 2.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDP-HFFVLEADNGETAFEI---------VLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTG 1189
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNlGFEIAEAVDGEEALNKlenlakegnDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1800169395 1190 HIPVILMTARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
957-1079 4.02e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 75.13  E-value: 4.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  957 EKVVFNLLSNAFKYTQAGGEivlsvaklklkdvpagQRKEL--ESLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIE 1034
Cdd:cd16920      2 QQVLINLVRNGIEAMSEGGC----------------ERRELtiRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTK 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1800169395 1035 drkakdVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16920     66 ------SEGLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
envZ PRK09467
osmolarity sensor protein; Provisional
848-1082 6.34e-16

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 81.88  E-value: 6.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  848 SHELRTPLTLI------ISPLQELLRRnefntGIRNKLDLIyNNsqrlllLVNQLMD-LRKNQAGKMQLkiakDDICSFV 920
Cdd:PRK09467   237 SHDLRTPLTRIrlatemMSEEDGYLAE-----SINKDIEEC-NA------IIEQFIDyLRTGQEMPMEM----ADLNALL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  921 MEIYCAfnqiASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTqaGGEIVLSvaklklkdvpagqrkelesL 1000
Cdd:PRK09467   301 GEVIAA----ESGYEREIETALQPGPIEVPMNPIAIKRALANLVVNAARYG--NGWIKVS-------------------S 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1001 SEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEdrKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPI 1080
Cdd:PRK09467   356 GTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPL 433

                   ..
gi 1800169395 1081 DR 1082
Cdd:PRK09467   434 TT 435
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1120-1235 6.52e-16

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


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 75.24  E-value: 6.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVR---ECLDPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILM 1196
Cdd:cd17535      1 VLIVDDHPLVREGLRrllESEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIVL 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILA 1235
Cdd:cd17535     79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1119-1234 9.57e-16

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: 74.72  E-value: 9.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDN----EEVRSYVR-ECLDPHFFvleaDNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKedlRTGHIPV 1193
Cdd:cd19938      1 RILIVEDEpklaQLLIDYLRaAGYAPTLL----AHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR---RFSDVPI 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1800169395 1194 ILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd19938     74 IMVTARVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
831-1226 2.07e-15

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 81.94  E-value: 2.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  831 QQAEEFHQTKmRMF-TNFSHELRTPLTLIISPLqELLRRNEFNTGIrNKLDLIYNNSQRLLL-LVNQLMDLRKNQAgkMQ 908
Cdd:PRK10841   438 QAAEQASQSK-SMFlATVSHELRTPLYGIIGNL-DLLQTKELPKGV-DRLVTAMNNSSSLLLkIISDILDFSKIES--EQ 512
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  909 LKI-AKDDICSFVM----------------EIYCAFN----QIASGKEIRFryeggevgivawfdkslfEKVVFNLLSNA 967
Cdd:PRK10841   513 LKIePREFSPREVInhitanylplvvkkrlGLYCFIEpdvpVALNGDPMRL------------------QQVISNLLSNA 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  968 FKYTQAGGeIVLSVAKlklkdvpagqrkeleslseDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIG 1047
Cdd:PRK10841   575 IKFTDTGC-IVLHVRV-------------------DGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLG 634
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1048 LSLTQSIVRLHHGTIRVENNARGGATFHVLFP-----------------------------------------IDRRVYT 1086
Cdd:PRK10841   635 LAICEKLINMMDGDISVDSEPGMGSQFTIRIPlygaqypqkkgveglqgkrcwlavrnasleqfletllqrsgIQVQRYE 714
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1087 EEEIDreAADRVVMDVIP------------------------------STTAP-EVFG-LEKKYTV-LLVEDNEEV---R 1130
Cdd:PRK10841   715 GQEPT--PEDVLITDDPVqkkwqgravitfcrrhigipleiapgewvhSTATPhELPAlLARIYRIeLESDDSANAlpsT 792
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1131 SYVRE--------CLDPH---------------FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLR 1187
Cdd:PRK10841   793 DKAVSdnddmmilVVDDHpinrrlladqlgslgYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGL 872
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1800169395 1188 TghIPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVL 1226
Cdd:PRK10841   873 T--LPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVL 909
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1120-1220 2.10e-15

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: 72.97  E-value: 2.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLElctLIKeDLRT-GHIPVILMT 1197
Cdd:cd17620      1 ILVIEDEPQIRRFLRTALEAHgYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLE---VIR-RLREwSAVPVIVLS 76
                           90       100
                   ....*....|....*....|...
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd17620     77 ARDEESDKIAALDAGADDYLTKP 99
PRK15479 PRK15479
transcriptional regulator TctD;
1120-1234 3.34e-15

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 76.30  E-value: 3.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLE-ADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTA 1198
Cdd:PRK15479     3 LLLAEDNRELAHWLEKALVQNGFAVDcVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRK--RGQTLPVLLLTA 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK15479    81 RSAVADRVKGLNVGADDYLPKPFELEELDARLRALL 116
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1120-1243 3.47e-15

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: 73.00  E-value: 3.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDP-HFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTA 1198
Cdd:cd17572      1 VLLVEDSPSLAALYQEYLSDeGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQE--RSLPTSVIVITA 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILasreKLRSL 1243
Cdd:cd17572     79 HGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNAL----KHRKL 119
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1117-1252 3.86e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 76.39  E-value: 3.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1117 KYTVLLVEDNEEVRSYVRECLDPHFF---VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPV 1193
Cdd:COG3279      1 MMKILIVDDEPLARERLERLLEKYPDlevVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDP--PPPI 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800169395 1194 ILMTArsmvmHIK---EGFSAGADDYIVKPFNMDvliyRIRNILasrEKLRSLYGKKFSPEA 1252
Cdd:COG3279     79 IFTTA-----YDEyalEAFEVNAVDYLLKPIDEE----RLAKAL---EKAKERLEAKAAAEA 128
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1118-1232 3.97e-15

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: 72.80  E-value: 3.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEVR----SYVREcldPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLelcTLIKEDLRTGHIPV 1193
Cdd:cd17619      1 PHILIVEDEPVTRatlkSYFEQ---EGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGL---SLTRELREQSEVGI 74
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1194 ILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRN 1232
Cdd:cd17619     75 ILVTGRDDEVDRIVGLEIGADDYVTKPFNPRELLVRAKN 113
cztR_silR_copR TIGR01387
heavy metal response regulator; Members of this family contain a response regulator receiver ...
1120-1242 5.58e-15

heavy metal response regulator; Members of this family contain a response regulator receiver domain (pfam00072) and an associated transcriptional regulatory region (pfam00486). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc. Most members encoded by genes adjacent to genes for encoding a member of the heavy metal sensor histidine kinase family (TIGRFAMs:TIGR01386), its partner in the two-component response regulator system. [Regulatory functions, DNA interactions]


Pssm-ID: 130454 [Multi-domain]  Cd Length: 218  Bit Score: 75.61  E-value: 5.58e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLE-ADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKedlRTGH-IPVILMT 1197
Cdd:TIGR01387    1 ILVVEDEQKTAEYLQQGLSESGYVVDaASNGRDGLHLALKDDYDLIILDVMLPGMDGWQILQTLR---RSGKqTPVLFLT 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREKLRS 1242
Cdd:TIGR01387   78 ARDSVADKVKGLDLGADDYLVKPFSFSELLARVRTLLRRSHSLNS 122
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1119-1234 5.60e-15

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: 72.33  E-value: 5.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLElctLIKEdLRtGH-----IP 1192
Cdd:cd17562      2 KILAVDDSASIRQMVSFTLrGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIE---LIKE-LR-KLpaykfTP 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1800169395 1193 VILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17562     77 ILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
PRK11517 PRK11517
DNA-binding response regulator HprR;
1120-1231 7.43e-15

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 75.32  E-value: 7.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLEA-DNGETAFEIVLDKYPDIVVSDIMMPRKDGLElctlIKEDLRTGH-IPVILMT 1197
Cdd:PRK11517     3 ILLIEDNQRTQEWVTQGLSEAGYVIDAvSDGRDGLYLALKDDYALIILDIMLPGMDGWQ----ILQTLRTAKqTPVICLT 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:PRK11517    79 ARDSVDDRVRGLDSGANDYLVKPFSFSELLARVR 112
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
958-1079 7.93e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 71.33  E-value: 7.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  958 KVVFNLLSNAFKYtqAGGEIvlsvaklKLKDVPAGQRKELEslsedtelvhlfVSDTGKGIPEEEMKNIFAPFYQIEdrK 1037
Cdd:cd16950      3 RVLSNLVDNALRY--GGGWV-------EVSSDGEGNRTRIQ------------VLDNGPGIAPEEVDELFQPFYRGD--N 59
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1800169395 1038 AKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16950     60 ARGTSGTGLGLAIVQRISDAHGGSLTLANRAGGGLCARIELP 101
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
1116-1233 1.11e-14

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: 75.60  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1116 KKYTVLLVEDNEEVRSYVRECL--DPHFFVLE-ADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIP 1192
Cdd:TIGR02875    1 HKIRIVIADDNKEFCNLLKEYLaaQPDMEVVGvAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARPR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1800169395 1193 VILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNI 1233
Cdd:TIGR02875   81 VIMLSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQL 121
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1119-1232 1.65e-14

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: 71.08  E-value: 1.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMT 1197
Cdd:cd17555      2 TILVIDDDEVVRESIAAYLeDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITK--ESPDTPVIVVS 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPF-NMDVLIYRIRN 1232
Cdd:cd17555     80 GAGVMSDAVEALRLGAWDYLTKPIeDLAVLEHAVRR 115
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1120-1234 1.70e-14

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 74.19  E-value: 1.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLE-ADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLikedLRTGH--IPVILM 1196
Cdd:PRK09836     3 LLIVEDEKKTGEYLTKGLTEAGFVVDlADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRM----LRSANkgMPILLL 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK09836    79 TALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL 116
resp_reg_YycF NF040534
response regulator YycF;
1143-1231 2.01e-14

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 74.37  E-value: 2.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1143 VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCtliKEDLRTGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFN 1222
Cdd:NF040534    27 VFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVC---REVRKKYDMPIIMLTAKDSEIDKVLGLELGADDYVTKPFS 103

                   ....*....
gi 1800169395 1223 MDVLIYRIR 1231
Cdd:NF040534   104 TRELIARVK 112
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1119-1231 2.41e-14

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: 70.55  E-value: 2.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVR----SYVRECldpHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKedlRTGHIPVI 1194
Cdd:cd17594      1 HVLVVDDDAAMRhlliLYLRER---GFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR---ARSDVPII 74
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1195 LMTARSMVMHIKE-GFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:cd17594     75 IISGDRRDEIDRVvGLELGADDYLAKPFGLRELLARVR 112
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
842-1079 2.45e-14

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 76.16  E-value: 2.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  842 RMFT-NFSHELRTPLTLIISPLqELLRRnefnTGIRNKLDLIynnsQRLLLL---VNQLMDL-RKNQAGKM----QLKIA 912
Cdd:PRK10755   138 RLFTaDVAHELRTPLAGIRLHL-ELLEK----QHHIDVAPLI----ARLDQMmhtVEQLLQLaRAGQSFSSghyqTVKLL 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  913 KDDICSFVMEiycaFNQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSvaklklkdvpag 992
Cdd:PRK10755   209 EDVILPSQDE----LSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTITIK------------ 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  993 qrkelesLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRkakdVAGTGIGLSLTQSIVRLHHGTIRVENNA-RGG 1071
Cdd:PRK10755   273 -------LSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMDSR----YGGIGLGLSIVSRITQLHHGQFFLQNRQeRSG 341

                   ....*...
gi 1800169395 1072 ATFHVLFP 1079
Cdd:PRK10755   342 TRAWVWLP 349
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1120-1234 4.09e-14

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 73.21  E-value: 4.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFV-LEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTA 1198
Cdd:PRK10161     5 ILVVEDEAPIREMVCFVLEQNGFQpVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK10161    85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
ompR PRK09468
osmolarity response regulator; Provisional
1118-1234 6.49e-14

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 73.08  E-value: 6.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDlrTGHIPVILM 1196
Cdd:PRK09468     6 YKILVVDDDMRLRALLERYLTEQgFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQ--NNPTPIIML 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1197 TAR-SMVMHIKeGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK09468    84 TAKgEEVDRIV-GLEIGADDYLPKPFNPRELLARIRAVL 121
PRK10610 PRK10610
chemotaxis protein CheY;
1115-1240 7.34e-14

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 69.62  E-value: 7.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1115 EKKYTVLLVEDNEEVRSYVRECLDPHFF--VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIP 1192
Cdd:PRK10610     3 DKELKFLVVDDFSTMRRIVRNLLKELGFnnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALP 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1193 VILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILasrEKL 1240
Cdd:PRK10610    83 VLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIF---EKL 127
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1120-1227 9.52e-14

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 68.98  E-value: 9.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF--VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIkedlrTGH--IPVIL 1195
Cdd:cd19932      3 VLIAEDEALIRMDLREMLEEAGYevVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKII-----TSEniAPIVL 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLI 1227
Cdd:cd19932     78 LTAYSQQDLVERAKEAGAMAYLVKPFSESDLI 109
PRK13557 PRK13557
histidine kinase; Provisional
952-1234 1.05e-13

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 75.48  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVAKLKLKDVPAGQRKELESlsedTELVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:PRK13557   274 DPTQAEVALLNVLINARDAMPEGGRVTIRTRNVEIEDEDLAMYHGLPP----GRYVSIAVTDTGSGMPPEILARVMDPFF 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1032 QIEDrKAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIdrrvyTEEEIDREAAdrvvmdviPSTTAPEV 1111
Cdd:PRK13557   350 TTKE-EGK---GTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPA-----SDQAENPEQE--------PKARAIDR 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1112 FGLEkkyTVLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIvLDKYP--DIVVSDIMMPrkDGLELCTLIKEDLRT 1188
Cdd:PRK13557   413 GGTE---TILIVDDRPDVAELARMILeDFGYRTLVASNGREALEI-LDSHPevDLLFTDLIMP--GGMNGVMLAREARRR 486
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1800169395 1189 -GHIPVILMT--ARSMVmhikEGFSAGAD--DYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK13557   487 qPKIKVLLTTgyAEASI----ERTDAGGSefDILNKPYRRAELARRVRMVL 533
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1119-1224 1.43e-13

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: 68.45  E-value: 1.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLD-PHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMT 1197
Cdd:cd19919      2 TVWIVDDDSSIRWVLERALAgAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ--RHPDLPVIIMT 79
                           90       100
                   ....*....|....*....|....*..
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMD 1224
Cdd:cd19919     80 AHSDLDSAVSAYQGGAFEYLPKPFDID 106
PRK10604 PRK10604
sensor protein RstB; Provisional
839-1080 1.63e-13

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 74.25  E-value: 1.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  839 TKMRMFTNFSHELRTPLtliisplqelLRrnefntgIRNKLDLIYN----NSQ-------RLLLLVNQLMDLRKNQAGKM 907
Cdd:PRK10604   211 SKKQLIDGIAHELRTPL----------VR-------LRYRLEMSDNlsaaESQalnrdigQLEALIEELLTYARLDRPQN 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  908 QLKIAKDDICSFVMEIYCAFNQIASGKEIRF-RYEGGEVGIVawfDKSLFEKVVFNLLSNAFKYtqaggeivlsvaklkl 986
Cdd:PRK10604   274 ELHLSEPDLPAWLSTHLADIQAVTPEKTVRLdTPHQGDYGAL---DMRLMERVLDNLLNNALRY---------------- 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  987 kdvpAGQRKELeSLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVEN 1066
Cdd:PRK10604   335 ----AHSRVRV-SLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDE 409
                          250
                   ....*....|....
gi 1800169395 1067 NARGGATFHVLFPI 1080
Cdd:PRK10604   410 SELGGARFSFSWPV 423
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1118-1231 1.77e-13

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 71.59  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCtlikEDLR---TGhiPV 1193
Cdd:PRK10701     2 NKIVFVEDDAEVGSLIAAYLAKHdIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTIC----RDLRpkwQG--PI 75
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1194 ILMTARSMVM-HIKeGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:PRK10701    76 VLLTSLDSDMnHIL-ALEMGACDYILKTTPPAVLLARLR 113
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1119-1314 1.85e-13

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: 70.51  E-value: 1.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRecldphfFVLEA--------DNGEtAFeivLDKY----PDIVVSDIMMPRKDGLELCTLIKEdl 1186
Cdd:COG4566      1 TVYIVDDDEAVRDSLA-------FLLESaglrvetfASAE-AF---LAALdpdrPGCLLLDVRMPGMSGLELQEELAA-- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1187 RTGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASREKLRSLYGKKfspeaigVEIVSGTDRFTQ 1266
Cdd:COG4566     68 RGSPLPVIFLTGHGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARR-------AELRARLASLTP 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1800169395 1267 KFFEVIERnIANPELNIDlICREVGLS-------RTNLYRKLKAItelSPVELIR 1314
Cdd:COG4566    141 REREVLDL-VVAGLSNKQ-IARELGISprtvevhRANVMEKLGAR---SLAELVR 190
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
957-1074 1.88e-13

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: 67.48  E-value: 1.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  957 EKVVFNLLSNAFkytqaggeivlsvakLKLKDVPAGQ-RKELESLSEDTELVhlfVSDTGKGIPEEEMKNIFAPFYQied 1035
Cdd:cd16976      2 QQVLMNLLQNAL---------------DAMGKVENPRiRIAARRLGGRLVLV---VRDNGPGIAEEHLSRVFDPFFT--- 60
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1800169395 1036 rkAKDVA-GTGIGLSLTQSIVRLHHGTIRVENNARGGATF 1074
Cdd:cd16976     61 --TKPVGkGTGLGLSISYGIVEEHGGRLSVANEEGAGARF 98
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
952-1074 2.47e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 67.49  E-value: 2.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSvaklklkdvpagqrkelesLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:cd16945      1 DPFLLRQAINNLLDNAIDFSPEGGLIALQ-------------------LEADTEGIELLVFDEGSGIPDYALNRVFERFY 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1800169395 1032 QIEdRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATF 1074
Cdd:cd16945     62 SLP-RPHSGQKSTGLGLAFVQEVAQLHGGRITLRNRPDGVLAF 103
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1118-1226 2.67e-13

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 67.65  E-value: 2.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEV----RSYVRECldPHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTlikeDLRTGHIP 1192
Cdd:cd19925      1 INVLIVEDDPMVaeihRAYVEQV--PGFTVIgTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLR----ELRAAGHD 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1193 --VILMTARSMVMHIKEGFSAGADDYIVKPFNMDVL 1226
Cdd:cd19925     75 vdVIVVTAANDVETVREALRLGVVDYLIKPFTFERL 110
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
1272-1362 2.75e-13

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 73.16  E-value: 2.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1272 IERNiANPELNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEvAARLLLESDYSVSEISTCVGFNSHAYFTQCF 1351
Cdd:COG2169     93 IEAG-AEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLL-RARQLLQTGLSVTDAAYAAGFGSLSRFYEAF 170
                           90
                   ....*....|.
gi 1800169395 1352 KSVYGCSPTEF 1362
Cdd:COG2169    171 KKLLGMTPSAY 181
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1120-1220 2.89e-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: 67.08  E-value: 2.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLEADN-GETAFEIVLDKYPDIVVSDIMMPRKDGLELCtlikEDLRT-GHIPVILMT 1197
Cdd:cd19936      1 IALVDDDRNILTSVSMALEAEGFSVETYTdGASALDGLNARPPDLAILDIKMPRMDGMELL----QRLRQkSTLPVIFLT 76
                           90       100
                   ....*....|....*....|...
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd19936     77 SKDDEIDEVFGLRMGADDYITKP 99
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1119-1226 3.18e-13

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: 67.43  E-value: 3.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHFF-VLE-ADNGETAFEIVLDKYPDIVVSDIMMP-RKDGLELCTLIKEDLrtgHIPVIL 1195
Cdd:cd17534      2 KILIVEDEAIIALDLKEILESLGYeVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKF---DIPVIF 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1800169395 1196 MTARS---MVMHIKEGFSAGaddYIVKPFNMDVL 1226
Cdd:cd17534     79 LTAYSdeeTLERAKETNPYG---YLVKPFNEREL 109
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
838-901 6.61e-13

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 64.93  E-value: 6.61e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1800169395  838 QTKMRMFTNFSHELRTPLTLIISPLQELLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRK 901
Cdd:cd00082      2 QAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1119-1232 6.80e-13

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 66.70  E-value: 6.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEE----VRSYVRE--------CLDPhffvLEAdngetafeivLDKY----PDIVVSDIMMPRKDGLELCTLI 1182
Cdd:cd17551      2 RILIVDDNPTnlllLEALLRSagylevvsFTDP----REA----------LAWCrenpPDLILLDYMMPGMDGLEFIRRL 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1183 KEDLRTGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRN 1232
Cdd:cd17551     68 RALPGLEDVPIVMITADTDREVRLRALEAGATDFLTKPFDPVELLARVRN 117
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1119-1231 7.51e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 69.45  E-value: 7.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCtlikEDLRT-GHIPVILM 1196
Cdd:PRK10529     3 NVLIVEDEQAIRRFLRTALEGDgMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFI----RDLRQwSAIPVIVL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:PRK10529    79 SARSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
959-1079 1.29e-12

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: 65.39  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  959 VVFNLLSNAFKYTQAGGEivlsvaklklkdvpagQRKELE-SLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQiedrk 1037
Cdd:cd16915      4 IVGNLIDNALDALAATGA----------------PNKQVEvFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVS----- 62
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1800169395 1038 AKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16915     63 TKGQGERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
962-1079 1.81e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 65.04  E-value: 1.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  962 NLLSNAFKYTQaggeivlsvaklklKDVPAgqrkELESLSEDTELVHLF-VSDTGKGIPEEEMKNIFAPFYQIEDRKakD 1040
Cdd:cd16921      7 NLLGNAIKFRR--------------PRRPP----RIEVGAEDVGEEWTFyVRDNGIGIDPEYAEKVFGIFQRLHSRE--E 66
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1041 VAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16921     67 YEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
957-1079 1.84e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 64.76  E-value: 1.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  957 EKVVFNLLSNAFKYtqaggeivlsvaklklkdvpAGQRKELESLSEDTELVhLFVSDTGKGIPEEEMKNIFAPFYQIEDR 1036
Cdd:cd16939      2 ARALDNLLRNALRY--------------------AHRTVRIALLVSGGRLT-LIVEDDGPGIPAAARERVFEPFVRLDPS 60
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1800169395 1037 KAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16939     61 RDRATGGFGLGLAIVHRVALWHGGHVECDDSELGGACFRLTWP 103
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1118-1171 1.89e-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: 62.97  E-value: 1.89e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1800169395  1118 YTVLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMP 1171
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLeKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
848-1094 2.14e-12

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 71.20  E-value: 2.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  848 SHELRTPLTLIISPLQELlrrnefNTGIRnKLDLIYNNSQR-----LLLLVNQLMDLRKNQAGKMQLKIAKDDICSFVME 922
Cdd:PRK10549   248 SHELRTPLAVLRGELEAI------QDGVR-KFTPESVASLQaevgtLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLLEV 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  923 IYCAFNQIASGKEIRFRYEGGEVGIVawF-DKSLFEKVVFNLLSNAFKYTQAGGEIvlsvaklklkdvpagqrkELESLS 1001
Cdd:PRK10549   321 AGGAFRERFASRGLTLQLSLPDSATV--FgDPDRLMQLFNNLLENSLRYTDSGGSL------------------HISAEQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1002 EDTELVhLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPId 1081
Cdd:PRK10549   381 RDKTLR-LTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPL- 458
                          250
                   ....*....|...
gi 1800169395 1082 rrvytEEEIDREA 1094
Cdd:PRK10549   459 -----ERDLQREV 466
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
840-905 2.28e-12

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 63.38  E-value: 2.28e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800169395  840 KMRMFTNFSHELRTPLTLIISPLqELLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAG 905
Cdd:pfam00512    2 KSEFLANLSHELRTPLTAIRGYL-ELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
PRK10766 PRK10766
two-component system response regulator TorR;
1118-1234 2.50e-12

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 67.76  E-value: 2.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEVRSYvrecLDPHF-----FVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELctliKEDLR-TGHI 1191
Cdd:PRK10766     3 YHILVVEDEPVTRAR----LQGYFeqegyTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLML----TRELRsRSTV 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1800169395 1192 PVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK10766    75 GIILVTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
879-1236 3.00e-12

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 71.25  E-value: 3.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  879 LDLIYNNSQRLLLLVNQLMDLRKNQAGKMQlkiaKDDICSFVMEIYCAFN-QIASGKEIRFRYEGGevGIVAWFDKSLFE 957
Cdd:PRK13837   489 IDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSELVTEIAPLLRvSLPPGVELDFDQDQE--PAVVEGNPAELQ 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  958 KVVFNLLSNAFKYTQAGG--EIVLSVAKLKLKDV------PAGqrkeleslsedtELVHLFVSDTGKGIPEEEMKNIFAP 1029
Cdd:PRK13837   563 QVLMNLCSNAAQAMDGAGrvDISLSRAKLRAPKVlshgvlPPG------------RYVLLRVSDTGAGIDEAVLPHIFEP 630
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1030 FYQIEDrkakdvAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRRVyteeeidrEAADRvvmdvipSTTAP 1109
Cdd:PRK13837   631 FFTTRA------GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKV--------PVAPQ-------AFFGP 689
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1110 EVFGLEKKYTVLLVEDNEEVRSYVRECL-----DPHFFVLEAD------NGETAFEIVLdkypdivvsdIMMPRKDGLEL 1178
Cdd:PRK13837   690 GPLPRGRGETVLLVEPDDATLERYEEKLaalgyEPVGFSTLAAaiawisKGPERFDLVL----------VDDRLLDEEQA 759
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1800169395 1179 CTLIKEDLRTghIPVILMTaRSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILAS 1236
Cdd:PRK13837   760 AAALHAAAPT--LPIILGG-NSKTMALSPDLLASVAEILAKPISSRTLAYALRTALAT 814
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
952-1072 3.47e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 64.02  E-value: 3.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFY 1031
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGGTVSISI-------------------YDEEEYLYFEIWDNGHGFSEQDLKKALELFY 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1800169395 1032 QieDRKAKDVAG-TGIGLSLTQSIVRLHHGTIRVENNARGGA 1072
Cdd:cd16975     62 R--DDTSRRSGGhYGMGLYIAKNLVEKHGGSLIIENSQKGGA 101
fixJ PRK09390
response regulator FixJ; Provisional
1117-1314 4.73e-12

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 66.56  E-value: 4.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1117 KYTVLLVEDNEEVRsyvrECLDphfFVLEADNGE-------TAFeivLDKYPDI----VVSDIMMPRKDGLELCTLIKEd 1185
Cdd:PRK09390     3 KGVVHVVDDDEAMR----DSLA---FLLDSAGFEvrlfesaQAF---LDALPGLrfgcVVTDVRMPGIDGIELLRRLKA- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1186 lRTGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILA-SREKLRSlygkkfspEAIGVEIVSGTDRF 1264
Cdd:PRK09390    72 -RGSPLPVIVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAqAPEAAKS--------EAVAADIRARIASL 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1800169395 1265 TQKFFEVIERNIANpeLNIDLICREVGLS-------RTNLYRKLKAiTELSpvELIR 1314
Cdd:PRK09390   143 SERERQVMDGLVAG--LSNKVIARDLDISprtvevyRANVMTKMQA-GSLS--ELVR 194
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
962-1079 5.80e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 63.76  E-value: 5.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  962 NLLSNAFKYTQAGGEIvlsvaKLKLKDVPAGqrkeleslsedtelVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDV 1041
Cdd:cd16952      7 NLVSNAVKYTPPSDTI-----TVRWSQEESG--------------ARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNT 67
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1042 AGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16952     68 GGTGLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFP 105
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1119-1302 6.33e-12

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: 65.71  E-value: 6.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMT 1197
Cdd:COG4567      6 SLLLVDDDEAFARVLARALERRgFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE--RDPDARIVVLT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1198 -ARS---MVMHIKegfsAGADDYIVKPFNMDVLiyrirnilasrekLRSLYGKKFSPEAIGVEIVSgTDRFTqkfFEVIE 1273
Cdd:COG4567     84 gYASiatAVEAIK----LGADDYLAKPADADDL-------------LAALERAEGDAPAPPENPMS-LDRLE---WEHIQ 142
                          170       180
                   ....*....|....*....|....*....
gi 1800169395 1274 RNIANPELNIDLICREVGLSRTNLYRKLK 1302
Cdd:COG4567    143 RVLAECDGNISATARALGMHRRTLQRKLA 171
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
956-1079 8.20e-12

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: 63.55  E-value: 8.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  956 FEKVVFNLLSNAFKYTQAGGEIVLSVAKLKLKDVPAGQRKELESlsedTELVHLFVSDTGKGIPEEEMKNIFAPFYQied 1035
Cdd:cd16919      1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYRDLIP----GNYVCLEVSDTGSGMPAEVLRRAFEPFFT--- 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1800169395 1036 rkAKDVA-GTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16919     74 --TKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1120-1226 9.68e-12

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 63.03  E-value: 9.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRE-CLDPHFFVLEADNGETAFEIVLDK--YPDIVVSDIMMPRKDGLELCTLIKEDLrtgHIPVILM 1196
Cdd:cd17584      1 VLVVDDDPTCLAILKRmLLRCGYQVTTCTDAEEALSMLRENkdEFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDVL 1226
Cdd:cd17584     78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
PRK11173 PRK11173
two-component response regulator; Provisional
1120-1280 1.33e-11

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 66.19  E-value: 1.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH-FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDlrtGHIPVILMTA 1198
Cdd:PRK11173     6 ILIVEDELVTRNTLKSIFEAEgYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQ---ANVALMFLTG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1199 R-SMVMHIKeGFSAGADDYIVKPFNMDVLIYRIRNILAsreklRSLYGKKFSPEAIGVEIVsgtdRFTQKFFEVIERNIA 1277
Cdd:PRK11173    83 RdNEVDKIL-GLEIGADDYITKPFNPRELTIRARNLLS-----RTMNLGTVSEERRSVESY----KFNGWELDINSRSLI 152

                   ...
gi 1800169395 1278 NPE 1280
Cdd:PRK11173   153 SPD 155
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
848-1081 1.47e-11

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 68.27  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  848 SHELRTPLTLIISPLQELLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKnqagKMQLKIAKDDICSFVMEIYCAF 927
Cdd:PRK10364   245 AHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVK----PTHLALQAVDLNDLINHSLQLV 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  928 NQIASGKEIRFRYEGGEVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSVaklklkdvpagqrkeleslSEDTELV 1007
Cdd:PRK10364   321 SQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTA-------------------SESGAGV 381
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1800169395 1008 HLFVSDTGKGIPEEEMKNIFAPFYQIedrKAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPID 1081
Cdd:PRK10364   382 KISVTDSGKGIAADQLEAIFTPYFTT---KAE---GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVN 449
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
840-905 1.49e-11

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 61.04  E-value: 1.49e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800169395   840 KMRMFTNFSHELRTPLTLIISPLqELLRRNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAG 905
Cdd:smart00388    2 KREFLANLSHELRTPLTAIRGYL-ELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1120-1235 1.56e-11

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: 62.67  E-value: 1.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPH---FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghIPVILM 1196
Cdd:cd19930      1 VLIAEDQEMVRGALAALLELEddlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPD--TKVLIV 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILA 1235
Cdd:cd19930     79 TTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1161-1234 1.77e-11

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 65.86  E-value: 1.77e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800169395 1161 PDIVVSDIMMPRKDGLELCTLIKedlRTGHIPVILMTARsmvmhIKE-----GFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK10710    55 PDLILLDLMLPGTDGLTLCREIR---RFSDIPIVMVTAK-----IEEidrllGLEIGADDYICKPYSPREVVARVKTIL 125
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
963-1079 1.78e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 62.30  E-value: 1.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  963 LLSNAFKYTQAGGEIVLSVAklklkdvpagqrkeleslsEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDRKaKDVA 1042
Cdd:cd16948     13 IVSNALKYSKQGGKIEIYSE-------------------TNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGR-NFQE 72
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1043 GTGIGLSLTQSIV-RLHHgTIRVENNARGGATFHVLFP 1079
Cdd:cd16948     73 STGMGLYLVKKLCdKLGH-KIDVESEVGEGTTFTITFP 109
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
844-1079 2.47e-11

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 67.73  E-value: 2.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  844 FTNFSHELRTPLTLIISPLqELLRRNEFNTGIRNK-LDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDICSFVME 922
Cdd:PRK11006   208 FANVSHELRTPLTVLQGYL-EMMQDQPLEGALREKaLHTMREQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPMMLRV 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  923 IYCAFNQIASGK-EIRFRyeggevgivawFDKSLfeKV----------VFNLLSNAFKYTQAGGEIVLSvaklkLKDVPA 991
Cdd:PRK11006   287 LEREAQTLSQGKhTITFE-----------VDNSL--KVfgnedqlrsaISNLVYNAVNHTPEGTHITVR-----WQRVPQ 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  992 GQRkeleslsedtelvhLFVSDTGKGIPEEEMKNIFAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGG 1071
Cdd:PRK11006   349 GAE--------------FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKG 414

                   ....*...
gi 1800169395 1072 ATFHVLFP 1079
Cdd:PRK11006   415 TRFSFVLP 422
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1120-1234 3.71e-11

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: 61.66  E-value: 3.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLE-ADNGETAFEIVLDKYPDIVVSDIMMPRKDGLElctlIKEDLRTGHI--PVILM 1196
Cdd:cd17616      1 VLLIEDDSATAQSIELMLKSEGFNVYtTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYE----VLRTLRLAKVktPILIL 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:cd17616     77 SGLADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
1120-1230 4.86e-11

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: 60.91  E-value: 4.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF---VLEA-DNGETAFEIvldKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVIL 1195
Cdd:cd17573      1 ILLIEDDSTLGKEISKGLNEKGYqadVAESlKDGEYYIDI---RNYDLVLVSDKLPDGNGLSIVSRIKE--KHPSIVVIV 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRI 1230
Cdd:cd17573     76 LSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1120-1241 6.03e-11

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 61.25  E-value: 6.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL--DPHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghiPVILM 1196
Cdd:cd17541      3 VLIVDDSAVMRKLLSRILesDPDIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPT---PVVMV 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1800169395 1197 TArsmvmHIKEG-------FSAGADDYIVKPFNM-DVLIYRIRNILasREKLR 1241
Cdd:cd17541     80 SS-----LTEEGaeitleaLELGAVDFIAKPSGGiSLDLEEIAEEL--IEKIK 125
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1118-1235 1.17e-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: 60.11  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILM 1196
Cdd:cd17569      1 PTILLVDDEPNILKALKRLLRREGYeVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRE--RYPDTVRILL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1800169395 1197 TARS---MVMH-IKEG--FSagaddYIVKPFNMDVLIYRIRNILA 1235
Cdd:cd17569     79 TGYAdldAAIEaINEGeiYR-----FLTKPWDDEELKETIRQALE 118
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1117-1182 1.18e-10

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 60.68  E-value: 1.18e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800169395 1117 KYTVLLVEDNEEVRSYVRECLD--PHF-FVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLI 1182
Cdd:COG2197      1 MIRVLIVDDHPLVREGLRALLEaePDIeVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1120-1242 1.40e-10

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 59.86  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDN----EEVRSYVREclDPHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIpvI 1194
Cdd:cd17532      1 ALIVDDEplarEELRYLLEE--HPDIEIVgEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLI--V 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1800169395 1195 LMTA-RSmvmHIKEGFSAGADDYIVKPFNMDvliyRIRNILASREKLRS 1242
Cdd:cd17532     77 FVTAyDE---YAVEAFELNAVDYLLKPFSEE----RLAEALAKLRKRLS 118
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
820-1072 1.99e-10

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 65.09  E-value: 1.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  820 EQALVYEHLKQQQAEEFHQTKM----RMFTNFSHELRTPLTLIISPLQELLRR--NEFNTGIRNKLDLIYNNSQRLLLLV 893
Cdd:COG4192    409 ERKRIEKNLRQTQDELIQAAKMavvgQTMTSLAHELNQPLNAMSMYLFSAKKAleQENYAQLPTSLDKIEGLIERMDKII 488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  894 NQLMDLRKNQAGKMQLKIAKDDICSfVMEIYcafnqiasgkEIRFRYEGGEVGI---VAWF-DKSLFEKVVFNLLSNAFK 969
Cdd:COG4192    489 KSLRQFSRKSDTPLQPVDLRQVIEQ-AWELV----------ESRAKPQQITLHIpddLMVQgDQVLLEQVLVNLLVNALD 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  970 YTQAGGEIVLSvaklklkdvpagqrkelesLSEDTELVHLFVSDTGKGIPEEEmkNIFAPFYQiedrkAKDVaGTGIGLS 1049
Cdd:COG4192    558 AVATQPQISVD-------------------LLSNAENLRVAISDNGNGWPLVD--KLFTPFTT-----TKEV-GLGLGLS 610
                          250       260
                   ....*....|....*....|...
gi 1800169395 1050 LTQSIVRLHHGTIRVENNARGGA 1072
Cdd:COG4192    611 ICRSIMQQFGGDLYLASTLERGA 633
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
947-1066 2.06e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 59.83  E-value: 2.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  947 IVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSvaklklkdvpagqrkelesLSEDTELVHLFVSDTGKGIPEEEMKNI 1026
Cdd:cd16947     12 IYANANTEALQRILKNLISNAIKYGSDGKFLGMT-------------------LREDEKHVYIDIWDKGKGISETEKDHV 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1800169395 1027 FAPFYQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVEN 1066
Cdd:cd16947     73 FERLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNS 112
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
1120-1226 2.17e-10

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: 59.49  E-value: 2.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIK---EDLRtghipVIL 1195
Cdd:cd17553      3 ILIVDDQYGIRILLNEVFNKEGYqTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKvidENIR-----VII 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVL 1226
Cdd:cd17553     78 MTAYGELDMIQESKELGALTHFAKPFDIDEI 108
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
1120-1220 2.42e-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: 58.95  E-value: 2.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYV----RECldpHFFVLEADNGETAFEIVLDKYP--DIVVSDIMMPRKDGLELCTLIKEDLRTGHIPV 1193
Cdd:cd17582      1 VLLVENDDSTRQIVtallRKC---SYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYIMRHKICKNIPV 77
                           90       100
                   ....*....|....*....|....*...
gi 1800169395 1194 ILMTAR-SMVMHIKeGFSAGADDYIVKP 1220
Cdd:cd17582     78 IMMSSQdSVGVVFK-CLSKGAADYLVKP 104
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
1119-1238 3.12e-10

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: 59.30  E-value: 3.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTA 1198
Cdd:cd17596      2 TILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRE--RWPEVVRIIISG 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1800169395 1199 RSMVMHIKEGFS-AGADDYIVKPFNMDVLIYRIRNILASRE 1238
Cdd:cd17596     80 YTDSEDIIAGINeAGIYQYLTKPWHPDQLLLTVRNAARLFE 120
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
1117-1221 4.43e-10

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: 58.00  E-value: 4.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1117 KYTVLLVEDNEEVRSYVRECLD--PHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPV 1193
Cdd:cd17561      1 KIKVLIADDNREFVQLLEEYLNsqPDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1800169395 1194 ILMTA--RSMVMhiKEGFSAGADDYIVKPF 1221
Cdd:cd17561     81 IMLTAfgQEDIT--QRAVELGASYYILKPF 108
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
417-672 6.76e-10

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 61.57  E-value: 6.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  417 DYIW-CGTTQGSIYRFDTRSKRFSLYyafPLHQSTSVYSILRTQDNNLWLATSKPEvGLVKLTeerkmqnrfelADSGRI 495
Cdd:COG4257     28 GAVWfTDQGGGRIGRLDPATGEFTEY---PLGGGSGPHGIAVDPDGNLWFTDNGNN-RIGRID-----------PKTGEI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  496 WT---PGSSRCLLELE---KGVLLV-GSRNNGLYKYDENKRECTVFSKNGKGANhlPADyvtsLVRTKSGQIWVGTFGGG 568
Cdd:COG4257     93 TTfalPGGGSNPHGIAfdpDGNLWFtDQGGNRIGRLDPATGEVTEFPLPTGGAG--PYG----IAVDPDGNLWVTDFGAN 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  569 -LSLFDQEKGIVKYITKKEGlLDDEVCMVVeDRNGDLWM--STNSCISRYNPKTDEVYNYYMDNGIGAqefsPHsGMLL- 644
Cdd:COG4257    167 aIGRIDPDTGTLTEYALPTP-GAGPRGLAV-DPDGNLWVadTGSGRIGRFDPKTGTVTEYPLPGGGAR----PY-GVAVd 239
                          250       260       270
                   ....*....|....*....|....*....|
gi 1800169395  645 PDGNICF--SANNGFITFDPANLQINSFLP 672
Cdd:COG4257    240 GDGRVWFaeSGANRIVRFDPDTELTEYVLP 269
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1120-1220 8.46e-10

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: 57.38  E-value: 8.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTA 1198
Cdd:cd17602      1 VACVDDRPSIQKMIEYFLEKQGFrVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                           90       100
                   ....*....|....*....|..
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd17602     81 KDGLVDRIRAKMAGASGYLTKP 102
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
957-1079 1.63e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 56.64  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  957 EKVVFNLLSNAfkyTQA----GGEIVLSVA---KLKLkdvpAGQRKELESLSEdtelvhlfVSDTGKGIPEEEMKNIFAP 1029
Cdd:cd16918      2 IQVFLNLVRNA---AQAlagsGGEIILRTRtqrQVTL----GHPRHRLALRVS--------VIDNGPGIPPDLQDTIFYP 66
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1030 FyqIEDRkakdVAGTGIGLSLTQSIVRLHHGTIRVEnNARGGATFHVLFP 1079
Cdd:cd16918     67 M--VSGR----ENGTGLGLAIAQNIVSQHGGVIECD-SQPGHTVFSVSLP 109
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
993-1080 1.63e-09

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 61.84  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  993 QRKELESLSE-DTELVHLFVSDTGKGIPEEEMKNIFAPFYQIedrKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGG 1071
Cdd:TIGR02938  409 KRRELSITTAlNGDLIVVSILDSGPGIPQDLRYKVFEPFFTT---KGGSRKHIGMGLSVAQEIVADHGGIIDLDDDYSEG 485

                   ....*....
gi 1800169395 1072 ATFHVLFPI 1080
Cdd:TIGR02938  486 CRIIVEFRV 494
PRK10337 PRK10337
sensor protein QseC; Provisional
842-1071 1.71e-09

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 61.97  E-value: 1.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  842 RMFT-NFSHELRTPLTLI--------ISPLQELLRRN---EFNTGIrnkldliynnsQRLLLLVNQLMDLRK----NQAG 905
Cdd:PRK10337   238 RRFTsDAAHELRSPLAALkvqtevaqLSDDDPQARKKallQLHAGI-----------DRATRLVDQLLTLSRldslDNLQ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  906 KMQLKIAKDDICSFVMEIYCAFNQiaSGKEIRFRYEGgeVGIVAWFDKSLFEKVVFNLLSNAFKYTQAGGEIVLSvaklk 985
Cdd:PRK10337   307 DVAEIPLEDLLQSAVMDIYHTAQQ--AGIDVRLTLNA--HPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSVVDVT----- 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  986 lkdvpagqrkelesLSEDtelvHLFVSDTGKGIPEEEMKNIFAPFYQiedRKAKDVAGTGIGLSLTQSIVRLHHGTIRVE 1065
Cdd:PRK10337   378 --------------LNAR----NFTVRDNGPGVTPEALARIGERFYR---PPGQEATGSGLGLSIVRRIAKLHGMNVSFG 436

                   ....*.
gi 1800169395 1066 NNARGG 1071
Cdd:PRK10337   437 NAPEGG 442
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1119-1234 2.08e-09

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 59.21  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRsyvreclDPHFFVLEADN--------GETAFEIVLDKYPDIVVSDIMMPRKDGLELCtlikEDLRTGH 1190
Cdd:PRK11083     5 TILLVEDEQAIA-------DTLVYALQSEGftvewferGLPALDKLRQQPPDLVILDVGLPDISGFELC----RQLLAFH 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1800169395 1191 --IPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK11083    74 paLPVIFLTARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTIL 119
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1120-1237 2.32e-09

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 59.44  E-value: 2.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLEADNGETAFEIVLDKYP-DIVVSDIMMPRKDGLElctlIKEDLRT-GHIPVILMT 1197
Cdd:PRK13856     4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETvDVVVVDLNLGREDGLE----IVRSLATkSDVPIIIIS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1800169395 1198 ARSMVMHIKE-GFSAGADDYIVKPFNMDVLIYRIRNILASR 1237
Cdd:PRK13856    80 GDRLEEADKVvALELGATDFIAKPFGTREFLARIRVALRVR 120
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
951-1078 2.53e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 56.87  E-value: 2.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  951 FDKSLFEKVVFNLLSNAFKYtqaggeivlsvaklklkdvpAGQRKELeSLSEDTELVHLFVSDTGKGIPEEEMKNIFapf 1030
Cdd:cd16954     33 GERNDLMELLGNLLDNACKW--------------------CLEFVEV-TARQTDGGLHLIVDDDGPGVPESQRSKIF--- 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1031 yQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLF 1078
Cdd:cd16954     89 -QRGQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
777-1079 2.66e-09

Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 61.04  E-value: 2.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  777 IRTLSIIVHPPYW--MTWYAYLFYaFSFFGICFLVMYYIIKKKnLEQALVYEHLkqQQAEefhqtKMRMFTNF----SHE 850
Cdd:COG5806    141 LLLLLLAIIFIADisELLDFILYF-IIIQLLAMLIAVYLIENL-IENILLRKEL--QRAE-----KLEVVSELaasiAHE 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  851 LRTPLT-------LIISPLQELLRRNEFntgirnkLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQLKIAKDDI--CSFVM 921
Cdd:COG5806    212 VRNPLTvvrgfiqLLQEPELSDEKRKQY-------IRIALEELDRAEAIITDYLTFAKPQPEKLEKIDVSEELehVIDVL 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  922 EIYCAFNQIasgkEIRFRYEGGEVgIVAwfDKSLFEKVVFNLLSNAFKYTQAGGeiVLSVaklklkdvpagqrkeleSLS 1001
Cdd:COG5806    285 SPYANMNNV----EIQTELEPGLY-IEG--DRQKLQQCLINIIKNGIEAMPNGG--TLTI-----------------DVS 338
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800169395 1002 EDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIedrKAKdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:COG5806    339 IDKNKVIISIKDTGVGMTKEQLERLGEPYFST---KEK---GTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLP 410
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
1119-1231 3.39e-09

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: 56.26  E-value: 3.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECL------DPHFFvleADNGEtAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIP 1192
Cdd:cd17575      2 MVLLVDDQAIIGEAVRRALadeediDFHYC---SDPTE-AIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1800169395 1193 VILMTARSMVMHIKEGFSAGADDYIVK-PFNMDvLIYRIR 1231
Cdd:cd17575     78 IIVLSTKEEPEVKSEAFALGANDYLVKlPDKIE-LVARIR 116
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1147-1224 4.46e-09

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 60.65  E-value: 4.46e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800169395 1147 DNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFNMD 1224
Cdd:PRK10923    34 ENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDID 109
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
1122-1220 5.46e-09

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 54.97  E-value: 5.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1122 LVEDNEEVRSYVRECLDPHFF---VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIpVILMTA 1198
Cdd:cd17565      3 IVDDDKNIIKILSDIIEDDDLgevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKF-IMISQV 81
                           90       100
                   ....*....|....*....|..
gi 1800169395 1199 RSMVMhIKEGFSAGADDYIVKP 1220
Cdd:cd17565     82 SDKEM-IGKAYQAGIEFFINKP 102
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1118-1231 6.11e-09

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: 55.29  E-value: 6.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEVRSYVRECLDPHFFVLEADNGETAFeivLDKYPD----IVVSDIMMPRKDGLELCTLIKEdlRTGHIPV 1193
Cdd:cd17537      1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAF---LAAAPPdqpgCLVLDVRMPGMSGLELQDELLA--RGSNIPI 75
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1800169395 1194 ILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:cd17537     76 IFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIE 113
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
1120-1230 6.58e-09

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 54.96  E-value: 6.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF--VLEADNGETAFEIVLDKYPDIVVSDIMM-PRKDGLELCtlikEDLRTGH-IP--- 1192
Cdd:cd17589      1 FLIVDDQPTFRSMLKSMLRSLGVtrIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLL----EELRHKKlISpst 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1800169395 1193 -VILMTA---RSMVMHIKEgfsAGADDYIVKPFNMDVLIYRI 1230
Cdd:cd17589     77 vFIMVTGessRAMVLSALE---LEPDDYLLKPFTVSELRERL 115
PRK10643 PRK10643
two-component system response regulator PmrA;
1120-1234 8.28e-09

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 57.35  E-value: 8.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNE----------EVRSYVRECldphffvleADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKedlRTG 1189
Cdd:PRK10643     3 ILIVEDDTlllqglilalQTEGYACDC---------ASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWR---QKK 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1800169395 1190 H-IPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK10643    71 YtLPVLILTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALI 116
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
846-1131 1.25e-08

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 59.86  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  846 NFSHELRTPLTLIISPLQELLRrNEFNTGIRNKLDLIYNNSQRLLLLVNQLMDLRKNQAGKMQL-KI------AKDDics 918
Cdd:PRK11107   299 NMSHELRTPLNGVIGFTRQTLK-TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLeNIpfslreTLDE--- 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  919 fVMEIycafnqIA-SGKE--------IRFRYEGGEVGivawfDKSLFEKVVFNLLSNAFKYTQAGgEIVLSVaklklkdv 989
Cdd:PRK11107   375 -VVTL------LAhSAHEkgleltlnIDPDVPDNVIG-----DPLRLQQIITNLVGNAIKFTESG-NIDILV-------- 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  990 pagqrkELESLSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQ----IEDRkakdVAGTGIGLSLTQSIVRLHHGTIRVE 1065
Cdd:PRK11107   434 ------ELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQadasISRR----HGGTGLGLVITQKLVNEMGGDISFH 503
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800169395 1066 NNARGGATFHVLFPIDrrvyteeeidreAADRVVMDVIPSTTapevfgLEKKyTVLLVEDNEEVRS 1131
Cdd:PRK11107   504 SQPNRGSTFWFHLPLD------------LNPNPIIDGLPTDC------LAGK-RLLYVEPNSAAAQ 550
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
1120-1221 1.59e-08

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 53.50  E-value: 1.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVL-DKYPDIVVSDIMMPRkdGLELCTLIKEDLRTG-HIPVILM 1196
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLeDLGYTVLEAASGDEALDLLEsGPDIDLLVTDVIMPG--GMNGSQLAEEARRRRpDLKVLLT 78
                           90       100
                   ....*....|....*....|....*
gi 1800169395 1197 TARSMVMHIKEGFSAGAdDYIVKPF 1221
Cdd:cd18161     79 SGYAENAIEGGDLAPGV-DVLSKPF 102
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
1120-1220 1.63e-08

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: 53.36  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlrTGHIPVILMTA 1198
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFeVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA---RSNVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
952-1079 1.68e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 53.70  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTQAGGEIVLSVAKlklkDVPAGQRKELEslsedtelvhLFVSDTGKGIPEEEMKNIFAPFy 1031
Cdd:cd16944      1 DTTQISQVLTNILKNAAEAIEGRPSDVGEVRI----RVEADQDGRIV----------LIVCDNGKGFPREMRHRATEPY- 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1032 qIEDRKAkdvaGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFP 1079
Cdd:cd16944     66 -VTTRPK----GTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
1119-1184 2.53e-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: 52.89  E-value: 2.53e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800169395 1119 TVLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYP-DIVVSDIMMPRKDGLELCTLIKE 1184
Cdd:cd18160      1 TILLADDEPSVRKFIVTTLkKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARK 68
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
1259-1362 3.78e-08

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 56.58  E-value: 3.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1259 SGTDRFTQKFFEVIERNIANPELNIDLICREVGLSRTNLYRkLKAITELSPVELIRNKRLEVAARLL--LESDYSVSEIS 1336
Cdd:PRK09685   193 PRRERQFQKVVALIDQSIQEEILRPEWIAGELGISVRSLYR-LFAEQGLVVAQYIRNRRLDRCADDLrpAADDEKITSIA 271
                           90       100
                   ....*....|....*....|....*.
gi 1800169395 1337 TCVGFNSHAYFTQCFKSVYGCSPTEF 1362
Cdd:PRK09685   272 YKWGFSDSSHFSTAFKQRFGVSPGEY 297
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1120-1225 4.72e-08

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: 52.75  E-value: 4.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFF-VLEADNGETAFEI---------VLDKYPDI--VVSDIMMPRKDGLELCTLIKEDLR 1187
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLRISSCrVTAVDSGKRALEFlgledeedsSNFNEPKVnmIITDYCMPGMTGYDLLKKVKESSA 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1188 TGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFNM-DV 1225
Cdd:cd17581     81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLaDV 119
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
91-334 4.81e-08

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 55.80  E-value: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395   91 TAIVEDRKNCLWVGTSRG--LNRLDLKTDRITPYAGKNFSlldsGVRSLFIDSNDRLWVGTSKGlylfvheaDTFQSVDL 168
Cdd:COG4257     20 RDVAVDPDGAVWFTDQGGgrIGRLDPATGEFTEYPLGGGS----GPHGIAVDPDGNLWFTDNGN--------NRIGRIDP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  169 DGkikGEFISVITETSDHQLL-IGTEHKG-LYVCDLNLKLISHYAK-----TEGNASLPDNNISDIHEDSRKQLWVSTNY 241
Cdd:COG4257     88 KT---GEITTFALPGGGSNPHgIAFDPDGnLWFTDQGGNRIGRLDPatgevTEFPLPTGGAGPYGIAVDPDGNLWVTDFG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  242 GG-VSKVDLSTGTSVHYTTANSKlttDNIRCLA-EADGTLFIGTFDG--LYTIDLTDNQLKGRSNAALEKGtlshfsIYS 317
Cdd:COG4257    165 ANaIGRIDPDTGTLTEYALPTPG---AGPRGLAvDPDGNLWVADTGSgrIGRFDPKTGTVTEYPLPGGGAR------PYG 235
                          250
                   ....*....|....*..
gi 1800169395  318 ICVDNSGNVWVGTYSGG 334
Cdd:COG4257    236 VAVDGDGRVWFAESGAN 252
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
960-1079 4.99e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 52.00  E-value: 4.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  960 VF-NLLSNAFKYTqaggeivlsvaklklkdvPAGQRKELESLSEDtELVHLFVSDTGKGIPEEEMKNIFAPFYQIEdrKA 1038
Cdd:cd16923      4 VFsNLLSNAIKYS------------------PENTRIYITSFLTD-DVVNIMFKNPSSHPLDFKLEKLFERFYRGD--NS 62
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1800169395 1039 KDVAGTGIGLSLTQSIVRLHHGTIRVENNARgGATFHVLFP 1079
Cdd:cd16923     63 RNTEGAGLGLSIAKAIIELHGGSASAEYDDN-HDLFKVRLP 102
PRK15369 PRK15369
two component system response regulator;
1116-1308 5.01e-08

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 55.08  E-value: 5.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1116 KKYTVLLVEDNEEVRSYVRECLD--PHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIP 1192
Cdd:PRK15369     2 KNYKILLVDDHELIINGIKNMLApyPRYKIVgQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQ--RWPAMN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1193 VILMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILAsreklrslyGKKFSPEAIGVEIVSG------------ 1260
Cdd:PRK15369    80 ILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAV---------GKRYIDPALNREAILAllnaddtnppll 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1800169395 1261 TDRFTQKFFEVIE----RNIANpELNIDLicREVGLSRTNLYRKLKA--ITELS 1308
Cdd:PRK15369   151 TPRERQILKLITEgytnRDIAE-QLSISI--KTVETHRLNMMRKLDVhkVAELL 201
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1120-1235 5.35e-08

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: 52.74  E-value: 5.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL--DPHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIpVILm 1196
Cdd:cd19931      1 VLLIDDHPLLRKGIKQLIelDPDFTVVgEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARI-VIL- 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILA 1235
Cdd:cd19931     79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
pleD PRK09581
response regulator PleD; Reviewed
1119-1231 5.79e-08

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 56.83  E-value: 5.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHF-FVLEADNGETAFEIVLDKYpDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMT 1197
Cdd:PRK09581   157 RILLVDDDVSQAERIANILKEEFrVVVVSDPSEALFNAAETNY-DLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLV 235
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1800169395 1198 ARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:PRK09581   236 DEDDDPRLVKALELGVNDYLMRPIDKNELLARVR 269
PRK10816 PRK10816
two-component system response regulator PhoP;
1120-1234 7.60e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 54.74  E-value: 7.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL-DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghIPVILMTA 1198
Cdd:PRK10816     3 VLVVEDNALLRHHLKVQLqDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVLTA 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNIL 1234
Cdd:PRK10816    81 RESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALM 116
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1146-1235 1.07e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 56.19  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1146 ADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTARSMVMHIKEGFSAGADDYIVKPFNMDV 1225
Cdd:PRK10365    35 ANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKA--LNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDN 112
                           90
                   ....*....|
gi 1800169395 1226 LIYRIRNILA 1235
Cdd:PRK10365   113 LQATLEKALA 122
PRK10693 PRK10693
two-component system response regulator RssB;
1145-1256 1.11e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 55.00  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1145 EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLE-LCTLIKEDLRTghiPVILMTARSMVMHIKEGFSAGADDYIVKPfnm 1223
Cdd:PRK10693     2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEfVEHLRNRGDQT---PVLVISATENMADIAKALRLGVQDVLLKP--- 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1800169395 1224 dvliyrIRNILASREK-LRSLYGKKFSPEAIGVE 1256
Cdd:PRK10693    76 ------VKDLNRLREMvFACLYPSMFNSRVEEEE 103
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
915-1083 1.45e-07

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 55.68  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  915 DICSFVMEIYCAFNQIASGKEIRFRYEGGEVGIVAwfDK----SLfekvVFN-LLSNAFKY---TQAGGEIVLSvaklkl 986
Cdd:COG3920    360 DLRDYLRELLEPLRDSYGGRGIRIELDGPDVELPA--DAavplGL----ILNeLVTNALKHaflSGEGGRIRVS------ 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  987 kdvpagqrkelesLSEDTELVHLFVSDTGKGIPEEemknifapfyqiedrkAKDVAGTGIGLSLTQSIVRLHHGTIRVEN 1066
Cdd:COG3920    428 -------------WRREDGRLRLTVSDNGVGLPED----------------VDPPARKGLGLRLIRALVRQLGGTLELDR 478
                          170
                   ....*....|....*..
gi 1800169395 1067 NArgGATFHVLFPIDRR 1083
Cdd:COG3920    479 PE--GTRVRITFPLAEL 493
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
958-1079 1.46e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 51.03  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  958 KVVFNLLSNAFKYT-QAGGEIVLSVAklklkdvPAGQRkeleslsedtelVHLFVSDTGKGIPEEEMKNIFAPFYQieDR 1036
Cdd:cd16953      3 QVLRNLIGNAISFSpPDTGRITVSAM-------PTGKM------------VTISVEDEGPGIPQEKLESIFDRFYT--ER 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1800169395 1037 KAKDVAGT--GIGLSLTQSIVRLHHGTIRVENNARG----GATFHVLFP 1079
Cdd:cd16953     62 PANEAFGQhsGLGLSISRQIIEAHGGISVAENHNQPgqviGARFTVQLP 110
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
1271-1362 1.78e-07

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 54.16  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1271 VIERNIANpELNIDLICREVGLSRTNLYRKLKAiTELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQC 1350
Cdd:PRK09978   150 VINNNIAH-EWTLARIASELLMSPSLLKKKLRE-EETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYV 227
                           90
                   ....*....|..
gi 1800169395 1351 FKSVYGCSPTEF 1362
Cdd:PRK09978   228 FRNYYGMTPTEY 239
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
1119-1227 1.17e-06

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: 48.59  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNE---EV--RSYVREcldpHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKE---DLR--- 1187
Cdd:cd17563      2 SLLLVDDDEvfaERlaRALERR----GFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAlqpDARivv 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1800169395 1188 -TGH--IPvilmTArsmVMHIKegfsAGADDYIVKPFNMDVLI 1227
Cdd:cd17563     78 lTGYasIA----TA---VEAIK----LGADDYLAKPADADEIL 109
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1118-1231 1.24e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 51.01  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1118 YTVLLVEDNEEVRSYVRECL--DPHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIpvI 1194
Cdd:PRK10403     7 FQVLIVDDHPLMRRGVRQLLelDPGFEVVaEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQI--I 84
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395 1195 LMTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:PRK10403    85 ILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIR 121
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1116-1243 1.24e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 52.07  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1116 KKYTVLLVEDNEEVRSYVRECL--DPHFFVL-EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLelcTLIKEDLRTGHIP 1192
Cdd:PRK00742     2 MKIRVLVVDDSAFMRRLISEILnsDPDIEVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGL---DALEKIMRLRPTP 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800169395 1193 VIL---MTAR----SMvmhikEGFSAGADDYIVKPF-----NMD----VLIYRIRNilASREKLRSL 1243
Cdd:PRK00742    79 VVMvssLTERgaeiTL-----RALELGAVDFVTKPFlgislGMDeykeELAEKVRA--AARARVRAL 138
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
1120-1220 1.37e-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: 47.88  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLD-PHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdLRTGhIPVILMTA 1198
Cdd:cd19928      1 ILVADDDRAIRTVLTQALGrAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKK-ARPD-LPIIVMSA 78
                           90       100
                   ....*....|....*....|..
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd19928     79 QNTLMTAVKAAERGAFEYLPKP 100
PRK10336 PRK10336
two-component system response regulator QseB;
1120-1221 1.56e-06

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 50.66  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDPHFFVLE-ADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIPVILMTA 1198
Cdd:PRK10336     3 ILLIEDDMLIGDGIKTGLSKMGFSVDwFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQ--REPVLILTA 80
                           90       100
                   ....*....|....*....|...
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPF 1221
Cdd:PRK10336    81 RDALAERVEGLRLGADDYLCKPF 103
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
959-1083 1.66e-06

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 52.61  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  959 VVFNLLSNAFKYT--QAGGEIVLSVAklklkdvpagqrkeleslSEDTELvHLFVSDTGKGIPEEEMKNIFAPFYQI--E 1034
Cdd:PRK11086   437 ILGNLIENALEAVggEEGGEISVSLH------------------YRNGWL-HCEVSDDGPGIAPDEIDAIFDKGYSTkgS 497
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1035 DRkakdvagtGIGLSLT-QSIVRLhHGTIRVENNARGGATFHVLFPIDRR 1083
Cdd:PRK11086   498 NR--------GVGLYLVkQSVENL-GGSIAVESEPGVGTQFFVQIPWDGE 538
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1115-1219 1.95e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 50.41  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1115 EKKYTVLLVEDNEEVRSYVRECL--DPHF-FVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHI 1191
Cdd:PRK10651     4 QEPATILLIDDHPMLRTGVKQLIsmAPDItVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRI 83
                           90       100
                   ....*....|....*....|....*...
gi 1800169395 1192 pvILMTARSMVMHIKEGFSAGADDYIVK 1219
Cdd:PRK10651    84 --VVFSVSNHEEDVVTALKRGADGYLLK 109
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
1248-1363 2.83e-06

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 50.83  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1248 FSPEAIGVEIVSGTDRFTQKFFEVIERNIANpELNIDLICREVGLSRTNLYRKLKAiTELSPVELIRNKRLEVAARLLLE 1327
Cdd:PRK15186   166 YEPEAFALFRELSQNTLAENIYNIIISDISR-KWALKDISDSLYMSCSTLKRKLKQ-ENTSFSEVYLNARMNKATKLLRN 243
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1800169395 1328 SDYSVSEISTCVGFNSHAYFTQCFKSVYGCSPTEFL 1363
Cdd:PRK15186   244 SEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEFL 279
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
963-1083 7.19e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 50.02  E-value: 7.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  963 LLSNAFKY----TQAGGEIVLSVaklklkdvpagqrkeleslSEDTELVHLFVSDTGKGIPEEEMKNIFAPFYQIEDrka 1038
Cdd:COG2972    344 LVENAIEHgiepKEGGGTIRISI-------------------RKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKGE--- 401
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1039 kdvaGTGIGLSLTQSIVRLHHG---TIRVENNARGGATFHVLFPIDRR 1083
Cdd:COG2972    402 ----GRGIGLRNVRERLKLYYGeeyGLEIESEPGEGTTVTIRIPLEEE 445
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
952-1078 8.28e-06

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 50.02  E-value: 8.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  952 DKSLFEKVVFNLLSNAFKYTqaggeivlsvakLKLKDVPAGQrkeleslSEDTelVHLFVSDTGKGIPEEEMKNIFapfy 1031
Cdd:PRK10815   375 EKNDFMEVMGNVLDNACKYC------------LEFVEISARQ-------TDEH--LHIVVEDDGPGIPESKRELIF---- 429
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1032 qieDRKAK-DV--AGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLF 1078
Cdd:PRK10815   430 ---DRGQRaDTlrPGQGLGLSVAREITEQYEGKISAGDSPLGGARMEVIF 476
glnL PRK11073
nitrogen regulation protein NR(II);
957-1080 8.58e-06

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 49.69  E-value: 8.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  957 EKVVFNLLSNAFK-YTQAGGEIVL---SVAKLKLKdvpaGQRKELESLSEdtelvhlfVSDTGKGIPEEEMKNIFAPFyq 1032
Cdd:PRK11073   239 EQVLLNIVRNALQaLGPEGGTITLrtrTAFQLTLH----GERYRLAARID--------IEDNGPGIPPHLQDTLFYPM-- 304
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1800169395 1033 IEDRKAkdvaGTGIGLSLTQSIVRLHHGTIRVeNNARGGATFHVLFPI 1080
Cdd:PRK11073   305 VSGREG----GTGLGLSIARNLIDQHSGKIEF-TSWPGHTEFSVYLPI 347
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
1292-1361 2.45e-05

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 47.75  E-value: 2.45e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1292 LSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCFKSVYGCSPTE 1361
Cdd:PRK13503   199 LSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRD 268
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
926-1079 2.75e-05

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 48.68  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  926 AFN--QIAS---GKEIRFRYEGGEVGIV---------AWFDKSLFEKVVFNLLSNAFKytqaggeivlsvAKLKlkdVPA 991
Cdd:PRK15053   389 AFAdrQVAGllfGKVQRARELGLKMVIVpgsqlsqlpPGLDSTEFAAIVGNLLDNAFE------------ASLR---SDE 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  992 GQRKELESLSEDTELVHLFVSDTGKGIPEEEMKNIFApfyQIEDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGG 1071
Cdd:PRK15053   454 GNKIVELFLSDEGDDVVIEVADQGCGVPESLRDKIFE---QGVSTRADEPGEHGIGLYLIASYVTRCGGVITLEDNDPCG 530

                   ....*...
gi 1800169395 1072 ATFHVLFP 1079
Cdd:PRK15053   531 TLFSIFIP 538
PRK10360 PRK10360
transcriptional regulator UhpA;
1119-1314 3.11e-05

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 46.51  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECL--DPHF-FVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTghipvIL 1195
Cdd:PRK10360     3 TVALIDDHLIVRSGFAQLLglEPDLqVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQLPKGMAT-----IM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1196 MTARSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIRNILASreklrslyGKKFSPEaIGVEIVSGT-DRFTQKFFEVIER 1274
Cdd:PRK10360    78 LSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTVATG--------GCYLTPD-IAIKLASGRqDPLTKRERQVAEK 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1800169395 1275 nIANpELNIDLICREVGLS-------RTNLYRKLKAITElspVELIR 1314
Cdd:PRK10360   149 -LAQ-GMAVKEIAAELGLSpktvhvhRANLMEKLGVSND---VELAR 190
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1120-1226 3.21e-05

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: 44.45  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECL--DPHFFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLE-LCTLIKEDLRTGHIPV--- 1193
Cdd:cd17593      3 VLICDDSSMARKQLARALpaDWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEvLEALPVEQLETKVIVVsgd 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1800169395 1194 ILMTARSMVMhikegfSAGADDYIVKPFNMDVL 1226
Cdd:cd17593     83 VQPEAKERVL------ELGALAFLKKPFDPEKL 109
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
1283-1363 3.25e-05

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 47.68  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1283 IDLICREVGLSRTNLYRKLkAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCFKSVYGCSPTEF 1362
Cdd:PRK15185   225 LTDVADHIFMSTSTLKRKL-AEEGTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPSTF 303

                   .
gi 1800169395 1363 L 1363
Cdd:PRK15185   304 I 304
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
1120-1231 4.46e-05

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 44.23  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVRSYVRECLDP-HFFVLEADnGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIPVILMTA 1198
Cdd:cd17539      1 VLLVDDRPSSAERIAAMLSSeHEVVVEAD-PDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVAD 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1800169395 1199 RSMVMHIKEGFSAGADDYIVKPFNMDVLIYRIR 1231
Cdd:cd17539     80 PGDRGRLIRALEIGVNDYLVRPIDPNELLARVR 112
PRK09483 PRK09483
response regulator; Provisional
1119-1242 5.21e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 45.87  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPH---FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIkedLR-TGHIPVI 1194
Cdd:PRK09483     3 NVLLVDDHELVRAGIRRILEDIkgiKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKI---LRyTPDVKII 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1800169395 1195 LMTAR------SMVMHikegfsAGADDYIVKPFNMDVLIYRIRNILASREKLRS 1242
Cdd:PRK09483    80 MLTVHtenplpAKVMQ------AGAAGYLSKGAAPQEVVSAIRSVHSGQRYIAS 127
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
1119-1264 6.64e-05

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 45.66  E-value: 6.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHFFVL--EADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEDLRTGHIpvILM 1196
Cdd:PRK09958     2 NAIIIDDHPLAIAAIRNLLIKNDIEIlaELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGII--IIV 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800169395 1197 TARSMVMHIKEGFSAGADDYIVKPFNMDvliyrirNILASREKLRSLYGK-KFSPEAIGVEIVSGTDRF 1264
Cdd:PRK09958    80 SAKNDHFYGKHCADAGANGFVSKKEGMN-------NIIAAIEAAKNGYCYfPFSLNRFVGSLTSDQQKL 141
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
1119-1198 1.82e-04

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: 42.43  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1119 TVLLVEDNEEVRSYVRECLDPHFF--VLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELctLIKEDLRTGHIPVILM 1196
Cdd:cd17530      2 RVLVLDDDPFQCMMAATILEDLGPgnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEF--LRHLAESHSNAAVILM 79

                   ..
gi 1800169395 1197 TA 1198
Cdd:cd17530     80 SG 81
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
1272-1362 2.58e-04

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 42.40  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1272 IERNIANPeLNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCF 1351
Cdd:PRK11511    18 IEDNLESP-LSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLTRTF 96
                           90
                   ....*....|.
gi 1800169395 1352 KSVYGCSPTEF 1362
Cdd:PRK11511    97 KNYFDVPPHKY 107
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
51-162 4.47e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 43.85  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395   51 DSKGYMWF--GTRNGLNKYDGNRMVVykhlDSDSLSLVDNHITAIVEDRKNCLWVgTSRGLN---RLDLKTDRITPYAGK 125
Cdd:COG4257    110 DPDGNLWFtdQGGNRIGRLDPATGEV----TEFPLPTGGAGPYGIAVDPDGNLWV-TDFGANaigRIDPDTGTLTEYALP 184
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1800169395  126 NfslLDSGVRSLFIDSNDRLWVGTSKGLYLFVHEADT 162
Cdd:COG4257    185 T---PGAGPRGLAVDPDGNLWVADTGSGRIGRFDPKT 218
PRK15115 PRK15115
response regulator GlrR; Provisional
1141-1237 4.83e-04

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 44.44  E-value: 4.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1141 FFVLEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVILMTARSmvmHIKEGFSA---GADDYI 1217
Cdd:PRK15115    30 YSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQK--VQPGMPVIILTAHG---SIPDAVAAtqqGVFSFL 104
                           90       100
                   ....*....|....*....|
gi 1800169395 1218 VKPFNMDVLIYRIRNILASR 1237
Cdd:PRK15115   105 TKPVDRDALYKAIDDALEQS 124
ftrA PRK09393
transcriptional activator FtrA; Provisional
1280-1360 5.14e-04

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 43.80  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1280 ELNIDLICREVGLSRTNLYRKLKAITELSPVELIRNKRLEVAARLLLESDYSVSEISTCVGFNSHAYFTQCFKSVYGCSP 1359
Cdd:PRK09393   234 PHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSP 313

                   .
gi 1800169395 1360 T 1360
Cdd:PRK09393   314 A 314
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
316-581 5.34e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 43.47  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  316 YSICVDNSGNVWVGTYSGG-VNYFSKYNNRFVFHePTNALNMLMGVY----GAmacqpphcLYIATEGGGLLdYHLESNT 390
Cdd:COG4257     20 RDVAVDPDGAVWFTDQGGGrIGRLDPATGEFTEY-PLGGGSGPHGIAvdpdGN--------LWFTDNGNNRI-GRIDPKT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  391 YQYYLYDTSSSQQYSRNIiksVMQEKDYIW-CGTTQGSIYRFDTRSKRFSLYYAfPLHQSTSvYSILRTQDNNLWLATSK 469
Cdd:COG4257     90 GEITTFALPGGGSNPHGI---AFDPDGNLWfTDQGGNRIGRLDPATGEVTEFPL-PTGGAGP-YGIAVDPDGNLWVTDFG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  470 --------PEVGLVK---LTEERKMQNRFELADSGRIWtpgssrcllelekgvlLVGSRNNGLYKYDENKRECTVFSKNG 538
Cdd:COG4257    165 anaigridPDTGTLTeyaLPTPGAGPRGLAVDPDGNLW----------------VADTGSGRIGRFDPKTGTVTEYPLPG 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1800169395  539 KGAnhLPadyvTSLVRTKSGQIWVGTFGGG-LSLFDQEKGIVKY 581
Cdd:COG4257    229 GGA--RP----YGVAVDGDGRVWFAESGANrIVRFDPDTELTEY 266
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
959-1063 5.35e-04

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 41.10  E-value: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  959 VVFNLLSNAFKYTQA-GGEIVLSVAKLKlkdvpagqrkelESLSEDTELVHL-F-VSDTGKGIPEEEMKNIFapfyqied 1035
Cdd:cd16932     10 VLADFLLNAVRFTPSpGGWVEIKVSPTK------------KQIGDGVHVIHLeFrITHPGQGLPEELVQEMF-------- 69
                           90       100
                   ....*....|....*....|....*...
gi 1800169395 1036 RKAKDVAGTGIGLSLTQSIVRLHHGTIR 1063
Cdd:cd16932     70 EENQWTTQEGLGLSISRKLVKLMNGDVR 97
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
931-1083 1.02e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 42.30  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  931 ASGKEIRFRYEGGEVGIVAWFDKSLFeKVVFNLLSNAFKYTQAGgEIVLSvaklklkdvpagqrkelesLSEDTELVHLF 1010
Cdd:COG4585    139 AAGIRVELDVDGDPDRLPPEVELALY-RIVQEALTNALKHAGAT-RVTVT-------------------LEVDDGELTLT 197
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800169395 1011 VSDTGKGIPEEEmknifapfyqiedrkakdVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVLFPIDRR 1083
Cdd:COG4585    198 VRDDGVGFDPEA------------------APGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLAAA 252
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
1328-1363 1.82e-03

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 37.52  E-value: 1.82e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1800169395 1328 SDYSVSEISTCVGFNSHaYFTQCFKSVYGCSPTEFL 1363
Cdd:pfam00165    7 TNLTIADIADELGFSRS-YFSRLFKKYTGVTPSQYR 41
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
1272-1314 2.50e-03

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 37.13  E-value: 2.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1800169395 1272 IERNIANpELNIDLICREVGLSRTNLYRKLKAITELSPVELIR 1314
Cdd:pfam00165    1 LRENLST-NLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
220-435 2.82e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 41.16  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  220 PDNNISDIHEDSRKQLWVSTNYGG-VSKVDLSTG--TSVHYTTANSKLTTdnirCLAEADGTLFIGTFDG--LYTIDLTD 294
Cdd:COG4257     57 GGSGPHGIAVDPDGNLWFTDNGNNrIGRIDPKTGeiTTFALPGGGSNPHG----IAFDPDGNLWFTDQGGnrIGRLDPAT 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  295 NQLKgrsnaaLEKGTLSHFSIYSICVDNSGNVWVGTYSGG-VNYFSKYNNRFVFHEPTNALNMLMGVY----GAmacqpp 369
Cdd:COG4257    133 GEVT------EFPLPTGGAGPYGIAVDPDGNLWVTDFGANaIGRIDPDTGTLTEYALPTPGAGPRGLAvdpdGN------ 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800169395  370 hcLYIA-TEGGGLLDYHLESNTYQYYLYDTSSSQQYSrniikSVMQEKDYIWCGTTQ-GSIYRFDTRS 435
Cdd:COG4257    201 --LWVAdTGSGRIGRFDPKTGTVTEYPLPGGGARPYG-----VAVDGDGRVWFAESGaNRIVRFDPDT 261
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
51-150 2.94e-03

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 41.03  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395   51 DSKGYMWFGtrnglnkyD--GNRMVVYkHLDSDSLSLV---DNHITAIVEDRKNCLWVG-TSRGLNRLDLKTDRITPYA- 123
Cdd:COG3386     16 DPDGRLYWV--------DipGGRIHRY-DPDGGAVEVFaepSGRPNGLAFDPDGRLLVAdHGRGLVRFDPADGEVTVLAd 86
                           90       100
                   ....*....|....*....|....*....
gi 1800169395  124 --GKNFSLLDSGVrslfIDSNDRLWVGTS 150
Cdd:COG3386     87 eyGKPLNRPNDGV----VDPDGRLYFTDM 111
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
511-655 4.89e-03

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 40.65  E-value: 4.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  511 VLLVGSRNNGLYKYDENKRECTVFskngkganHLPADYVTSLVRTKSGQIWVGTFGGGLSLFDQEKGIVKYITKKEGL-- 588
Cdd:COG3386     21 LYWVDIPGGRIHRYDPDGGAVEVF--------AEPSGRPNGLAFDPDGRLLVADHGRGLVRFDPADGEVTVLADEYGKpl 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  589 --LDDevcMVVeDRNGDLWMSTnsciSRYNPKTDEVYnYYMDNGigaqEFSP-HSGMLLPDGnICFSANN 655
Cdd:COG3386     93 nrPND---GVV-DPDGRLYFTD----MGEYLPTGALY-RVDPDG----SLRVlADGLTFPNG-IAFSPDG 148
PRK10430 PRK10430
two-component system response regulator DcuR;
1120-1221 5.32e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 40.09  E-value: 5.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEV----RSYVRECldPHFFVL-EADNGETAFEIVLDK--YPDIVVSDIMMPRKDGLELCTLIKEDLRtgHIP 1192
Cdd:PRK10430     4 VLIVDDDAMVaelnRRYVAQI--PGFQCCgTASTLEQAKEIIFNSdtPIDLILLDIYMQQENGLDLLPVLHEAGC--KSD 79
                           90       100
                   ....*....|....*....|....*....
gi 1800169395 1193 VILMTARSMVMHIKEGFSAGADDYIVKPF 1221
Cdd:PRK10430    80 VIVISSAADAATIKDSLHYGVVDYLIKPF 108
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
84-107 6.48e-03

Two component regulator propeller; A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats. These repeats show homology to pfam01011 and pfam00400 indicating that they are likely to form a beta-propeller. This family has been built with artificially high cut-offs in order to avoid overlaps with other beta-propeller families. The fourteen repeats are likely to form two propellers; it is not clear if these structures are likely to recruit other proteins or interact with DNA.


Pssm-ID: 400050 [Multi-domain]  Cd Length: 24  Bit Score: 35.37  E-value: 6.48e-03
                           10        20
                   ....*....|....*....|....
gi 1800169395   84 SLVDNHITAIVEDRKNCLWVGTSR 107
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTNG 24
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
1120-1220 6.87e-03

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: 37.52  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395 1120 VLLVEDNEEVR-----SYVRECLDPHffvlEADNGETAFEIVLDKYPDIVVSDIMMPRKDGLELCTLIKEdlRTGHIPVI 1194
Cdd:cd19926      1 VLVVDDEPDIRelleiTLGRMGLDVR----SARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQ--RLPQTPVA 74
                           90       100
                   ....*....|....*....|....*.
gi 1800169395 1195 LMTARSMVMHIKEGFSAGADDYIVKP 1220
Cdd:cd19926     75 VITAYGSLDTAIEALKAGAFDFLTKP 100
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
959-1077 8.54e-03

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 38.21  E-value: 8.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800169395  959 VVFNLLSNAFKYTQAGGEIVLSVAklkLKDVPAGQRKELE-----SLSEDTELVHLFVSDTGKGIPEEEMKNIFApfyQI 1033
Cdd:cd16938     15 VLLHMLGNLLKMRNGGGNITFRVF---LEGGSEDRSDRDWgpwrpSMSDESVEIRFEVEINDSGSPSIESASMRN---SL 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1800169395 1034 EDRKAKDVAGTGIGLSLTQSIVRLHHGTIRVENNARGGATFHVL 1077
Cdd:cd16938     89 NRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLL 132
 
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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