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Conserved domains on  [gi|1735101206|gb|QEM08915|]
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response regulator [Mucilaginibacter rubeus]

Protein Classification

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];
7-1113 1.96e-107

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


:

Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 363.15  E-value: 1.96e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206    7 FCIVLFLIISLAHAQSPIKNKILNYSLKNGLSFGIVNSITQDDKGFMWFATNDGLNRFDGTTFKVFKSRAGDSTALASNY 86
Cdd:COG3292      3 LLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206   87 VQKVLCDVHGNIWASSRNGLSKLDTRTEKFVHYKLKLSRAvKSDIGNITQSHDGNLWITSYNlGFSYFDIKTASFINYTQ 166
Cdd:COG3292     83 IRALLEDSDGRLWIGTDGGLSRYDPKTDKFTRYPLDPGLP-NNSIRSIAEDSDGNIWVGTSN-GLYRYDPKTGKFKRFTL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  167 INLPrlaSNRVICLFEDSKGLLWVgtqegninifrhkggliskadgltpqianlpttrindifeDHFHNIWIAT-GSGLI 245
Cdd:COG3292    161 DGLP---SNTITSLAEDADGNLWV----------------------------------------DSDGNLWIGTdGNGLY 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  246 YYNRQTNKFTLLQANqpgikskryisvnedndnqllvglqdgglfklnigsnpnfntanyflqpvtgDDGFYLTQRSVQT 325
Cdd:COG3292    198 RLDPNTGKFEHITHD----------------------------------------------------PDPNSLSSNSIYS 225
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  326 LFIDKDKNVWVGTYGDGIYMISSIKEKFSLITKKKYETSGESPIRfyGMCQDRDGFLWLgtdgeglfktsrngtlikqyk 405
Cdd:COG3292    226 LFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRHNDPNGLSGNSVR--SIAEDSDGNLWI--------------------- 282
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  406 adgragsitdnailygytdsngNVWFGTYAKGLLLYNKKTDSFTSYahnasDSKSLGGNDVRVIYQDSRKNIWIGTNGGG 485
Cdd:COG3292    283 ----------------------RLWIGTYGGGLFRLDPKTGKFKRY-----NPNGLPSNSVYSILEDSDGNLWIGTSGGG 335
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  486 LSLFDPVSKTFSNFTPANsGLTAYDVRAITEDEQGNLWIGTYgGGLDFYDIRQKKFSRYFTPIDeRNNLPGQVIFSLYVD 565
Cdd:COG3292    336 LYRYDPKTGKFTKFSEDN-GLSNNFIRSILEDSDGNLWVGTN-GGLYRLDPKTGKFTNFTHDPD-KNGLSSNYINSIFED 412
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  566 KYRRLWIATEGDGLIAYDLKKRVFKKFNETNGLANNTVSAFKEVADGTLWMSTNKglsnlnpatgkilnydqsdglqagq 645
Cdd:COG3292    413 SDGRLWIGTDGGGLYRYDPKTGKFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSA------------------------- 467
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  646 fnagsvlFDADNSLVYFGGTEGLNFFDPAKVNKSNYQPKVIITGLQIFGKqvEVGEQDKNRTVLTQAINETQQITLGPDQ 725
Cdd:COG3292    468 -------SNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLS--LVRSLISLLTLLLLALLLLLSLLLLLLL 538
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  726 SVFSIQYASLNYTYPDKGGFAYKLDGLDKTWnyvgdQRLATYRYLEPGVYTFRVKASNQDGLWFDNCATLQVKILPPWYK 805
Cdd:COG3292    539 LLLLLLLLLLLLLLLLLLILLLLLLRLLLLL-----LLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLL 613
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  806 TWWAYLIYIAAAGLVTYYYILYKSRQTRLKYEVKVAQLSAEKDKELNERKLSFFTNISHEFRTPLTLIINPVKDMLFgks 885
Cdd:COG3292    614 LLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLL--- 690
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  886 EATDDAGNLHIIYKNARRLLSLVDQLLLFRKAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIY 965
Cdd:COG3292    691 ALLLLLLLLLALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLE 770
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  966 ADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYL 1045
Cdd:COG3292    771 LLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLL 850
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735101206 1046 VKAFIEHHKGTITYTSKQDQGTTFHVSLLKGKEHFGQQFIFEDVAETSVFLDELMENKGELVTVEAEN 1113
Cdd:COG3292    851 GLLLLLLLEILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIELLLEEE 918
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1128-1332 7.16e-40

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: 147.02  E-value: 7.16e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1128 TKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVIL 1206
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKsRNNLQKYFYNEITLNKSNDLKISQEykeflekclqivEQ 1286
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR-RRAAEVLRVGDLLDLAAREVTRDGE------------PV 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1287 HLTDPDFSI-KTLAAEIG--MSHSNLYKRIKSISGQSANSFIRFI-RLRK 1332
Cdd:COG0745    146 ELTPKEFRLlELLMRNPGrvVSREQLLEEVWGYDYGDDRTVDVHIsRLRK 195
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1292-1374 1.10e-18

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 81.83  E-value: 1.10e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  1292 DFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKLFGINP 1371
Cdd:smart00342    1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                    ...
gi 1735101206  1372 SDY 1374
Cdd:smart00342   81 SEY 83
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
7-1113 1.96e-107

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 363.15  E-value: 1.96e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206    7 FCIVLFLIISLAHAQSPIKNKILNYSLKNGLSFGIVNSITQDDKGFMWFATNDGLNRFDGTTFKVFKSRAGDSTALASNY 86
Cdd:COG3292      3 LLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206   87 VQKVLCDVHGNIWASSRNGLSKLDTRTEKFVHYKLKLSRAvKSDIGNITQSHDGNLWITSYNlGFSYFDIKTASFINYTQ 166
Cdd:COG3292     83 IRALLEDSDGRLWIGTDGGLSRYDPKTDKFTRYPLDPGLP-NNSIRSIAEDSDGNIWVGTSN-GLYRYDPKTGKFKRFTL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  167 INLPrlaSNRVICLFEDSKGLLWVgtqegninifrhkggliskadgltpqianlpttrindifeDHFHNIWIAT-GSGLI 245
Cdd:COG3292    161 DGLP---SNTITSLAEDADGNLWV----------------------------------------DSDGNLWIGTdGNGLY 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  246 YYNRQTNKFTLLQANqpgikskryisvnedndnqllvglqdgglfklnigsnpnfntanyflqpvtgDDGFYLTQRSVQT 325
Cdd:COG3292    198 RLDPNTGKFEHITHD----------------------------------------------------PDPNSLSSNSIYS 225
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  326 LFIDKDKNVWVGTYGDGIYMISSIKEKFSLITKKKYETSGESPIRfyGMCQDRDGFLWLgtdgeglfktsrngtlikqyk 405
Cdd:COG3292    226 LFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRHNDPNGLSGNSVR--SIAEDSDGNLWI--------------------- 282
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  406 adgragsitdnailygytdsngNVWFGTYAKGLLLYNKKTDSFTSYahnasDSKSLGGNDVRVIYQDSRKNIWIGTNGGG 485
Cdd:COG3292    283 ----------------------RLWIGTYGGGLFRLDPKTGKFKRY-----NPNGLPSNSVYSILEDSDGNLWIGTSGGG 335
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  486 LSLFDPVSKTFSNFTPANsGLTAYDVRAITEDEQGNLWIGTYgGGLDFYDIRQKKFSRYFTPIDeRNNLPGQVIFSLYVD 565
Cdd:COG3292    336 LYRYDPKTGKFTKFSEDN-GLSNNFIRSILEDSDGNLWVGTN-GGLYRLDPKTGKFTNFTHDPD-KNGLSSNYINSIFED 412
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  566 KYRRLWIATEGDGLIAYDLKKRVFKKFNETNGLANNTVSAFKEVADGTLWMSTNKglsnlnpatgkilnydqsdglqagq 645
Cdd:COG3292    413 SDGRLWIGTDGGGLYRYDPKTGKFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSA------------------------- 467
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  646 fnagsvlFDADNSLVYFGGTEGLNFFDPAKVNKSNYQPKVIITGLQIFGKqvEVGEQDKNRTVLTQAINETQQITLGPDQ 725
Cdd:COG3292    468 -------SNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLS--LVRSLISLLTLLLLALLLLLSLLLLLLL 538
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  726 SVFSIQYASLNYTYPDKGGFAYKLDGLDKTWnyvgdQRLATYRYLEPGVYTFRVKASNQDGLWFDNCATLQVKILPPWYK 805
Cdd:COG3292    539 LLLLLLLLLLLLLLLLLLILLLLLLRLLLLL-----LLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLL 613
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  806 TWWAYLIYIAAAGLVTYYYILYKSRQTRLKYEVKVAQLSAEKDKELNERKLSFFTNISHEFRTPLTLIINPVKDMLFgks 885
Cdd:COG3292    614 LLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLL--- 690
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  886 EATDDAGNLHIIYKNARRLLSLVDQLLLFRKAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIY 965
Cdd:COG3292    691 ALLLLLLLLLALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLE 770
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  966 ADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYL 1045
Cdd:COG3292    771 LLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLL 850
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735101206 1046 VKAFIEHHKGTITYTSKQDQGTTFHVSLLKGKEHFGQQFIFEDVAETSVFLDELMENKGELVTVEAEN 1113
Cdd:COG3292    851 GLLLLLLLEILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIELLLEEE 918
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1128-1332 7.16e-40

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: 147.02  E-value: 7.16e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1128 TKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVIL 1206
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKsRNNLQKYFYNEITLNKSNDLKISQEykeflekclqivEQ 1286
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR-RRAAEVLRVGDLLDLAAREVTRDGE------------PV 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1287 HLTDPDFSI-KTLAAEIG--MSHSNLYKRIKSISGQSANSFIRFI-RLRK 1332
Cdd:COG0745    146 ELTPKEFRLlELLMRNPGrvVSREQLLEEVWGYDYGDDRTVDVHIsRLRK 195
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1130-1232 1.48e-34

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: 128.00  E-value: 1.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLT 1208
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPF 1232
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
966-1073 7.73e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.45  E-value: 7.73e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206   966 ADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYL 1045
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGTGLGLSI 80
                            90       100
                    ....*....|....*....|....*...
gi 1735101206  1046 VKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITL 108
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1132-1242 2.65e-31

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: 118.79  E-value: 2.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTAS 1210
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTAH 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARVN 1242
Cdd:pfam00072   80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
971-1073 4.97e-29

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: 111.93  E-value: 4.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  971 MEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPlAGGFGIGLYLVKAFI 1050
Cdd:cd00075      1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSRE-GGGTGLGLAIVRRIV 79
                           90       100
                   ....*....|....*....|...
gi 1735101206 1051 EHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd00075     80 EAHGGRITVESEPGGGTTFTVTL 102
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
1127-1246 8.75e-27

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: 110.11  E-value: 8.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1127 DTKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVI 1205
Cdd:TIGR02154    1 MTRRILVVEDEPAIRELIAYNLEKAgYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPII 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1735101206 1206 LLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:TIGR02154   81 MLTARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLR 121
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
966-1073 9.05e-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: 100.14  E-value: 9.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  966 ADREKMEIALFNLISNALKFTPDFGLVTCTInDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAplAGGFGIGLYL 1045
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAGEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRG--GGGTGLGLSI 77
                           90       100
                   ....*....|....*....|....*...
gi 1735101206 1046 VKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:pfam02518   78 VRKLVELLGGTITVESEPGGGTTVTLTL 105
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
846-1073 2.76e-22

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: 103.29  E-value: 2.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  846 EKDKELNERKlSFFTNISHEFRTPLTLIinpvkdmlfgKS--EATDD--------AGN-LHIIYKNARRllslvdqllLF 914
Cdd:NF033092   364 EQEKIEQERR-EFVANVSHELRTPLTTM----------RSylEALADgawkdpelAPRfLGVTQNETER---------MI 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  915 R---------KAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQF--DFISEKDTIEIyaDREKMEIALFNLISNAL 983
Cdd:NF033092   424 RlvndllqlsRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFkrEFPKRDLWVEI--DTDKITQVLDNIISNAI 501
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  984 KFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFY--------QLqnsaplaGGFGIGLYLVKAFIEHHKG 1055
Cdd:NF033092   502 KYSPEGGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFYrvdkarsrKM-------GGTGLGLAIAKEVVEAHGG 574
                          250
                   ....*....|....*...
gi 1735101206 1056 TITYTSKQDQGTTFHVSL 1073
Cdd:NF033092   575 RIWAESEEGKGTTIYFTL 592
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
840-1343 3.54e-22

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 104.05  E-value: 3.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  840 VAQLSAEKDKELNER--KLSFFTNISHEFRTPLTLIINPVkDMLFGKSEATDD-AGNLHIIYKNARRLLSLVDQLLLFRK 916
Cdd:PRK09959   695 IHALEVERNKAINATvaKSQFLATMSHEIRTPISSIMGFL-ELLSGSGLSKEQrVEAISLAYATGQSLLGLIGEILDVDK 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  917 AESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISE-KDTIEIYADREKMEIALFNLISNALKFTPDfGLVTCT 995
Cdd:PRK09959   774 IESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPDHYLVKIDPQAFKQVLSNLLSNALKFTTE-GAVKIT 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  996 -----INDTGNGITINIKDSGCGIAEGTGDELFGKFYQlQNSAPLAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFH 1070
Cdd:PRK09959   853 tslghIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ-TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFT 931
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1071 VSLlkgkehfgqqfifedvaetsvfldelmenkgeLVTVEAENTAVAAKNSEALSSDTKTMLLI-DDNQQIRTYLK-QIF 1148
Cdd:PRK09959   932 ITI--------------------------------PVEISQQVATVEAKAEQPITLPEKLSILIaDDHPTNRLLLKrQLN 979
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1149 SGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTASSSPEIKLKGIEGGADDYI 1228
Cdd:PRK09959   980 LLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPIWGLTANAQANEREKGLSCGMNLCL 1057
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1229 SKPFEKEILVARVNGILKSRNNLQKYFYNEITL---NKSNDLKISQEykeflekcLQIVEQHLTDPDFSIKTLAAEIGmS 1305
Cdd:PRK09959  1058 FKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEAlknNTANDLQLMQE--------ILMTFQHETHKDLPAAFHALEAG-D 1128
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1306 HSNLYKRIKSISGqSAN--SFIRFIRLRKAAEILLTTDST 1343
Cdd:PRK09959  1129 NRTFHQCIHRIHG-AANilNLQKLINISHQLEITPVSDDS 1167
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
833-1247 4.11e-22

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: 103.70  E-value: 4.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  833 RLKYEVKVAQLSAEKDKELNERKLSFFTNISHEFRTPLTLIINPVKdMLFGKSEATDDAGNLHIIYKNARRLLSLVDQLL 912
Cdd:TIGR02956  442 RLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDIL 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  913 LFRKAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDF-ISEKDTIEIYADREKMEIALFNLISNALKFTpDFGL 991
Cdd:TIGR02956  521 DYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLnIPEQLPNWWQGDGPRIRQVLINLVGNAIKFT-DRGS 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  992 VTCTIN-DTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPlAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFH 1070
Cdd:TIGR02956  600 VVLRVSlNDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGRRR-SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFW 678
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1071 VSLlkgkehfgqQFIFEDVAETSVFLdelmenkgelvtveaentavaaknsEALSSDTKTMLLIDDNQqirtyLKQIFSG 1150
Cdd:TIGR02956  679 FTL---------PLTRGKPAEDSATL-------------------------TVIDLPPQRVLLVEDNE-----VNQMVAQ 719
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1151 EF------EIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKE-DAVLNHIPVILLTASSSPEIKLKGIEGG 1223
Cdd:TIGR02956  720 GFltrlghKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAiYGAKNEVKFIAFSAHVFNEDVAQYLAAG 799
                          410       420
                   ....*....|....*....|....
gi 1735101206 1224 ADDYISKPFEKEILVARVNGILKS 1247
Cdd:TIGR02956  800 FDGFLAKPVVEEQLTAMIAVILAG 823
pleD PRK09581
response regulator PleD; Reviewed
1152-1241 5.52e-21

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 98.05  E-value: 5.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1152 FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTASSSPEIKLKGIEGGADDYISKP 1231
Cdd:PRK09581    27 YTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKP 106
                           90
                   ....*....|
gi 1735101206 1232 FEKEILVARV 1241
Cdd:PRK09581   107 INDVALFARV 116
resp_reg_YycF NF040534
response regulator YycF;
1129-1246 2.28e-20

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 91.71  E-value: 2.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavlNHIPVILL 1207
Cdd:NF040534     1 KKILVVDDEKPIADILEFNLKKEgYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKK---YDMPIIML 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:NF040534    78 TAKDSEIDKVLGLELGADDYVTKPFSTRELIARVKANLR 116
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
1132-1241 5.31e-20

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 90.31  E-value: 5.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTAS 1210
Cdd:NF040689     2 LVVDDDPALAEMLGIVLRAEgFETVFCADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIRAES---GVPIIMLTAK 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:NF040689    79 SDTVDVVRGLEAGADDYVVKPFKPKELVARI 109
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1292-1374 1.10e-18

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 81.83  E-value: 1.10e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  1292 DFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKLFGINP 1371
Cdd:smart00342    1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                    ...
gi 1735101206  1372 SDY 1374
Cdd:smart00342   81 SEY 83
HTH_18 pfam12833
Helix-turn-helix domain;
1298-1377 2.39e-16

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 75.32  E-value: 2.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1298 LAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILL-TTDSTVYETAYKVGLNDLKYFREQFNKLFGINPSDYIK 1376
Cdd:pfam12833    1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80

                   .
gi 1735101206 1377 K 1377
Cdd:pfam12833   81 R 81
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1132-1181 2.34e-09

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: 54.50  E-value: 2.34e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1735101206  1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMM 1181
Cdd:smart00448    4 LVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMM 54
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
844-1057 1.63e-08

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 58.68  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  844 SAEKDKELNERklSFFTNISHEFRTPLTLIINPVKDMLFGKSEATDDagNLHIIYKNARRLLSLVDQLLLFRKAESDTDK 923
Cdd:NF012163   231 STLEKNEQMRR--DFMADISHELRTPLAVLRAELEAIQDGIRKFTPE--SLDSLQAEVGTLTKLVDDLHDLSMSDEGALA 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  924 LKIVRLNIVSLCHEVFLCFNHQ--ARTKHIQFDFiseKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGN 1001
Cdd:NF012163   307 YQKASVDLVPLLEVEGGAFRERfaSAGLELEVSL---PDSSLVFGDRDRLMQLFNNLLENSLRYTDSGGSLHISASQRPK 383
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1735101206 1002 GITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLA-GGFGIGLYLVKAFIEHHKGTI 1057
Cdd:NF012163   384 EVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRAsGGSGLGLAISLNIVQAHGGTL 440
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
1292-1385 2.24e-04

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 44.92  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1292 DFSIKTLAAEIGMSHSNLYKRIKSiSGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKLFGINP 1371
Cdd:PRK09978   158 EWTLARIASELLMSPSLLKKKLRE-EETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTP 236
                           90
                   ....*....|....
gi 1735101206 1372 SDYIKKYRKPFHNN 1385
Cdd:PRK09978   237 TEYQERSAQGLPNR 250
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
7-1113 1.96e-107

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 363.15  E-value: 1.96e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206    7 FCIVLFLIISLAHAQSPIKNKILNYSLKNGLSFGIVNSITQDDKGFMWFATNDGLNRFDGTTFKVFKSRAGDSTALASNY 86
Cdd:COG3292      3 LLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206   87 VQKVLCDVHGNIWASSRNGLSKLDTRTEKFVHYKLKLSRAvKSDIGNITQSHDGNLWITSYNlGFSYFDIKTASFINYTQ 166
Cdd:COG3292     83 IRALLEDSDGRLWIGTDGGLSRYDPKTDKFTRYPLDPGLP-NNSIRSIAEDSDGNIWVGTSN-GLYRYDPKTGKFKRFTL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  167 INLPrlaSNRVICLFEDSKGLLWVgtqegninifrhkggliskadgltpqianlpttrindifeDHFHNIWIAT-GSGLI 245
Cdd:COG3292    161 DGLP---SNTITSLAEDADGNLWV----------------------------------------DSDGNLWIGTdGNGLY 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  246 YYNRQTNKFTLLQANqpgikskryisvnedndnqllvglqdgglfklnigsnpnfntanyflqpvtgDDGFYLTQRSVQT 325
Cdd:COG3292    198 RLDPNTGKFEHITHD----------------------------------------------------PDPNSLSSNSIYS 225
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  326 LFIDKDKNVWVGTYGDGIYMISSIKEKFSLITKKKYETSGESPIRfyGMCQDRDGFLWLgtdgeglfktsrngtlikqyk 405
Cdd:COG3292    226 LFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRHNDPNGLSGNSVR--SIAEDSDGNLWI--------------------- 282
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  406 adgragsitdnailygytdsngNVWFGTYAKGLLLYNKKTDSFTSYahnasDSKSLGGNDVRVIYQDSRKNIWIGTNGGG 485
Cdd:COG3292    283 ----------------------RLWIGTYGGGLFRLDPKTGKFKRY-----NPNGLPSNSVYSILEDSDGNLWIGTSGGG 335
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  486 LSLFDPVSKTFSNFTPANsGLTAYDVRAITEDEQGNLWIGTYgGGLDFYDIRQKKFSRYFTPIDeRNNLPGQVIFSLYVD 565
Cdd:COG3292    336 LYRYDPKTGKFTKFSEDN-GLSNNFIRSILEDSDGNLWVGTN-GGLYRLDPKTGKFTNFTHDPD-KNGLSSNYINSIFED 412
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  566 KYRRLWIATEGDGLIAYDLKKRVFKKFNETNGLANNTVSAFKEVADGTLWMSTNKglsnlnpatgkilnydqsdglqagq 645
Cdd:COG3292    413 SDGRLWIGTDGGGLYRYDPKTGKFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSA------------------------- 467
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  646 fnagsvlFDADNSLVYFGGTEGLNFFDPAKVNKSNYQPKVIITGLQIFGKqvEVGEQDKNRTVLTQAINETQQITLGPDQ 725
Cdd:COG3292    468 -------SNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLS--LVRSLISLLTLLLLALLLLLSLLLLLLL 538
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  726 SVFSIQYASLNYTYPDKGGFAYKLDGLDKTWnyvgdQRLATYRYLEPGVYTFRVKASNQDGLWFDNCATLQVKILPPWYK 805
Cdd:COG3292    539 LLLLLLLLLLLLLLLLLLILLLLLLRLLLLL-----LLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLL 613
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  806 TWWAYLIYIAAAGLVTYYYILYKSRQTRLKYEVKVAQLSAEKDKELNERKLSFFTNISHEFRTPLTLIINPVKDMLFgks 885
Cdd:COG3292    614 LLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLL--- 690
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  886 EATDDAGNLHIIYKNARRLLSLVDQLLLFRKAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIY 965
Cdd:COG3292    691 ALLLLLLLLLALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLE 770
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  966 ADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYL 1045
Cdd:COG3292    771 LLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELILLELELGLLL 850
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735101206 1046 VKAFIEHHKGTITYTSKQDQGTTFHVSLLKGKEHFGQQFIFEDVAETSVFLDELMENKGELVTVEAEN 1113
Cdd:COG3292    851 GLLLLLLLEILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIELLLEEE 918
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
845-1073 2.01e-54

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 190.12  E-value: 2.01e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  845 AEKDKELNERKLSFFTNISHEFRTPLTLIINPVkDMLFGKSEATDD--AGNLHIIYKNARRLLSLVDQLLLFRKAESDTD 922
Cdd:COG2205      6 LEELEELERLKSEFLANVSHELRTPLTSILGAA-ELLLDEEDLSPEerRELLEIIRESAERLLRLIEDLLDLSRLESGKL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  923 KLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNG 1002
Cdd:COG2205     85 SLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARREGDG 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735101206 1003 ITINIKDSGCGIAEGTGDELFGKFYQLQNSaPLAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG2205    165 VRISVSDNGPGIPEEELERIFERFYRGDNS-RGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
849-1073 4.73e-54

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 192.43  E-value: 4.73e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  849 KELNERKLSFFTNISHEFRTPLTLIINPVKDMLFGKSEATDDAgnLHIIYKNARRLLSLVDQLLLFRKAESDTDKLKIVR 928
Cdd:COG0642    104 EEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQREY--LETILRSADRLLRLINDLLDLSRLEAGKLELEPEP 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  929 LNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIK 1008
Cdd:COG0642    182 VDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSVRREGDRVRISVE 261
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735101206 1009 DSGCGIAEGTGDELFGKFYQLQNSAPlAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG0642    262 DTGPGIPPEDLERIFEPFFRTDPSRR-GGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
811-1073 2.16e-48

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 177.82  E-value: 2.16e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  811 LIYIAAAGLVTYYYILYKSRQTRLKYEVKVAQLSAEKDKELNERKLSFFTNISHEFRTPLTLIINPVKDMLFGKSEATDD 890
Cdd:COG5002    121 LSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEE 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  891 AGN-LHIIYKNARRLLSLVDQLLLFRKAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIYADRE 969
Cdd:COG5002    201 RREyLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPD 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  970 KMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNS-APLAGGFGIGLYLVKA 1048
Cdd:COG5002    281 RLEQVLTNLLDNAIKYTPEGGTITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSrSRETGGTGLGLAIVKH 360
                          250       260
                   ....*....|....*....|....*
gi 1735101206 1049 FIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG5002    361 IVEAHGGRIWVESEPGKGTTFTITL 385
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1128-1332 7.16e-40

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: 147.02  E-value: 7.16e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1128 TKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVIL 1206
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKsRNNLQKYFYNEITLNKSNDLKISQEykeflekclqivEQ 1286
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR-RRAAEVLRVGDLLDLAAREVTRDGE------------PV 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1287 HLTDPDFSI-KTLAAEIG--MSHSNLYKRIKSISGQSANSFIRFI-RLRK 1332
Cdd:COG0745    146 ELTPKEFRLlELLMRNPGrvVSREQLLEEVWGYDYGDDRTVDVHIsRLRK 195
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1132-1241 1.67e-37

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: 139.27  E-value: 1.67e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTAS 1210
Cdd:COG3706      5 LVVDDDPTNRKLLRRLLEAAgYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLTAL 84
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:COG3706     85 DDEEDRARALEAGADDYLTKPFDPEELLARV 115
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1125-1253 1.46e-36

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: 137.99  E-value: 1.46e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1125 SSDTKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIP 1203
Cdd:COG3437      3 TGQAPTVLIVDDDPENLELLRQLLRTLgYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIP 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1204 VILLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRNNLQK 1253
Cdd:COG3437     83 VIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRE 132
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1130-1232 1.48e-34

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: 128.00  E-value: 1.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLT 1208
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPF 1232
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1125-1248 1.32e-32

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: 123.42  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1125 SSDTKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIP 1203
Cdd:COG0784      2 PLGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIP 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1735101206 1204 VILLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSR 1248
Cdd:COG0784     82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1132-1231 7.49e-32

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 120.02  E-value: 7.49e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTAS 1210
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKP 1231
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
966-1073 7.73e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.45  E-value: 7.73e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206   966 ADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYL 1045
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGTGLGLSI 80
                            90       100
                    ....*....|....*....|....*...
gi 1735101206  1046 VKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITL 108
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1132-1242 2.65e-31

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: 118.79  E-value: 2.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTAS 1210
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTAH 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARVN 1242
Cdd:pfam00072   80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1132-1231 1.06e-30

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: 116.74  E-value: 1.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavLNHIPVILLTAS 1210
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREK--GSDIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKP 1231
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
971-1073 4.97e-29

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: 111.93  E-value: 4.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  971 MEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPlAGGFGIGLYLVKAFI 1050
Cdd:cd00075      1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSRE-GGGTGLGLAIVRRIV 79
                           90       100
                   ....*....|....*....|...
gi 1735101206 1051 EHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd00075     80 EAHGGRITVESEPGGGTTFTVTL 102
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1132-1232 4.24e-28

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: 109.52  E-value: 4.24e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTAS 1210
Cdd:cd19920      2 LIVDDVPDNLRLLSELLRAAgYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTAL 81
                           90       100
                   ....*....|....*....|..
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPF 1232
Cdd:cd19920     82 TDTEDKVKGFELGAVDYITKPF 103
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1128-1253 1.78e-27

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: 116.99  E-value: 1.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1128 TKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVIL 1206
Cdd:COG2204      2 MARILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALD--PDLPVIL 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRNNLQK 1253
Cdd:COG2204     80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRE 126
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1129-1245 3.16e-27

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: 107.34  E-value: 3.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKqiFSGE---FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVI 1205
Cdd:cd17618      1 RTILIVEDEPAIREMIA--FNLEragFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPII 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1206 LLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd17618     79 MLTARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
1127-1246 8.75e-27

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: 110.11  E-value: 8.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1127 DTKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVI 1205
Cdd:TIGR02154    1 MTRRILVVEDEPAIRELIAYNLEKAgYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPII 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1735101206 1206 LLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:TIGR02154   81 MLTARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLR 121
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1132-1246 1.17e-26

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: 105.82  E-value: 1.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTAS 1210
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEgYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd19937     81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVLR 116
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1131-1245 1.44e-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: 102.79  E-value: 1.44e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTA 1209
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1131-1246 7.85e-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: 100.54  E-value: 7.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQI--FSGeFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLT 1208
Cdd:cd17627      1 ILVVDDDRAVRESLRRSlrFEG-YEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAG--NDLPILVLT 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17627     78 ARDSVSDRVAGLDAGADDYLVKPFALEELLARVRALLR 115
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
966-1073 9.05e-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: 100.14  E-value: 9.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  966 ADREKMEIALFNLISNALKFTPDFGLVTCTInDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAplAGGFGIGLYL 1045
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAGEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRG--GGGTGLGLSI 77
                           90       100
                   ....*....|....*....|....*...
gi 1735101206 1046 VKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:pfam02518   78 VRKLVELLGGTITVESEPGGGTTVTLTL 105
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
862-1073 1.08e-24

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 107.58  E-value: 1.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  862 ISHEFRTPLTLIIN---PVKDMLFGKSEATDDAGNLHIIYKNARRLLSLVDQLLLFrkaeSDTDKLKIVRLNIVSLCHEV 938
Cdd:COG4191    149 IAHEINNPLAAILGnaeLLRRRLEDEPDPEELREALERILEGAERAAEIVRSLRAF----SRRDEEEREPVDLNELIDEA 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  939 FLCFNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPD--FGLVTCTINDTGNGITINIKDSGCGIAE 1016
Cdd:COG4191    225 LELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEgeGGRITISTRREGDYVVISVRDNGPGIPP 304
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1735101206 1017 GTGDELFGKFYqlqNSAPLAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG4191    305 EVLERIFEPFF---TTKPVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1132-1231 1.16e-24

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 99.46  E-value: 1.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGEF---EIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLT 1208
Cdd:COG4753      3 LIVDDEPLIREGLKRILEWEAgfeVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELD--PDTKIIILS 80
                           90       100
                   ....*....|....*....|...
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKP 1231
Cdd:COG4753     81 GYSDFEYAQEAIKLGADDYLLKP 103
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
811-1073 6.11e-24

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 107.56  E-value: 6.11e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  811 LIYIAAAGLVTYYYILYKSRQTRLkyEVKVAQLsAEKDKELNErklsfFTNI-SHEFRTPL-------TLIINPVKDMLf 882
Cdd:COG4251    245 LLLLILVLELLELRLELEELEEEL--EERTAEL-ERSNEELEQ-----FAYVaSHDLREPLrkisgfsQLLEEDYGDKL- 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  883 gkSEATDDagNLHIIYKNARRLLSLVDQLLLFRKAESDTDKLKIVRLNivSLCHEVFLCFNHQARTKHIQFDFiseKDTI 962
Cdd:COG4251    316 --DEEGRE--YLERIRDAAERMQALIDDLLAYSRVGRQELEFEPVDLN--ELLEEVLEDLEPRIEERGAEIEV---GPLP 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  963 EIYADREKMEIALFNLISNALKFTPDF--GLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLqNSAPLAGGFG 1040
Cdd:COG4251    387 TVRGDPTLLRQVFQNLISNAIKYSRPGepPRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRL-HSRDEYEGTG 465
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1735101206 1041 IGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG4251    466 IGLAIVKKIVERHGGRIWVESEPGEGATFYFTL 498
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1131-1246 1.62e-23

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: 96.99  E-value: 1.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTA 1209
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEgFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17623     78 RGDDIDRILGLELGADDYLPKPFNPRELVARIRAILR 114
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1132-1241 2.57e-23

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: 96.36  E-value: 2.57e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFS--GEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTA 1209
Cdd:cd17551      4 LIVDDNPTNLLLLEALLRsaGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMITA 83
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:cd17551     84 DTDREVRLRALEAGATDFLTKPFDPVELLARV 115
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
923-1073 3.00e-23

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: 104.27  E-value: 3.00e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  923 KLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNG 1002
Cdd:COG5000    270 EPQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDGR 349
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735101206 1003 ITINIKDSGCGIAEGTGDELF-----GKfyqlqnsaplAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG5000    350 VRIEVSDNGPGIPEEVLERIFepfftTK----------PKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL 415
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1132-1231 6.81e-23

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: 94.43  E-value: 6.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTAS 1210
Cdd:cd19935      2 LVVEDEKKLAEYLKKGLTEEgYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAG--KQTPVLMLTAR 79
                           90       100
                   ....*....|....*....|.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKP 1231
Cdd:cd19935     80 DSVEDRVKGLDLGADDYLVKP 100
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
967-1073 1.03e-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: 94.48  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  967 DREKMEIALFNLISNALKFTPDFGLVTCTINDT-GNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLA-GGFGIGLY 1044
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFrLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAhGGTGLGLS 80
                           90       100
                   ....*....|....*....|....*....
gi 1735101206 1045 LVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16925     81 IVKEFVELHGGTVTVSDAPGGGALFQVEL 109
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1127-1253 1.15e-22

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 95.04  E-value: 1.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1127 DTKTMLLIDDNQQIRTYLKQIFS---GEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIP 1203
Cdd:COG4565      2 KMIRVLIVEDDPMVAELLRRYLErlpGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARG--PDVD 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1204 VILLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRNNLQK 1253
Cdd:COG4565     80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
846-1073 2.76e-22

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: 103.29  E-value: 2.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  846 EKDKELNERKlSFFTNISHEFRTPLTLIinpvkdmlfgKS--EATDD--------AGN-LHIIYKNARRllslvdqllLF 914
Cdd:NF033092   364 EQEKIEQERR-EFVANVSHELRTPLTTM----------RSylEALADgawkdpelAPRfLGVTQNETER---------MI 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  915 R---------KAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQF--DFISEKDTIEIyaDREKMEIALFNLISNAL 983
Cdd:NF033092   424 RlvndllqlsRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFkrEFPKRDLWVEI--DTDKITQVLDNIISNAI 501
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  984 KFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFY--------QLqnsaplaGGFGIGLYLVKAFIEHHKG 1055
Cdd:NF033092   502 KYSPEGGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFYrvdkarsrKM-------GGTGLGLAIAKEVVEAHGG 574
                          250
                   ....*....|....*...
gi 1735101206 1056 TITYTSKQDQGTTFHVSL 1073
Cdd:NF033092   575 RIWAESEEGKGTTIYFTL 592
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
840-1343 3.54e-22

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 104.05  E-value: 3.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  840 VAQLSAEKDKELNER--KLSFFTNISHEFRTPLTLIINPVkDMLFGKSEATDD-AGNLHIIYKNARRLLSLVDQLLLFRK 916
Cdd:PRK09959   695 IHALEVERNKAINATvaKSQFLATMSHEIRTPISSIMGFL-ELLSGSGLSKEQrVEAISLAYATGQSLLGLIGEILDVDK 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  917 AESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISE-KDTIEIYADREKMEIALFNLISNALKFTPDfGLVTCT 995
Cdd:PRK09959   774 IESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPDHYLVKIDPQAFKQVLSNLLSNALKFTTE-GAVKIT 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  996 -----INDTGNGITINIKDSGCGIAEGTGDELFGKFYQlQNSAPLAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFH 1070
Cdd:PRK09959   853 tslghIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ-TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFT 931
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1071 VSLlkgkehfgqqfifedvaetsvfldelmenkgeLVTVEAENTAVAAKNSEALSSDTKTMLLI-DDNQQIRTYLK-QIF 1148
Cdd:PRK09959   932 ITI--------------------------------PVEISQQVATVEAKAEQPITLPEKLSILIaDDHPTNRLLLKrQLN 979
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1149 SGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTASSSPEIKLKGIEGGADDYI 1228
Cdd:PRK09959   980 LLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPIWGLTANAQANEREKGLSCGMNLCL 1057
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1229 SKPFEKEILVARVNGILKSRNNLQKYFYNEITL---NKSNDLKISQEykeflekcLQIVEQHLTDPDFSIKTLAAEIGmS 1305
Cdd:PRK09959  1058 FKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEAlknNTANDLQLMQE--------ILMTFQHETHKDLPAAFHALEAG-D 1128
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1306 HSNLYKRIKSISGqSAN--SFIRFIRLRKAAEILLTTDST 1343
Cdd:PRK09959  1129 NRTFHQCIHRIHG-AANilNLQKLINISHQLEITPVSDDS 1167
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
833-1247 4.11e-22

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: 103.70  E-value: 4.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  833 RLKYEVKVAQLSAEKDKELNERKLSFFTNISHEFRTPLTLIINPVKdMLFGKSEATDDAGNLHIIYKNARRLLSLVDQLL 912
Cdd:TIGR02956  442 RLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDIL 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  913 LFRKAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDF-ISEKDTIEIYADREKMEIALFNLISNALKFTpDFGL 991
Cdd:TIGR02956  521 DYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLnIPEQLPNWWQGDGPRIRQVLINLVGNAIKFT-DRGS 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  992 VTCTIN-DTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPlAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFH 1070
Cdd:TIGR02956  600 VVLRVSlNDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGRRR-SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFW 678
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1071 VSLlkgkehfgqQFIFEDVAETSVFLdelmenkgelvtveaentavaaknsEALSSDTKTMLLIDDNQqirtyLKQIFSG 1150
Cdd:TIGR02956  679 FTL---------PLTRGKPAEDSATL-------------------------TVIDLPPQRVLLVEDNE-----VNQMVAQ 719
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1151 EF------EIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKE-DAVLNHIPVILLTASSSPEIKLKGIEGG 1223
Cdd:TIGR02956  720 GFltrlghKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAiYGAKNEVKFIAFSAHVFNEDVAQYLAAG 799
                          410       420
                   ....*....|....*....|....
gi 1735101206 1224 ADDYISKPFEKEILVARVNGILKS 1247
Cdd:TIGR02956  800 FDGFLAKPVVEEQLTAMIAVILAG 823
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
975-1073 5.76e-22

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: 92.17  E-value: 5.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  975 LFNLISNALKFTPDfGLVTCTIN-----DTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSA-PLAGGFGIGLYLVKA 1048
Cdd:cd16922      5 LLNLLGNAIKFTEE-GEVTLRVSleeeeEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTtRKYGGTGLGLAISKK 83
                           90       100
                   ....*....|....*....|....*
gi 1735101206 1049 FIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16922     84 LVELMGGDISVESEPGQGSTFTFTL 108
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1131-1246 1.37e-21

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: 91.33  E-value: 1.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTA 1209
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEgYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS---NVPIIMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17614     78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVKANLR 114
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1131-1241 2.14e-21

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: 90.61  E-value: 2.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTA 1209
Cdd:cd17626      3 ILVVDDDAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES---GVPIVMLTA 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:cd17626     80 KSDTVDVVLGLESGADDYVAKPFKPKELVARI 111
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1130-1246 2.17e-21

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: 90.87  E-value: 2.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavLNHIPVILLT 1208
Cdd:cd17615      1 RVLVVDDEPNITELLSMALRYEgWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17615     79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLR 116
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1128-1245 5.32e-21

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: 89.92  E-value: 5.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1128 TKTMLLIDDNQQIRTYLK---QIFSGeFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPV 1204
Cdd:cd17552      1 SKRILVIDDEEDIREVVQaclEKLAG-WEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1735101206 1205 ILLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd17552     80 ILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
pleD PRK09581
response regulator PleD; Reviewed
1152-1241 5.52e-21

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 98.05  E-value: 5.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1152 FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTASSSPEIKLKGIEGGADDYISKP 1231
Cdd:PRK09581    27 YTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKP 106
                           90
                   ....*....|
gi 1735101206 1232 FEKEILVARV 1241
Cdd:PRK09581   107 INDVALFARV 116
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1132-1246 6.85e-21

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: 89.20  E-value: 6.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTAS 1210
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEG--IETPVLLLTAL 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17625     79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIRALLR 114
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1131-1242 9.23e-21

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: 89.11  E-value: 9.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGEFEI---FEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavLNHIPVILL 1207
Cdd:cd17535      1 VLIVDDHPLVREGLRRLLESEPDIevvGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRR--YPDLKVIVL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVN 1242
Cdd:cd17535     79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIR 113
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1131-1246 1.01e-20

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 88.93  E-value: 1.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE---FE-IFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavLNHIPVIL 1206
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIDWEelgFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL--YPDIKIII 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17536     79 LSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
PRK15347 PRK15347
two component system sensor kinase;
837-1306 1.24e-20

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 98.95  E-value: 1.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  837 EVKVAQLS-----AEKDKEL-NERKLSFFTNISHEFRTPLTLIINPVkdMLFGKSEAT-------DDAGN-----LHIIy 898
Cdd:PRK15347   374 ENKVAERTqalaeAKQRAEQaNKRKSEHLTTISHEIRTPLNGVLGAL--ELLQNTPLTaeqmdlaDTARQctlslLAII- 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  899 kNArrllslvdqLLLFRKAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFD-FISEKDTIEIYADREKMEIALFN 977
Cdd:PRK15347   451 -NN---------LLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRtFVGAHVPLYLHLDSLRLRQILVN 520
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  978 LISNALKFTPDfGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSaplAGGFGIGLYLVKAFIEHHKGTI 1057
Cdd:PRK15347   521 LLGNAVKFTET-GGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTH---SQGTGLGLTIASSLAKMMGGEL 596
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1058 TYTSKQDQGTTFHVSLlkgkehfgqqfIFEDVAetsvfldELMENKGELVTVEA----------------ENTAVAAK-- 1119
Cdd:PRK15347   597 TLFSTPGVGSCFSLVL-----------PLNEYA-------PPEPLKGELSAPLAlhrqlsawgitcqpghQNPALLDPel 658
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1120 ----------------NSEALSSDTK-------TMLLIDD---NQQI--RTYLKQifsGEfEIFEADNGTDGLELVYHLV 1171
Cdd:PRK15347   659 aylpgrlydllqqiiqGAPNEPVINLplqpwqlQILLVDDvetNRDIigMMLVEL---GQ-QVTTAASGTEALELGRQHR 734
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1172 PDIVISDVMMQGLSGIEvCSRIKEDAVLN---HIPVILLTASSSPEIKLKGIEGGADDYISKPfekeILVARVNGILK-- 1246
Cdd:PRK15347   735 FDLVLMDIRMPGLDGLE-TTQLWRDDPNNldpDCMIVALTANAAPEEIHRCKKAGMNHYLTKP----VTLAQLARALEla 809
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735101206 1247 -----SRN-NLQKYFYNEITLNKSNDLKISQEYKEFLEKCLQIVEQHLTDPDF------SIKTLAAEIGMSH 1306
Cdd:PRK15347   810 aeyqlLRGiELSPQDSSCSPLLDTDDMALNSKLYQSLLLLLAQIEQAVENQEVlsqllhTLKGCAGQAGLTE 881
resp_reg_YycF NF040534
response regulator YycF;
1129-1246 2.28e-20

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 91.71  E-value: 2.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavlNHIPVILL 1207
Cdd:NF040534     1 KKILVVDDEKPIADILEFNLKKEgYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKK---YDMPIIML 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:NF040534    78 TAKDSEIDKVLGLELGADDYVTKPFSTRELIARVKANLR 116
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
861-1073 3.48e-20

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 94.14  E-value: 3.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  861 NISHEFRTPLTLIINPVkDMLFGKSEATDDAGNLHIIYKNARRllslvdqlllfrkAE---------SDTDKLKIVRLNI 931
Cdd:COG3852    141 GLAHEIRNPLTGIRGAA-QLLERELPDDELREYTQLIIEEADR-------------LNnlvdrllsfSRPRPPEREPVNL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  932 VSLCHEVFLCFNHQARtKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVT--------CTINDT--GN 1001
Cdd:COG3852    207 HEVLERVLELLRAEAP-KNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITirtrverqVTLGGLrpRL 285
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735101206 1002 GITINIKDSGCGIAEGTGDELF-----GKfyqlqnsaplAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG3852    286 YVRIEVIDNGPGIPEEILDRIFepfftTK----------EKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYL 352
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
1132-1241 5.31e-20

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 90.31  E-value: 5.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTAS 1210
Cdd:NF040689     2 LVVDDDPALAEMLGIVLRAEgFETVFCADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIRAES---GVPIIMLTAK 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:NF040689    79 SDTVDVVRGLEAGADDYVVKPFKPKELVARI 109
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1129-1245 6.45e-20

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: 86.56  E-value: 6.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavLNHIPVIL 1206
Cdd:cd17542      1 KKVLIVDDAAFMRMMLKDILTKAgYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKI--DPNAKVIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd17542     79 CSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1281-1380 9.28e-20

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 90.61  E-value: 9.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1281 LQIVEQHLTDPDFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFR 1360
Cdd:COG2207    157 LLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFS 236
                           90       100
                   ....*....|....*....|
gi 1735101206 1361 EQFNKLFGINPSDYIKKYRK 1380
Cdd:COG2207    237 RAFKKRFGVTPSEYRKRLRA 256
orf27 CHL00148
Ycf27; Reviewed
1131-1250 1.02e-19

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 89.78  E-value: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFS-GEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTA 1209
Cdd:CHL00148     9 ILVVDDEAYIRKILETRLSiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES---DVPIIMLTA 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRNN 1250
Cdd:CHL00148    86 LGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNK 126
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
919-1073 1.34e-19

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: 94.03  E-value: 1.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  919 SDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTIND 998
Cdd:COG5805    344 AKPQAVNKEKENINELIQDVVTLLETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEE 423
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735101206  999 TGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSaplagGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG5805    424 EDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKEK-----GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITL 493
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1130-1242 1.62e-19

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


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 85.28  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLT 1208
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPFEKEILVARVN 1242
Cdd:cd17548     81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
862-1073 2.28e-19

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: 93.12  E-value: 2.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  862 ISHEFRTPLTLIINPVKdmLFGKSEATDDAGNLHIIYKNARRLLSLVDQLLLFRKAESdtdkLKIVRLNIVSLCHEVFLC 941
Cdd:COG5809    277 IAHEIRNPLTSLKGFIQ--LLKDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQA----IKYEPKDLNTLIEEVIPL 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  942 FNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDT-GNGITINIKDSGCGIAEGTGD 1020
Cdd:COG5809    351 LQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIETKAEdDDKVVISVTDEGCGIPEERLK 430
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1735101206 1021 ELFGKFYQLQNsaplaGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG5809    431 KLGEPFYTTKE-----KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1131-1231 4.26e-19

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: 83.58  E-value: 4.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQ-IFSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTA 1209
Cdd:cd19927      1 ILLVDDDPGIRLAVKDyLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                           90       100
                   ....*....|....*....|..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKP 1231
Cdd:cd19927     81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1131-1246 1.03e-18

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: 83.19  E-value: 1.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQI----RTYLKQifsGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVIL 1206
Cdd:cd19939      2 ILIVEDELELarltRDYLIK---AGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS---HVPILM 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd19939     76 LTARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLR 115
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1132-1239 1.08e-18

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: 82.90  E-value: 1.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFS--GeFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKED-AVLNHIPVILLT 1208
Cdd:cd17546      2 LVVDDNPVNRKVLKKLLEklG-YEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeGGGRRTPIIALT 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPFEKEILVA 1239
Cdd:cd17546     81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKE 111
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1292-1374 1.10e-18

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 81.83  E-value: 1.10e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  1292 DFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKLFGINP 1371
Cdd:smart00342    1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                    ...
gi 1735101206  1372 SDY 1374
Cdd:smart00342   81 SEY 83
PRK09303 PRK09303
histidine kinase;
922-1073 1.16e-18

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 89.63  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  922 DKLKI--VRLNIVSLCHEVFLCFNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTI-ND 998
Cdd:PRK09303   222 EALRFnpQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGGTITLSMlHR 301
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735101206  999 TGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPlAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:PRK09303   302 TTQKVQVSICDTGPGIPEEEQERIFEDRVRLPRDEG-TEGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTL 375
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1132-1246 2.14e-18

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 82.15  E-value: 2.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTAS 1210
Cdd:cd17624      2 LLVEDDALLGDGLKTGLRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQG--QSLPVLILTAR 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17624     80 DGVDDRVAGLDAGADDYLVKPFALEELLARLRALLR 115
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
945-1078 2.40e-18

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 89.14  E-value: 2.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  945 QARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNAL----KFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGD 1020
Cdd:COG3290    256 RARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIeaveKLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLE 335
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1735101206 1021 ELFGKFYqlqnSAPLAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSLLKGKE 1078
Cdd:COG3290    336 KIFERGF----STKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
cztR_silR_copR TIGR01387
heavy metal response regulator; Members of this family contain a response regulator receiver ...
1131-1246 2.78e-18

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: 85.24  E-value: 2.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTA 1209
Cdd:TIGR01387    1 ILVVEDEQKTAEYLQQGLSESgYVVDAASNGRDGLHLALKDDYDLIILDVMLPGMDGWQILQTLRRSG--KQTPVLFLTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:TIGR01387   79 RDSVADKVKGLDLGADDYLVKPFSFSELLARVRTLLR 115
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1131-1246 5.54e-18

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 81.17  E-value: 5.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLK-QIFSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVILLTA 1209
Cdd:cd19934      1 LLLVEDDALLAAQLKeQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLILTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd19934     79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALIR 115
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
858-1069 7.10e-18

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: 86.49  E-value: 7.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  858 FFTNISHEFRTPLTlIINPVKDMLFGKSEATDDAGN--LHIIYKNARRLLSLVDQLLLFRKAESDTDKLKIVRLNIVSLC 935
Cdd:TIGR02966  117 FVANVSHELRTPLT-VLRGYLETLADGPDEDPEEWNraLEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALL 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  936 HEVFLCFNHQARTKHIQFDFISEKDtIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIA 1015
Cdd:TIGR02966  196 DHLRDEAEALSQGKNHQITFEIDGG-VDVLGDEDELRSAFSNLVSNAIKYTPEGGTITVRWRRDGGGAEFSVTDTGIGIA 274
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1735101206 1016 EGTGDELFGKFYQLQNSAP-LAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTF 1069
Cdd:TIGR02966  275 PEHLPRLTERFYRVDKSRSrDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1132-1239 7.89e-18

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: 80.58  E-value: 7.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTAS 1210
Cdd:cd17580      2 LVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTGY 81
                           90       100
                   ....*....|....*....|....*....
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVA 1239
Cdd:cd17580     82 GQPEDRERALEAGFDAHLVKPVDPDELIE 110
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1131-1246 8.60e-18

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: 80.50  E-value: 8.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIF-SGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLnhiPVILLTA 1209
Cdd:cd17622      3 ILLVEDDPKLARLIADFLeSHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG---PILLLTA 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17622     80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRALLR 116
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1131-1249 1.08e-17

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 83.70  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVpDIVISDVMMQGLSGIEVcsrIKEDAVLNHIPVILLTA 1209
Cdd:PRK10955     4 ILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQALDLLDDSI-DLLLLDVMMPKKNGIDT---LKELRQTHQTPVIMLTA 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRN 1249
Cdd:PRK10955    80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSH 119
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1132-1231 1.18e-17

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 79.52  E-value: 1.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavLNHIPVILLTAS 1210
Cdd:cd17620      2 LVIEDEPQIRRFLRTALEAHgYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLRE---WSAVPVIVLSAR 78
                           90       100
                   ....*....|....*....|.
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKP 1231
Cdd:cd17620     79 DEESDKIAALDAGADDYLTKP 99
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1127-1245 1.81e-17

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: 79.69  E-value: 1.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1127 DTKTMLLIddnqqIRTYLKQIfsGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVIL 1206
Cdd:cd19923      8 DFSTMRRI-----IKNLLKEL--GFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd19923     81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1130-1245 2.85e-17

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: 78.96  E-value: 2.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQI----RTYLKQifsGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavLNHIPVI 1205
Cdd:cd19938      1 RILIVEDEPKLaqllIDYLRA---AGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRR---FSDVPII 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1206 LLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd19938     75 MVTARVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1132-1239 2.13e-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: 78.85  E-value: 2.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIF--SGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavlNHIPVILLTA 1209
Cdd:COG3707      7 LVVDDEPLRRADLREGLreAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEE---RPAPVILLTA 83
                           90       100       110
                   ....*....|....*....|....*....|
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVA 1239
Cdd:COG3707     84 YSDPELIERALEAGVSAYLVKPLDPEDLLP 113
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
1131-1241 2.37e-16

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: 80.61  E-value: 2.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGEFEIF---EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILL 1207
Cdd:TIGR02875    5 IVIADDNKEFCNLLKEYLAAQPDMEvvgVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARPRVIML 84
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:TIGR02875   85 SAFGQEKITQRAVALGADYYVLKPFDLEILAARI 118
HTH_18 pfam12833
Helix-turn-helix domain;
1298-1377 2.39e-16

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 75.32  E-value: 2.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1298 LAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILL-TTDSTVYETAYKVGLNDLKYFREQFNKLFGINPSDYIK 1376
Cdd:pfam12833    1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80

                   .
gi 1735101206 1377 K 1377
Cdd:pfam12833   81 R 81
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1132-1231 2.64e-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: 2.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDN----QQIRTYLKQIfsgEFEIFEADNGTDGLELVYHLVP---------DIVISDVMMQGLSGIEVCSRIKEDAV 1198
Cdd:cd19924      2 LVVDDSptarKQLRDLLKNL---GFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDDPR 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1735101206 1199 LNHIPVILLTASSSPEIKLKGIEGGADDYISKP 1231
Cdd:cd19924     79 LANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1129-1246 4.88e-16

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 78.99  E-value: 4.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILL 1207
Cdd:PRK10161     3 RRILVVEDEAPIREMVCFVLEQNgFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVML 82
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:PRK10161    83 TARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
ompR PRK09468
osmolarity response regulator; Provisional
1132-1248 5.19e-16

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 79.25  E-value: 5.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTAS 1210
Cdd:PRK09468     9 LVVDDDMRLRALLERYLTEQgFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQN--NPTPIIMLTAK 86
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSR 1248
Cdd:PRK09468    87 GEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQ 124
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1132-1245 6.18e-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: 75.01  E-value: 6.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSG-EFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavLNHIPVILLTAS 1210
Cdd:cd18159      2 LIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFISSR 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1211 SSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd18159     79 DDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1129-1245 6.43e-16

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 75.03  E-value: 6.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILL 1207
Cdd:cd17562      1 KKILAVDDSASIRQMVSFTLRGAgYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd17562     81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1129-1237 9.30e-16

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: 74.75  E-value: 9.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIFE-ADNGTDGLELVYHLVPDIVISDVMMQG-LSGIEVCSRIKEdavLNHIPVI 1205
Cdd:cd17534      1 KKILIVEDEAIIALDLKEILESLgYEVVGiADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIRE---KFDIPVI 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1206 LLTASSSPEIKLKGIEGGADDYISKPFEKEIL 1237
Cdd:cd17534     78 FLTAYSDEETLERAKETNPYGYLVKPFNEREL 109
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1130-1246 1.11e-15

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 77.69  E-value: 1.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLkqIFSGEFEIFEADN---GTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKedAVLNHIPVIL 1206
Cdd:PRK11083     5 TILLVEDEQAIADTL--VYALQSEGFTVEWferGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLL--AFHPALPVIF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1735101206 1207 LTASSSpEI-KLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:PRK11083    81 LTARSD-EVdRLVGLEIGADDYVAKPFSPREVAARVRTILR 120
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
1132-1241 1.92e-15

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: 74.06  E-value: 1.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKE-DAvlnHIPVILLTA 1209
Cdd:cd17549      2 LLVDDDADVREALQQTLELAgFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRElDP---DLPVILITG 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:cd17549     79 HGDVPMAVEAMRAGAYDFLEKPFDPERLLDVV 110
PRK11517 PRK11517
DNA-binding response regulator HprR;
1131-1277 3.15e-15

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 76.48  E-value: 3.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFS-GEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKedaVLNHIPVILLTA 1209
Cdd:PRK11517     3 ILLIEDNQRTQEWVTQGLSeAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR---TAKQTPVICLTA 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRNNLQKYF-YNEITLNKS------NDLKISQEYKEFL 1277
Cdd:PRK11517    80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHHALNSTLeISGLRMDSVsqsvsrDNISITLTRKEFQ 154
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
854-1073 3.18e-15

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 80.20  E-value: 3.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  854 RKLSFFTNISHEFRTPLTLIINPVKDMLfgkSEATDDAGNLHIIYKNAR---RLLSLVDQLLLFRKAESDTDKLKIVRLN 930
Cdd:PRK09835   261 RQSNFSADIAHEIRTPITNLITQTEIAL---SQSRSQKELEDVLYSNLEeltRMAKMVSDMLFLAQADNNQLIPEKKMLD 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  931 IVSLCHEVFLCFNHQARTKHIQFDFisEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDS 1010
Cdd:PRK09835   338 LADEVGKVFDFFEAWAEERGVELRF--VGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEAITVRCQEVDHQVQLVVENP 415
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735101206 1011 GCGIAEGTGDELFGKFYQLQNSAPLAG-GFGIGLYLVKAFIEHHKGTITYTSKQDqGTTFHVSL 1073
Cdd:PRK09835   416 GTPIAPEHLPRLFDRFYRVDPSRQRKGeGSGIGLAIVKSIVVAHKGTVAVTSDAR-GTRFVISL 478
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
977-1074 4.27e-15

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: 72.42  E-value: 4.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  977 NLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPlAGGFGIGLYLVKAFIEHHKGT 1056
Cdd:cd16923      7 NLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRN-TEGAGLGLSIAKAIIELHGGS 85
                           90
                   ....*....|....*...
gi 1735101206 1057 ITYTSkQDQGTTFHVSLL 1074
Cdd:cd16923     86 ASAEY-DDNHDLFKVRLP 102
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
1131-1246 4.57e-15

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: 72.53  E-value: 4.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVILLTA 1209
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYP--DLPVIMISG 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd17550     79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1129-1242 4.76e-15

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: 72.82  E-value: 4.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKE---DAVLnhipv 1204
Cdd:cd17569      1 PTILLVDDEPNILKALKRLLRREgYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRErypDTVR----- 75
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1205 ILLTASSSPEIKLKGI-EGGADDYISKPFEKEILVARVN 1242
Cdd:cd17569     76 ILLTGYADLDAAIEAInEGEIYRFLTKPWDDEELKETIR 114
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
1131-1231 4.82e-15

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: 72.23  E-value: 4.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTA 1209
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEgFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS---NVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKP 1231
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1159-1352 5.05e-15

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 76.26  E-value: 5.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1159 NGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTASSSpEI-KLKGIEGGADDYISKPFEKEIL 1237
Cdd:PRK10710    42 HGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS---DIPIVMVTAKIE-EIdRLLGLEIGADDYICKPYSPREV 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1238 VARVNGILKsRNNLQKyfyNEITLNKSNDLKISQEY--KEFLEKCLQiveqhLTDPDFS-IKTLAAEIGMSHS------N 1308
Cdd:PRK10710   118 VARVKTILR-RCKPQR---ELQQQDAESPLIIDESRfqASWRGKMLD-----LTPAEFRlLKTLSHEPGKVFSreqllnH 188
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1735101206 1309 LYKRIKSISGQSANSFIRfiRLRKAAEiLLTTDSTVYETAYKVG 1352
Cdd:PRK10710   189 LYDDYRVVTDRTIDSHIK--NLRRKLE-SLDAEQSFIRAVYGVG 229
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1129-1233 6.13e-15

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: 72.31  E-value: 6.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE---FEIFeaDNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVI 1205
Cdd:cd19919      1 KTVWIVDDDSSIRWVLERALAGAgltVTSF--ENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRH--PDLPVI 76
                           90       100
                   ....*....|....*....|....*...
gi 1735101206 1206 LLTASSSPEIKLKGIEGGADDYISKPFE 1233
Cdd:cd19919     77 IMTAHSDLDSAVSAYQGGAFEYLPKPFD 104
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1132-1249 6.34e-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: 72.62  E-value: 6.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIR----TYLKQifsGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVILL 1207
Cdd:cd17572      2 LLVEDSPSLAalyqEYLSD---EGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSL--PTSVIVI 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRN 1249
Cdd:cd17572     77 TAHGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRK 118
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
974-1073 6.42e-15

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: 71.97  E-value: 6.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  974 ALFNLISNALKFT--PDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLqNSAPLAGGFGIGLYLVKAFIE 1051
Cdd:cd16921      4 VLTNLLGNAIKFRrpRRPPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRL-HSREEYEGTGVGLAIVRKIIE 82
                           90       100
                   ....*....|....*....|..
gi 1735101206 1052 HHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16921     83 RHGGRIWLESEPGEGTTFYFTL 104
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1132-1274 6.57e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 75.62  E-value: 6.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFS--GEFEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLT 1208
Cdd:COG3279      5 LIVDDEPLARERLERLLEkyPDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD--PPPPIIFTT 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735101206 1209 AssSPEIKLKGIEGGADDYISKPFEKEILVARVNgilKSRNNLQKYFYNEITLNKSNDLKISQEYK 1274
Cdd:COG3279     83 A--YDEYALEAFEVNAVDYLLKPIDEERLAKALE---KAKERLEAKAAAEASPEEKDRIFVKSGGK 143
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1131-1245 7.07e-15

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: 72.06  E-value: 7.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDN----QQIRTYLKqifSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVIL 1206
Cdd:cd17616      1 VLLIEDDsataQSIELMLK---SEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKV--KTPILI 75
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:cd17616     76 LSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1132-1242 7.96e-15

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 72.17  E-value: 7.96e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLE-LVYHlvPDI--VISDVMMQGLSGIEVCSRIKEDAVLNHIPVILL 1207
Cdd:cd17544      4 LVVDDSATSRNHLRALLRRHnFQVLEAANGQEALEvLEQH--PDIklVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVN 1242
Cdd:cd17544     82 SASGDNALSARFIKAGANDFLTKPFLPEEFYCRVT 116
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1126-1239 8.35e-15

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 75.07  E-value: 8.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1126 SDTKTMLLIDDNQQIRTYLKQIFSGEFE---IFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHI 1202
Cdd:PRK10651     4 QEPATILLIDDHPMLRTGVKQLISMAPDitvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRI 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1203 pvILLTASSSPEIKLKGIEGGADDYISKPFEKEILVA 1239
Cdd:PRK10651    84 --VVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLK 118
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1131-1237 1.54e-14

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: 71.22  E-value: 1.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE--FEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIpvILL 1207
Cdd:cd19931      1 VLLIDDHPLLRKGIKQLIELDpdFTVVgEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARI--VIL 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEIL 1237
Cdd:cd19931     79 TVSDAEDDVVTALRAGADGYLLKDMEPEDL 108
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
1277-1381 1.95e-14

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: 75.96  E-value: 1.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1277 LEKCLQIVEQHLTDPdFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDL 1356
Cdd:COG4977    212 LARAQAWMEANLEEP-LSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSA 290
                           90       100
                   ....*....|....*....|....*
gi 1735101206 1357 KYFREQFNKLFGINPSDYIKKYRKP 1381
Cdd:COG4977    291 SHFRRAFRRRFGVSPSAYRRRFRAR 315
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
837-1073 1.96e-14

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 78.44  E-value: 1.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  837 EVKVAQLSAEKdkelNER-KLSFFTNISHEFRTPLTLIINpVKDMLFgKSEATDDAGN-LHIIYKNA------------- 901
Cdd:PRK11091   268 ERKRYQDALEK----ASRdKTTFISTISHELRTPLNGIVG-LSRILL-DTELTAEQRKyLKTIHVSAitlgnifndiidm 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  902 ----RRllslvdqlllfrKAESDTDKLKIVRL-----NIVSLchevflcfnhQARTKHIQFDF-ISEKDTIEIYADREKM 971
Cdd:PRK11091   342 dkmeRR------------KLQLDNQPIDFTDFladleNLSGL----------QAEQKGLRFDLePLLPLPHKVITDGTRL 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  972 EIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSA--PLAGGFGIGLYLVKAF 1049
Cdd:PRK11091   400 RQILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHggKPATGTGIGLAVSKRL 479
                          250       260
                   ....*....|....*....|....
gi 1735101206 1050 IEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:PRK11091   480 AQAMGGDITVTSEEGKGSCFTLTI 503
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1129-1233 2.69e-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: 70.69  E-value: 2.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIR----TYLKQifSGeFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLnhIPV 1204
Cdd:cd17555      1 ATILVIDDDEVVResiaAYLED--SG-FQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPD--TPV 75
                           90       100
                   ....*....|....*....|....*....
gi 1735101206 1205 ILLTASSSPEIKLKGIEGGADDYISKPFE 1233
Cdd:cd17555     76 IVVSGAGVMSDAVEALRLGAWDYLTKPIE 104
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
833-1073 5.00e-14

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 76.93  E-value: 5.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  833 RLKYEVKVAQlsAEKDKELNErklsFFTNISHEFRTPLTLIINPVKdmlFGKSEATDDAGN--LHIIYKNARRLLSLVDQ 910
Cdd:PRK11360   374 RKRLQRRVAR--QERLAALGE----LVAGVAHEIRNPLTAIRGYVQ---IWRQQTSDPPSQeyLSVVLREVDRLNKVIDQ 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  911 LLLF-RKAESDTDKlkiVRLNIvsLCHEVFLCFNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDF 989
Cdd:PRK11360   445 LLEFsRPRESQWQP---VSLNA--LVEEVLQLFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISAR 519
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  990 GLVTCTINDTGNG-ITINIKDSGCGIAEGTGDELFGKFYQLQnsaplAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTT 1068
Cdd:PRK11360   520 GKIRIRTWQYSDGqVAVSIEDNGCGIDPELLKKIFDPFFTTK-----AKGTGLGLALSQRIINAHGGDIEVESEPGVGTT 594

                   ....*
gi 1735101206 1069 FHVSL 1073
Cdd:PRK11360   595 FTLYL 599
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1129-1242 1.22e-13

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 68.40  E-value: 1.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdaVLNHIPVILL 1207
Cdd:cd17554      1 KKILVVDDEENIRELYKEELEDEgYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIIC 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1208 TASSSPEIKLKGIegGADDYISKPFEKEILVARVN 1242
Cdd:cd17554     79 TAYSEYKSDFSSW--AADAYVVKSSDLTELKETIK 111
PRK15479 PRK15479
transcriptional regulator TctD;
1131-1246 1.54e-13

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 71.29  E-value: 1.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGEFeiFEADNGTDGLeLVYHLVPD----IVISDVMMQGLSGIEVCSRIKEDAvlNHIPVIL 1206
Cdd:PRK15479     3 LLLAEDNRELAHWLEKALVQNG--FAVDCVFDGL-AADHLLQSemyaLAVLDINMPGMDGLEVLQRLRKRG--QTLPVLL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:PRK15479    78 LTARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLR 117
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
946-1073 1.80e-13

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 74.44  E-value: 1.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  946 ARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGK 1025
Cdd:PRK10364   324 ANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTP 403
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1735101206 1026 FYQLQNSaplagGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:PRK10364   404 YFTTKAE-----GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWL 446
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
977-1073 2.66e-13

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: 67.31  E-value: 2.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  977 NLISNALKFTPDFGL----VTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYqlqnSAPLAGGFGIGLYLVKAFIEH 1052
Cdd:cd16915      7 NLIDNALDALAATGApnkqVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGV----STKGQGERGIGLALVRQSVER 82
                           90       100
                   ....*....|....*....|.
gi 1735101206 1053 HKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16915     83 LGGSITVESEPGGGTTFSIRI 103
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1130-1241 4.40e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 70.22  E-value: 4.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVcsrIKEDAVLNHIPVILLT 1208
Cdd:PRK10529     3 NVLIVEDEQAIRRFLRTALEGDgMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEF---IRDLRQWSAIPVIVLS 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:PRK10529    80 ARSEESDKIAALDAGADDYLSKPFGIGELQARL 112
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1132-1233 5.59e-13

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: 67.06  E-value: 5.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDN----QQIRTYLKQIfSGEFEIFEADNGTDGLELVYH-------LVPDIVISDVMMQGLSGIEVCSRIKEDAVLN 1200
Cdd:cd17557      3 LLVEDNpgdaELIQEAFKEA-GVPNELHVVRDGEEALDFLRGegeyadaPRPDLILLDLNMPRMDGFEVLREIKADPDLR 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1735101206 1201 HIPVILLTASSSPEIKLKGIEGGADDYISKPFE 1233
Cdd:cd17557     82 RIPVVVLTTSDAEEDIERAYELGANSYIVKPVD 114
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
858-1073 7.77e-13

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 72.35  E-value: 7.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  858 FFTNISHEFRTPLTLiinpvkdmLFGKSEATDD--------AGNLHIIYKNARRLLSLVDQLLLFRKAESDTD------- 922
Cdd:PRK11006   207 FFANVSHELRTPLTV--------LQGYLEMMQDqplegalrEKALHTMREQTQRMEGLVKQLLTLSKIEAAPTidlnekv 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  923 ----KLKIVRLNIVSLCHEvflcfNHqartkHIQFDfISEKdtIEIYADREKMEIALFNLISNALKFTPDFGLVTCTIND 998
Cdd:PRK11006   279 dvpmMLRVLEREAQTLSQG-----KH-----TITFE-VDNS--LKVFGNEDQLRSAISNLVYNAVNHTPEGTHITVRWQR 345
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735101206  999 TGNGITINIKDSGCGIAEGTGDELFGKFYQLQNS-APLAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:PRK11006   346 VPQGAEFSVEDNGPGIAPEHIPRLTERFYRVDKArSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVL 421
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1130-1242 1.04e-12

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 65.93  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGEFEIFEAdnGTDGLELV---YHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVIL 1206
Cdd:cd17594      1 HVLVVDDDAAMRHLLILYLRERGFDVTA--AADGAEEArlmLHRRVDLVLLDLRLGQESGLDLLRTIRARS---DVPIII 75
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1207 LTASSSPEI-KLKGIEGGADDYISKPFEKEILVARVN 1242
Cdd:cd17594     76 ISGDRRDEIdRVVGLELGADDYLAKPFGLRELLARVR 112
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
916-1058 1.46e-12

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 71.80  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  916 KAESDTDKLKIVRLNIVSLCHEVFLCFNHQARTKHIQFDFisEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCT 995
Cdd:PRK11100   316 RLEQRQELEVLEPVALAALLEELVEAREAQAAAKGITLRL--RPDDARVLGDPFLLRQALGNLLDNAIDFSPEGGTITLS 393
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735101206  996 INDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYLVKAFIEHHKGTIT 1058
Cdd:PRK11100   394 AEVDGEQVALSVEDQGPGIPDYALPRIFERFYSLPRPANGRKSTGLGLAFVREVARLHGGEVT 456
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1133-1231 1.50e-12

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: 65.16  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1133 LIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavlNHIPVILLTASS 1211
Cdd:cd19936      3 LVDDDRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFLTSKD 79
                           90       100
                   ....*....|....*....|
gi 1735101206 1212 SPEIKLKGIEGGADDYISKP 1231
Cdd:cd19936     80 DEIDEVFGLRMGADDYITKP 99
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
1132-1232 1.75e-12

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: 64.94  E-value: 1.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSG--EFEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLT 1208
Cdd:cd17561      5 LIADDNREFVQLLEEYLNSqpDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIMLT 84
                           90       100
                   ....*....|....*....|....
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPF 1232
Cdd:cd17561     85 AFGQEDITQRAVELGASYYILKPF 108
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1129-1239 2.69e-12

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: 64.74  E-value: 2.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavlNHIPVIL 1206
Cdd:cd19932      1 VRVLIAEDEALIRMDLREMLEEAgYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE---NIAPIVL 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVA 1239
Cdd:cd19932     78 LTAYSQQDLVERAKEAGAMAYLVKPFSESDLIP 110
Y_Y_Y pfam07495
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ...
736-800 3.13e-12

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: 62.75  E-value: 3.13e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735101206  736 NYTYPDKGGFAYKLDGLDKTWNYVGDQRLATYRYLEPGVYTFRVKASNQDGLWFDNCATLQVKIL 800
Cdd:pfam07495    1 NYDGPENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSYDDASLNFTIL 65
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1131-1249 4.03e-12

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 67.26  E-value: 4.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYL-KQIFSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTA 1209
Cdd:PRK09836     3 LLIVEDEKKTGEYLtKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSAN--KGMPILLLTA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRN 1249
Cdd:PRK09836    81 LGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGA 120
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1132-1231 4.58e-12

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: 64.34  E-value: 4.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFS--GEFE-IFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavLNHIPVILLT 1208
Cdd:cd17541      4 LIVDDSAVMRKLLSRILEsdPDIEvVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMA---ERPTPVVMVS 80
                           90       100
                   ....*....|....*....|....*
gi 1735101206 1209 ASSSP--EIKLKGIEGGADDYISKP 1231
Cdd:cd17541     81 SLTEEgaEITLEALELGAVDFIAKP 105
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1132-1202 5.41e-12

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: 64.53  E-value: 5.41e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGEFEI---FEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRI---KEDAVLNHI 1202
Cdd:COG2197      5 LIVDDHPLVREGLRALLEAEPDIevvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLltpREREVLRLL 81
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1131-1241 6.04e-12

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 63.56  E-value: 6.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVILLTA 1209
Cdd:cd17619      3 ILIVEDEPVTRATLKSYFEQEgYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS---EVGIILVTG 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:cd17619     80 RDDEVDRIVGLEIGADDYVTKPFNPRELLVRA 111
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
1129-1242 6.52e-12

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: 63.73  E-value: 6.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdaVLNHIPVILL 1207
Cdd:cd17553      1 EKILIVDDQYGIRILLNEVFNKEgYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKV--IDENIRVIIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVN 1242
Cdd:cd17553     79 TAYGELDMIQESKELGALTHFAKPFDIDEIRDAVK 113
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1130-1240 8.27e-12

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 69.11  E-value: 8.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLT 1208
Cdd:PRK11361     6 RILIVDDEDNVRRMLSTAFALQgFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHE--TRTPVILMT 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPF---EKEILVAR 1240
Cdd:PRK11361    84 AYAEVETAVEALRCGAFDYVIKPFdldELNLIVQR 118
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1125-1239 9.21e-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: 64.94  E-value: 9.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1125 SSDTKTMLLIDDNQQIRTYLKQIFS--GeFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdaVLNHI 1202
Cdd:COG4567      1 SAEDRSLLLVDDDEAFARVLARALErrG-FEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE--RDPDA 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1735101206 1203 PVILLTASSSPEIKLKGIEGGADDYISKPFE-KEILVA 1239
Cdd:COG4567     78 RIVVLTGYASIATAVEAIKLGADDYLAKPADaDDLLAA 115
PRK10610 PRK10610
chemotaxis protein CheY;
1132-1246 1.56e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 63.07  E-value: 1.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFS--GEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTA 1209
Cdd:PRK10610     9 LVVDDFSTMRRIVRNLLKelGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTA 88
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:PRK10610    89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1133-1241 1.70e-11

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: 64.74  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1133 LIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVILLTASS 1211
Cdd:COG4566      4 IVDDDEAVRDSLAFLLESAgLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGS--PLPVIFLTGHG 81
                           90       100       110
                   ....*....|....*....|....*....|
gi 1735101206 1212 SPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:COG4566     82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAV 111
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
974-1069 1.87e-11

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: 62.09  E-value: 1.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  974 ALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYLVKAFIEHH 1053
Cdd:cd16945      8 AINNLLDNAIDFSPEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQKSTGLGLAFVQEVAQLH 87
                           90
                   ....*....|....*.
gi 1735101206 1054 KGTITYTSKQDQGTTF 1069
Cdd:cd16945     88 GGRITLRNRPDGVLAF 103
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1132-1248 2.31e-11

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 62.17  E-value: 2.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDN---QQIRTYLKQIFSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavLNHIP-VILL 1207
Cdd:cd17532      2 LIVDDEplaREELRYLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSK---LAKPPlIVFV 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1735101206 1208 TASSspEIKLKGIEGGADDYISKPFEKEILVARVNGILKSR 1248
Cdd:cd17532     79 TAYD--EYAVEAFELNAVDYLLKPFSEERLAEALAKLRKRL 117
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
964-1073 3.09e-11

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: 62.15  E-value: 3.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  964 IYA--DREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLA-GGFG 1040
Cdd:cd16947     12 IYAnaNTEALQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAkQGNG 91
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1735101206 1041 IGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16947     92 LGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
974-1073 5.36e-11

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: 60.80  E-value: 5.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  974 ALFNLISNALKFTPDFglVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLA-GGFGIGLYLVKAFIEH 1052
Cdd:cd16949      4 ALENVLRNALRYSPSK--ILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDREsGGTGLGLAIAERAIEQ 81
                           90       100
                   ....*....|....*....|.
gi 1735101206 1053 HKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16949     82 HGGKIKASNRKPGGLRVRIWL 102
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1073 5.85e-11

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: 60.49  E-value: 5.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  975 LFNLISNALKFTPDFG------LVTCTINDTGnGITINIKDSGCGIAEGTGDELFGKFYQLQNSaplagGFGIGLYLVKA 1048
Cdd:cd16920      5 LINLVRNGIEAMSEGGcerrelTIRTSPADDR-AVTISVKDTGPGIAEEVAGQLFDPFYTTKSE-----GLGMGLSICRS 78
                           90       100
                   ....*....|....*....|....*
gi 1735101206 1049 FIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16920     79 IIEAHGGRLSVESPAGGGATFQFTL 103
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1124-1233 6.27e-11

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 66.21  E-value: 6.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1124 LSSDTKTMLLIDDNQQIRTYLKQIFSG-EFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKedAVLNHI 1202
Cdd:PRK10365     1 MTHDNIDILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK--ALNPAI 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1735101206 1203 PVILLTASSSPEIKLKGIEGGADDYISKPFE 1233
Cdd:PRK10365    79 PVLIMTAYSSVETAVEALKTGALDYLIKPLD 109
PRK11173 PRK11173
two-component response regulator; Provisional
1128-1292 6.98e-11

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 63.88  E-value: 6.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1128 TKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVIL 1206
Cdd:PRK11173     3 TPHILIVEDELVTRNTLKSIFEAEgYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQA---NVALMF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARvngilkSRNNLQKyfynEITLNKSNDLKISQEYKEFLEKCLQIVEQ 1286
Cdd:PRK11173    80 LTGRDNEVDKILGLEIGADDYITKPFNPRELTIR------ARNLLSR----TMNLGTVSEERRSVESYKFNGWELDINSR 149

                   ....*.
gi 1735101206 1287 HLTDPD 1292
Cdd:PRK11173   150 SLISPD 155
PRK10766 PRK10766
two-component system response regulator TorR;
1128-1245 7.11e-11

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 63.52  E-value: 7.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1128 TKTMLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlnHIPVIL 1206
Cdd:PRK10766     2 SYHILVVEDEPVTRARLQGYFEQEgYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS---TVGIIL 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGIL 1245
Cdd:PRK10766    79 VTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
372-630 1.71e-10

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 63.50  E-value: 1.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  372 YGMCQDRDGFLWlgtdgeglFKTSRNGTLIKQYKADGRAGSITDNAILYGYT---DSNGNVWF-GTYAKGLLLYNKKTDS 447
Cdd:COG4257     20 RDVAVDPDGAVW--------FTDQGGGRIGRLDPATGEFTEYPLGGGSGPHGiavDPDGNLWFtDNGNNRIGRIDPKTGE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  448 FTSYAHNASDSkslGGNDVRViyqDSRKNIWI-GTNGGGLSLFDPVSKTFSNFTPANSGLTAYdvrAITEDEQGNLWIGT 526
Cdd:COG4257     92 ITTFALPGGGS---NPHGIAF---DPDGNLWFtDQGGNRIGRLDPATGEVTEFPLPTGGAGPY---GIAVDPDGNLWVTD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  527 YGGG-LDFYDIRQKKFSRYFTPIdernnlPGQVIFSLYVDKYRRLWIA-TEGDGLIAYDLKKRVFKKFNETNGLANNTVS 604
Cdd:COG4257    163 FGANaIGRIDPDTGTLTEYALPT------PGAGPRGLAVDPDGNLWVAdTGSGRIGRFDPKTGTVTEYPLPGGGARPYGV 236
                          250       260
                   ....*....|....*....|....*....
gi 1735101206  605 AFkeVADGTLW---MSTNKgLSNLNPATG 630
Cdd:COG4257    237 AV--DGDGRVWfaeSGANR-IVRFDPDTE 262
PRK10816 PRK10816
two-component system response regulator PhoP;
1131-1250 2.20e-10

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 62.06  E-value: 2.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGEFEifEADNGTDGLELVYHL---VPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVILL 1207
Cdd:PRK10816     3 VLVVEDNALLRHHLKVQLQDAGH--QVDAAEDAKEADYYLnehLPDIAIVDLGLPDEDGLSLIRRWRSNDV--SLPILVL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKsRNN 1250
Cdd:PRK10816    79 TARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMR-RNS 120
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
977-1237 3.01e-10

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 64.87  E-value: 3.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  977 NLISNALKFTP----DFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNS-APLAGGFGIGLYLVKAFIE 1051
Cdd:PRK11107   415 NLVGNAIKFTEsgniDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASiSRRHGGTGLGLVITQKLVN 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1052 HHKGTITYTSKQDQGTTF--HVSL---------------LKGK------------------------------------- 1077
Cdd:PRK11107   495 EMGGDISFHSQPNRGSTFwfHLPLdlnpnpiidglptdcLAGKrllyvepnsaaaqatldilsetplevtysptlsqlpe 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1078 EHF-------------GQQFIFEDVAETS---------------VFLDELME-----------NKGELVTVEAENTAVAA 1118
Cdd:PRK11107   575 AHYdilllglpvtfrePLTMLHERLAKAKsmtdflilalpcheqVLAEQLKQdgadaclskplSHTRLLPALLEPCHHKQ 654
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1119 KNSEALSSDTK---TMLLIDDN----QQIRTYLKQIFSgefEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCS 1191
Cdd:PRK11107   655 PPLLPPTDESRlplTVMAVDDNpanlKLIGALLEEQVE---HVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACE 731
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1735101206 1192 RIKEDAVLNHIPVILLTASSSPEIKLKGIEGGADDYISKPFEKEIL 1237
Cdd:PRK11107   732 LIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAML 777
fixJ PRK09390
response regulator FixJ; Provisional
1134-1249 3.37e-10

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 61.17  E-value: 3.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1134 IDDNQQIRTYLKQIF-SGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLnhIPVILLTASSS 1212
Cdd:PRK09390     9 VDDDEAMRDSLAFLLdSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSP--LPVIVMTGHGD 86
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1213 PEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRN 1249
Cdd:PRK09390    87 VPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAP 123
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
961-1073 3.52e-10

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: 58.57  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  961 TIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTgNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAplAGGFG 1040
Cdd:cd16940      4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSAD-DGAVIRVEDNGPGIDEEELEALFERFYRSDGQN--YGGSG 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1735101206 1041 IGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16940     81 LGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1131-1241 3.54e-10

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 61.41  E-value: 3.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE--FEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIpvILL 1207
Cdd:PRK10403     9 VLIVDDHPLMRRGVRQLLELDpgFEVVaEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQI--IIL 86
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:PRK10403    87 TVSDASSDVFALIDAGADGYLLKDSDPEVLLEAI 120
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
96-388 3.63e-10

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 62.34  E-value: 3.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206   96 GNIWASSRNG--LSKLDTRTEKFVHYKLKLSRAVKsdigNITQSHDGNLWITSYNLG-FSYFDIKTASFinyTQINLPRL 172
Cdd:COG4257     28 GAVWFTDQGGgrIGRLDPATGEFTEYPLGGGSGPH----GIAVDPDGNLWFTDNGNNrIGRIDPKTGEI---TTFALPGG 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  173 ASNrVICLFEDSKGLLWVGTQEGN-INIFRHKGGLISKADGLTPQianlptTRINDIFEDHFHNIWIAT--GSGLIYYNR 249
Cdd:COG4257    101 GSN-PHGIAFDPDGNLWFTDQGGNrIGRLDPATGEVTEFPLPTGG------AGPYGIAVDPDGNLWVTDfgANAIGRIDP 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  250 QTNKFTLLQANQPgikskryisvnedndnqllvglqdgglfklniGSNPNFntanyflqpvtgddgfyltqrsvqtLFID 329
Cdd:COG4257    174 DTGTLTEYALPTP--------------------------------GAGPRG-------------------------LAVD 196
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  330 KDKNVWVGTYGDG-IYMISSIKEKFslitkKKYETSGeSPIRFYGMCQDRDGFLWLGTDG 388
Cdd:COG4257    197 PDGNLWVADTGSGrIGRFDPKTGTV-----TEYPLPG-GGARPYGVAVDGDGRVWFAESG 250
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
862-1073 6.25e-10

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: 62.96  E-value: 6.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  862 ISHEFRTPLTLiinpVKDML-FGKSEATDDAGN---LHIIYKNARRLLSLVDQLLLFRKAESDtdklKIVRLNIVSLCHE 937
Cdd:COG5806    208 IAHEVRNPLTV----VRGFIqLLQEPELSDEKRkqyIRIALEELDRAEAIITDYLTFAKPQPE----KLEKIDVSEELEH 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  938 VFLCFNHQARTK--HIQFDFiseKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIa 1015
Cdd:COG5806    280 VIDVLSPYANMNnvEIQTEL---EPGLYIEGDRQKLQQCLINIIKNGIEAMPNGGTLTIDVSIDKNKVIISIKDTGVGM- 355
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735101206 1016 egTGDEL--FGK-FYQLQNSaplagGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:COG5806    356 --TKEQLerLGEpYFSTKEK-----GTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITL 409
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
974-1069 6.36e-10

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: 57.98  E-value: 6.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  974 ALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNS-APLAGGFGIGLYLVKAFIEH 1052
Cdd:cd16952      4 AFSNLVSNAVKYTPPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIErCRNTGGTGLGLAIVKHVMSR 83
                           90
                   ....*....|....*..
gi 1735101206 1053 HKGTITYTSKQDQGTTF 1069
Cdd:cd16952     84 HDARLLIASELGKGSRF 100
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
967-1069 7.52e-10

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: 57.68  E-value: 7.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  967 DREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYLV 1046
Cdd:cd16948      2 DAKWLSFIIGQIVSNALKYSKQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGRNFQESTGMGLYLV 81
                           90       100
                   ....*....|....*....|....*
gi 1735101206 1047 KAFIE--HHKgtITYTSKQDQGTTF 1069
Cdd:cd16948     82 KKLCDklGHK--IDVESEVGEGTTF 104
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1133-1241 1.42e-09

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 62.20  E-value: 1.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1133 LIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLnhIPVILLTASS 1211
Cdd:PRK10923     8 VVDDDSSIRWVLERALAGAgLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTAHS 85
                           90       100       110
                   ....*....|....*....|....*....|
gi 1735101206 1212 SPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:PRK10923    86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALV 115
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
1277-1379 1.51e-09

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 60.82  E-value: 1.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1277 LEKCLQIVEQHLTDPDFSIKTLAAEIGMSHSNLYkRIKSISGQSANSFIRFIRLRKAAEIL--LTTDSTVYETAYKVGLN 1354
Cdd:PRK09685   199 FQKVVALIDQSIQEEILRPEWIAGELGISVRSLY-RLFAEQGLVVAQYIRNRRLDRCADDLrpAADDEKITSIAYKWGFS 277
                           90       100
                   ....*....|....*....|....*
gi 1735101206 1355 DLKYFREQFNKLFGINPSDYIKKYR 1379
Cdd:PRK09685   278 DSSHFSTAFKQRFGVSPGEYRRKFR 302
PRK10490 PRK10490
sensor protein KdpD; Provisional
964-1073 1.65e-09

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 62.75  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  964 IYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFY--QLQNSAPlagGFGI 1041
Cdd:PRK10490   772 IHVDGPLFERVLINLLENAVKYAGAQAEIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFArgNKESAIP---GVGL 848
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1042 GLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:PRK10490   849 GLAICRAIVEVHGGTIWAENRPEGGACFRVTL 880
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
1130-1241 1.72e-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: 57.03  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGEFEI---FEADNgTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVIL 1206
Cdd:cd17575      2 MVLLVDDQAIIGEAVRRALADEEDIdfhYCSDP-TEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIV 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:cd17575     81 LSTKEEPEVKSEAFALGANDYLVKLPDKIELVARI 115
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1132-1181 2.34e-09

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: 54.50  E-value: 2.34e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1735101206  1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMM 1181
Cdd:smart00448    4 LVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMM 54
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1132-1246 2.48e-09

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 56.51  E-value: 2.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGEFEIF---EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVILLT 1208
Cdd:cd19930      2 LIAEDQEMVRGALAALLELEDDLEvvaQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELP--DTKVLIVT 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILK 1246
Cdd:cd19930     80 TFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
1133-1231 2.79e-09

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 55.74  E-value: 2.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1133 LIDDNQQIRTYLKQIFSGEFE---IFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKedAVLNHIPVILLTA 1209
Cdd:cd17565      3 IVDDDKNIIKILSDIIEDDDLgevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLK--DTGSNGKFIMISQ 80
                           90       100
                   ....*....|....*....|..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKP 1231
Cdd:cd17565     81 VSDKEMIGKAYQAGIEFFINKP 102
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
967-1066 2.99e-09

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: 55.93  E-value: 2.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  967 DREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLAGGFGIGLYLV 1046
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGHYGMGLYIA 80
                           90       100
                   ....*....|....*....|
gi 1735101206 1047 KAFIEHHKGTITYTSKQDQG 1066
Cdd:cd16975     81 KNLVEKHGGSLIIENSQKGG 100
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1130-1242 3.13e-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: 56.06  E-value: 3.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIF-SGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVILLT 1208
Cdd:cd17537      2 TVYVVDDDEAVRDSLAFLLrSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGS--NIPIIFIT 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPFEKEILVARVN 1242
Cdd:cd17537     80 GHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIE 113
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1132-1231 3.56e-09

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 56.22  E-value: 3.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIF-SGEFEIFEADNGTDGLEL---------VYHLVPDI--VISDVMMQGLSGIEVCSRIKEDAVL 1199
Cdd:cd17581      2 LAVDDSLVDRKVIERLLrISSCRVTAVDSGKRALEFlgledeedsSNFNEPKVnmIITDYCMPGMTGYDLLKKVKESSAL 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1200 NHIPVILLTASSSPEIKLKGIEGGADDYISKP 1231
Cdd:cd17581     82 KEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
pleD PRK09581
response regulator PleD; Reviewed
1123-1252 3.84e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 60.68  E-value: 3.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1123 ALSSDTKTMLLIDDN----QQIRTYLKQIFSgefEIFEADNgTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAV 1198
Cdd:PRK09581   150 ANKDEDGRILLVDDDvsqaERIANILKEEFR---VVVVSDP-SEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKER 225
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735101206 1199 LNHIPVILLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKS-------RNNLQ 1252
Cdd:PRK09581   226 TRYVPILLLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRkryqdalRNNLE 286
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
968-1073 3.91e-09

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: 55.51  E-value: 3.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  968 REKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYqlqNSAPLAGGFGIGLYLVK 1047
Cdd:cd16943      1 PSQLNQVLLNLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFF---TTKPVGEGTGLGLSLSY 77
                           90       100
                   ....*....|....*....|....*.
gi 1735101206 1048 AFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16943     78 RIIQKHGGTIRVASVPGGGTRFTIIL 103
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
1270-1374 4.00e-09

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: 60.07  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1270 SQEYKEFLEKCLQIVEQHLTDPDfSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEiLLTTDSTVYETAY 1349
Cdd:COG2169     79 SPPRADLVARACRLIEAGAEDRP-SLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQ-LLQTGLSVTDAAY 156
                           90       100
                   ....*....|....*....|....*
gi 1735101206 1350 KVGLNDLKYFREQFNKLFGINPSDY 1374
Cdd:COG2169    157 AAGFGSLSRFYEAFKKLLGMTPSAY 181
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
971-1073 1.41e-08

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: 53.61  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  971 MEIALFNLISNALKFTPdfGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNsAPLAGGFGIGLYLVKAFI 1050
Cdd:cd16950      1 LKRVLSNLVDNALRYGG--GWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDN-ARGTSGTGLGLAIVQRIS 77
                           90       100
                   ....*....|....*....|...
gi 1735101206 1051 EHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16950     78 DAHGGSLTLANRAGGGLCARIEL 100
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
844-1057 1.63e-08

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 58.68  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  844 SAEKDKELNERklSFFTNISHEFRTPLTLIINPVKDMLFGKSEATDDagNLHIIYKNARRLLSLVDQLLLFRKAESDTDK 923
Cdd:NF012163   231 STLEKNEQMRR--DFMADISHELRTPLAVLRAELEAIQDGIRKFTPE--SLDSLQAEVGTLTKLVDDLHDLSMSDEGALA 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  924 LKIVRLNIVSLCHEVFLCFNHQ--ARTKHIQFDFiseKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGN 1001
Cdd:NF012163   307 YQKASVDLVPLLEVEGGAFRERfaSAGLELEVSL---PDSSLVFGDRDRLMQLFNNLLENSLRYTDSGGSLHISASQRPK 383
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1735101206 1002 GITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLA-GGFGIGLYLVKAFIEHHKGTI 1057
Cdd:NF012163   384 EVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRAsGGSGLGLAISLNIVQAHGGTL 440
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
977-1066 2.28e-08

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: 53.35  E-value: 2.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  977 NLISNALKFTP-DFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFY-QLQNSAPLAGGFGIGLYLVKAFIEHHK 1054
Cdd:cd16953      7 NLIGNAISFSPpDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYtERPANEAFGQHSGLGLSISRQIIEAHG 86
                           90
                   ....*....|..
gi 1735101206 1055 GTITYTSKQDQG 1066
Cdd:cd16953     87 GISVAENHNQPG 98
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1132-1237 2.40e-08

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: 53.40  E-value: 2.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELV------YHLVpdivISDVMMQGLSGIEVCSRIKEdavLNHIPV 1204
Cdd:cd17584      2 LVVDDDPTCLAILKRMLLRCgYQVTTCTDAEEALSMLrenkdeFDLV----ITDVHMPDMDGFEFLELIRL---EMDLPV 74
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1735101206 1205 ILLTASSSPEIKLKGIEGGADDYISKPFEKEIL 1237
Cdd:cd17584     75 IMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
842-1128 2.98e-08

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 58.38  E-value: 2.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  842 QLSAEKDKElNERKLSFFTNISHEFRTPLTLIINPVKdMLFGKSEATDDAGNLHIIYKNARRLLSLVDQLLLFRKAESDT 921
Cdd:PRK11466   432 QARAEAEKA-SQAKSAFLAAMSHEIRTPLYGILGTAQ-LLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGG 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  922 DKlkivrlniVSLCHEVF---------LCFNH---QARTKHIQFDFiSEKDTIEIYADREKMEIALFNLISNALKFTpDF 989
Cdd:PRK11466   510 KN--------VSVSDEPFeprpllestLQLMSgrvKGRPIRLATDI-ADDLPTALMGDPRRIRQVITNLLSNALRFT-DE 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  990 GLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSaplAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTF 1069
Cdd:PRK11466   580 GSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGK---RGGTGLGLTISSRLAQAMGGELSATSTPEVGSCF 656
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735101206 1070 HVSL------LKGKEHFGQQ--------FIFEDVAETSVFLDELMENKGELVTVeAENtavAAKNSEALSSDT 1128
Cdd:PRK11466   657 CLRLplrvatAPVPKTVNQAvrldglrlLLIEDNPLTQRITAEMLNTSGAQVVA-VGN---AAQALETLQNSE 725
PRK10336 PRK10336
two-component system response regulator QseB;
1131-1265 3.70e-08

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 55.67  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTA 1209
Cdd:PRK10336     3 ILLIEDDMLIGDGIKTGLSKMgFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKG--QREPVLILTA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPF-------EKEILVARVNGilKSRNNLQkyfYNEITLNKSN 1265
Cdd:PRK10336    81 RDALAERVEGLRLGADDYLCKPFalievaaRLEALMRRTNG--QASNELR---HGNVMLDPGK 138
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
45-245 3.71e-08

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 56.18  E-value: 3.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206   45 ITQDDKGFMWFAT--NDGLNRFDGTT--FKVFKSRAGDStalasnYVQKVLCDVHGNIW--ASSRNGLSKLDTRTEKFVH 118
Cdd:COG4257     64 IAVDPDGNLWFTDngNNRIGRIDPKTgeITTFALPGGGS------NPHGIAFDPDGNLWftDQGGNRIGRLDPATGEVTE 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  119 YKLKLSRAVKSDignITQSHDGNLWITSYNLG-FSYFDIKTASFinyTQINLPRLASnRVICLFEDSKGLLWVGTQEGNI 197
Cdd:COG4257    138 FPLPTGGAGPYG---IAVDPDGNLWVTDFGANaIGRIDPDTGTL---TEYALPTPGA-GPRGLAVDPDGNLWVADTGSGR 210
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1735101206  198 nIFRhkgglISKADG-----LTPQIANLPTtrinDIFEDHFHNIWIA-TGSGLI 245
Cdd:COG4257    211 -IGR-----FDPKTGtvteyPLPGGGARPY----GVAVDGDGRVWFAeSGANRI 254
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
1131-1241 3.79e-08

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: 52.82  E-value: 3.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDD----NQQIRTYLKQifSGeFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavlNH--IPV 1204
Cdd:cd17573      1 ILLIEDdstlGKEISKGLNE--KG-YQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKE----KHpsIVV 73
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1735101206 1205 ILLTASSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:cd17573     74 IVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1134-1231 4.50e-08

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: 52.37  E-value: 4.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1134 IDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTASSS 1212
Cdd:cd17602      4 VDDRPSIQKMIEYFLEKQgFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDG 83
                           90
                   ....*....|....*....
gi 1735101206 1213 PEIKLKGIEGGADDYISKP 1231
Cdd:cd17602     84 LVDRIRAKMAGASGYLTKP 102
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1152-1239 7.16e-08

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: 52.15  E-value: 7.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1152 FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavlNHIP--VILLTASSSPEIKLKGIEGGADDYIS 1229
Cdd:cd17593     26 VEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPV----EQLEtkVIVVSGDVQPEAKERVLELGALAFLK 101
                           90
                   ....*....|
gi 1735101206 1230 KPFEKEILVA 1239
Cdd:cd17593    102 KPFDPEKLAQ 111
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
1273-1374 7.40e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 51.85  E-value: 7.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1273 YKEFLEKCLQIVEQHLTDPdFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVG 1352
Cdd:PRK10219     3 HQKIIQTLIAWIDEHIDQP-LNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLG 81
                           90       100
                   ....*....|....*....|..
gi 1735101206 1353 LNDLKYFREQFNKLFGINPSDY 1374
Cdd:PRK10219    82 YVSQQTFSRVFRRQFDRTPSDY 103
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
1132-1241 9.73e-08

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: 51.93  E-value: 9.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTASS 1211
Cdd:cd17539      2 LLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVADPG 81
                           90       100       110
                   ....*....|....*....|....*....|
gi 1735101206 1212 SPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:cd17539     82 DRGRLIRALEIGVNDYLVRPIDPNELLARV 111
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
977-1079 1.16e-07

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 56.38  E-value: 1.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  977 NLISNA----LKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPlaGGFGIGLYLVKAFIEH 1052
Cdd:PRK15053   439 NLLDNAfeasLRSDEGNKIVELFLSDEGDDVVIEVADQGCGVPESLRDKIFEQGVSTRADEP--GEHGIGLYLIASYVTR 516
                           90       100
                   ....*....|....*....|....*..
gi 1735101206 1053 HKGTITYTSKQDQGTTFHVSLLKGKEH 1079
Cdd:PRK15053   517 CGGVITLEDNDPCGTLFSIFIPKVKPN 543
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
977-1237 1.31e-07

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 56.52  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  977 NLISNALKFTpDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQL-QNSAPLAGGFGIGLYLVKAFIEHHKG 1055
Cdd:PRK10841   569 NLLSNAIKFT-DTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVgTGVQRNFQGTGLGLAICEKLINMMDG 647
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1056 TITYTSKQDQGTTFHVSL---------------LKGK-----------EHF----------------GQQFIFEDV---- 1089
Cdd:PRK10841   648 DISVDSEPGMGSQFTIRIplygaqypqkkgvegLQGKrcwlavrnaslEQFletllqrsgiqvqryeGQEPTPEDVlitd 727
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1090 --------AETSVFLD--------ELMENK--------GEL---------VTVEAENTAVAAKNSEALSSDTKT-MLLID 1135
Cdd:PRK10841   728 dpvqkkwqGRAVITFCrrhigiplEIAPGEwvhstatpHELpallariyrIELESDDSANALPSTDKAVSDNDDmMILVV 807
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1136 DNQQIRTYL--KQIFSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVILLTASSSP 1213
Cdd:PRK10841   808 DDHPINRRLlaDQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGL--TLPVIGVTANALA 885
                          330       340
                   ....*....|....*....|....
gi 1735101206 1214 EIKLKGIEGGADDYISKPFEKEIL 1237
Cdd:PRK10841   886 EEKQRCLEAGMDSCLSKPVTLDVL 909
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
1130-1253 1.56e-07

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: 51.60  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKE---DAVLnhipvIL 1206
Cdd:cd17596      2 TILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRErwpEVVR-----II 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1735101206 1207 LTASSSPEIKLKGI-EGGADDYISKPFEKEILVARVNGILKSRnNLQK 1253
Cdd:cd17596     77 ISGYTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRNAARLF-ELQR 123
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
967-1057 1.98e-07

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: 50.54  E-value: 1.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  967 DREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLA-GGFGIGLYL 1045
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRAsGGSGLGLAI 80
                           90
                   ....*....|..
gi 1735101206 1046 VKAFIEHHKGTI 1057
Cdd:cd16946     81 CHNIALAHGGTI 92
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1130-1240 2.06e-07

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: 51.09  E-value: 2.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDN---QQI-RTYLKQIfSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVI 1205
Cdd:cd19925      2 NVLIVEDDpmvAEIhRAYVEQV-PGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAG--HDVDVI 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1206 LLTASSSPEIKLKGIEGGADDYISKPFEKEILVAR 1240
Cdd:cd19925     79 VVTAANDVETVREALRLGVVDYLIKPFTFERLRQR 113
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
850-1058 2.64e-07

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 55.02  E-value: 2.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  850 ELNER-KLSFFTNISHEFRTPLTLiinpvkdmLFGKSEATDDA----------------GNLHIIYKNARRLLSLVDQLL 912
Cdd:PRK10549   234 EKNEQmRRDFMADISHELRTPLAV--------LRGELEAIQDGvrkftpesvaslqaevGTLTKLVDDLHQLSLSDEGAL 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  913 LFRKAEsdtdklkivrLNIVSLCHEVFLCFNHQARTKHIQFDFiSEKDTIEIYADREKMeIALF-NLISNALKFTPDFGL 991
Cdd:PRK10549   306 AYRKTP----------VDLVPLLEVAGGAFRERFASRGLTLQL-SLPDSATVFGDPDRL-MQLFnNLLENSLRYTDSGGS 373
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735101206  992 VTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLA-GGFGIGLYLVKAFIEHHKGTIT 1058
Cdd:PRK10549   374 LHISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRAsGGSGLGLAICLNIVEAHNGRII 441
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
950-1057 3.02e-07

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 54.55  E-value: 3.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  950 HIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDfgLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQL 1029
Cdd:PRK09470   333 GKSLTVSAPPGPWPINGNPNALASALENIVRNALRYSHT--KIEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRV 410
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1735101206 1030 Q-----NSaplaGGFGIGLYLVKAFIEHHKGTI 1057
Cdd:PRK09470   411 DeardrES----GGTGLGLAIVENAIQQHRGWV 439
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
971-1073 3.57e-07

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: 49.74  E-value: 3.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  971 MEIALFNLISNALKFTPDfgLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSAPLA-GGFGIGLYLVKAF 1049
Cdd:cd16939      1 MARALDNLLRNALRYAHR--TVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRAtGGFGLGLAIVHRV 78
                           90       100
                   ....*....|....*....|....
gi 1735101206 1050 IEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16939     79 ALWHGGHVECDDSELGGACFRLTW 102
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
1131-1231 4.23e-07

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: 49.42  E-value: 4.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdaVLNHIPVILLTA 1209
Cdd:cd19928      1 ILVADDDRAIRTVLTQALGRAgYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKK--ARPDLPIIVMSA 78
                           90       100
                   ....*....|....*....|..
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKP 1231
Cdd:cd19928     79 QNTLMTAVKAAERGAFEYLPKP 100
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
1132-1241 4.49e-07

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: 49.95  E-value: 4.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFS--GEFEIFEADNGTDGLELVYHLVPDIVISDVMMQ-GLSGIEVCSRIKEDAVLNHIPV-ILL 1207
Cdd:cd17589      2 LIVDDQPTFRSMLKSMLRslGVTRIDTASSGEEALRMCENKTYDIVLCDYNLGkGKNGQQLLEELRHKKLISPSTVfIMV 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARV 1241
Cdd:cd17589     82 TGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
977-1073 7.41e-07

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 53.76  E-value: 7.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  977 NLISNAL---KFTPDfGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQLQNSaplagGFGIGLYLVKAFIEHH 1053
Cdd:PRK11086   440 NLIENALeavGGEEG-GEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTKGS-----NRGVGLYLVKQSVENL 513
                           90       100
                   ....*....|....*....|
gi 1735101206 1054 KGTITYTSKQDQGTTFHVSL 1073
Cdd:PRK11086   514 GGSIAVESEPGVGTQFFVQI 533
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
1129-1239 9.31e-07

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: 48.98  E-value: 9.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFS--GeFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdaVLNHIPVIL 1206
Cdd:cd17563      1 KSLLLVDDDEVFAERLARALErrG-FEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRA--LQPDARIVV 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1207 LTASSS-----PEIKLkgiegGADDYISKPFE-KEILVA 1239
Cdd:cd17563     78 LTGYASiatavEAIKL-----GADDYLAKPADaDEILAA 111
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
1173-1231 1.42e-06

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: 48.17  E-value: 1.42e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1735101206 1173 DIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTASSSPEIKLKGIEGGADDYISKP 1231
Cdd:cd17582     46 DLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1132-1248 1.66e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 52.07  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIRTYLKQIFSGEFEI---FEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavLNHIPVIL-- 1206
Cdd:PRK00742     7 LVVDDSAFMRRLISEILNSDPDIevvGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMR---LRPTPVVMvs 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1735101206 1207 -LTASSSpEIKLKGIEGGADDYISKPFE---------KEILVARVNGILKSR 1248
Cdd:PRK00742    84 sLTERGA-EITLRALELGAVDFVTKPFLgislgmdeyKEELAEKVRAAARAR 134
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
950-1073 1.90e-06

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 52.37  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  950 HIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTIN---------------DTGNGITINIKDSGCGI 1014
Cdd:PRK13837   540 GVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGRVDISLSraklrapkvlshgvlPPGRYVLLRVSDTGAGI 619
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1735101206 1015 AEGTGDELFGKFYQLQnsaplAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:PRK13837   620 DEAVLPHIFEPFFTTR-----AGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYL 673
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
365-530 3.23e-06

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: 50.28  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  365 GESPIRfygmcqDRDGFLWLgTDGEG--LFKTSRNGTLIKQYK-ADGRAGSITdnailygyTDSNGNVWFGTYAKGLLLY 441
Cdd:COG3386     10 GEGPVW------DPDGRLYW-VDIPGgrIHRYDPDGGAVEVFAePSGRPNGLA--------FDPDGRLLVADHGRGLVRF 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  442 NKKTDSFTSYAHNAsDSKSLGGNDVRViyqDSRKNIWIGT-----NGGGLSLFDP---VSK-----TFSN---FTP---- 501
Cdd:COG3386     75 DPADGEVTVLADEY-GKPLNRPNDGVV---DPDGRLYFTDmgeylPTGALYRVDPdgsLRVladglTFPNgiaFSPdgrt 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1735101206  502 ---ANSG---LTAYDVRA----------------------ITEDEQGNLWIGTYGGG 530
Cdd:COG3386    151 lyvADTGagrIYRFDLDAdgtlgnrrvfadlpdgpggpdgLAVDADGNLWVALWGGG 207
PRK10643 PRK10643
two-component system response regulator PmrA;
1203-1265 3.26e-06

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 49.65  E-value: 3.26e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735101206 1203 PVILLTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRNNLQKYFYN--EITLNKSN 1265
Cdd:PRK10643    74 PVLILTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQGQGENELQvgNLTLNLGR 138
PRK10604 PRK10604
sensor protein RstB; Provisional
949-1069 3.97e-06

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 51.14  E-value: 3.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  949 KHIQFDFISEKDTIeiYADREKMEIALFNLISNALKFTPdfGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYQ 1028
Cdd:PRK10604   300 KTVRLDTPHQGDYG--ALDMRLMERVLDNLLNNALRYAH--SRVRVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVR 375
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1735101206 1029 LQNSAPLA-GGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTF 1069
Cdd:PRK10604   376 LDPSRDRAtGGCGLGLAIVHSIALAMGGSVNCDESELGGARF 417
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
1130-1241 4.54e-06

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


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 46.86  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFS--GEFEIFEADNGTDGLELVYHLVPDIVISDV-MMQGLSGIEVCSRIKEDavlNHIPVIL 1206
Cdd:cd17540      2 RVLIIEDEPLIAMDLEQIVEdlGHQVVGIARTRDEAVALARRERPDLILADIqLADGSSGIDAVNEILTT---HDVPVIF 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1735101206 1207 LTAssSPEIKLKGiEGGADDY-ISKPFEKEILVARV 1241
Cdd:cd17540     79 VTA--YPERLLTG-ERPEPTFlITKPFDPEMVKAAI 111
PRK15115 PRK15115
response regulator GlrR; Provisional
1131-1248 5.45e-06

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 50.61  E-value: 5.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGE-FEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdaVLNHIPVILLTA 1209
Cdd:PRK15115     8 LLLVDDDPGLLKLLGMRLTSEgYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQK--VQPGMPVIILTA 85
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1735101206 1210 SSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSR 1248
Cdd:PRK15115    86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQS 124
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
971-1073 7.12e-06

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: 46.60  E-value: 7.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  971 MEIALFNLISNALKFTPDFG-LVTCTINDT--------------GNGITINIKDSGCGIAEGTGDELFGKFYqlqNSAPL 1035
Cdd:cd16919      1 LELAILNLAVNARDAMPEGGrLTIETSNQRvdadyalnyrdlipGNYVCLEVSDTGSGMPAEVLRRAFEPFF---TTKEV 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1735101206 1036 AGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16919     78 GKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYL 115
PRK14084 PRK14084
DNA-binding response regulator;
1132-1269 9.22e-06

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 48.59  E-value: 9.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1132 LLIDDNQQIR---TYLKQIFSGEFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavLNHIPVILLt 1208
Cdd:PRK14084     4 LIVDDEPLARnelTYLLNEIGGFEEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQK---MKEPPAIIF- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735101206 1209 ASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSR---NNLQKYFYNEITLNKSNDLKI 1269
Cdd:PRK14084    80 ATAHDQFAVKAFELNATDYILKPFEQKRIEQAVNKVRATKakdDNNASAIANDMSANFDQSLPI 143
ftrA PRK09393
transcriptional activator FtrA; Provisional
1277-1379 1.44e-05

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 48.81  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1277 LEKCLQIVEQHLTDPdFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDL 1356
Cdd:PRK09393   220 LGPLIDWMRAHLAEP-HTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSE 298
                           90       100
                   ....*....|....*....|...
gi 1735101206 1357 KYFREQFNKLFGINPSDYIKKYR 1379
Cdd:PRK09393   299 ESLRHHFRRRAATSPAAYRKRFG 321
PLN03029 PLN03029
type-a response regulator protein; Provisional
1173-1231 1.58e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 47.72  E-value: 1.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1735101206 1173 DIVISDVMMQGLSGIEVCSRIKEDAVLNHIPVILLTASSSPEIKLKGIEGGADDYISKP 1231
Cdd:PLN03029    74 NLIITDYCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKP 132
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
978-1073 2.44e-05

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 48.75  E-value: 2.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  978 LISNALK--FTPDF-GLVTCTINDTGNGITINIKDSGCGIAEGTgdelfgkfyqlqnSAPLAGGFgiGLYLVKAFIEHHK 1054
Cdd:COG3920    407 LVTNALKhaFLSGEgGRIRVSWRREDGRLRLTVSDNGVGLPEDV-------------DPPARKGL--GLRLIRALVRQLG 471
                           90
                   ....*....|....*....
gi 1735101206 1055 GTITYTSkqDQGTTFHVSL 1073
Cdd:COG3920    472 GTLELDR--PEGTRVRITF 488
PRK11697 PRK11697
two-component system response regulator BtsR;
1130-1237 3.05e-05

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 47.15  E-value: 3.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFS--GEFEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavlnHIP-VI 1205
Cdd:PRK11697     3 KVLIVDDEPLAREELRELLQeeGDIEIVgECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPE----HMPyIV 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1735101206 1206 LLTASSspEIKLKGIEGGADDYISKPFEKEIL 1237
Cdd:PRK11697    79 FVTAFD--EYAIKAFEEHAFDYLLKPIDPARL 108
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
852-903 3.39e-05

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: 42.97  E-value: 3.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1735101206  852 NERKLSFFTNISHEFRTPLTLIINPVKDMLFGKSEATDDAGNLHIIYKNARR 903
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAER 52
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
1130-1232 7.79e-05

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: 43.26  E-value: 7.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYL-KQIFSGEFEIFEADNGTDGLELVYHLVP-DIVISDVMMQGLSGIEVCSRIKEdaVLNHIPVILL 1207
Cdd:cd18160      1 TILLADDEPSVRKFIvTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARK--IDPDVKILFI 78
                           90       100
                   ....*....|....*....|....*..
gi 1735101206 1208 T--ASSSPEIKLKGIegGADDYISKPF 1232
Cdd:cd18160     79 SggAAAAPELLSDAV--GDNATLKKPF 103
PRK09483 PRK09483
response regulator; Provisional
1130-1259 1.02e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 45.10  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGEFEIF---EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVlnHIPVIL 1206
Cdd:PRK09483     3 NVLLVDDHELVRAGIRRILEDIKGIKvvgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTP--DVKIIM 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISK---PFEKeilvarVNGIlKSRNNLQKYFYNEI 1259
Cdd:PRK09483    81 LTVHTENPLPAKVMQAGAAGYLSKgaaPQEV------VSAI-RSVHSGQRYIASDI 129
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
947-1073 1.03e-04

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: 43.77  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  947 RTKHIQFDF-ISEKDTIEIyaDREK-MEIaLFNLISNALKFTPDFglVTCTINDTGNGITINIKDSGCGIAEGTGDELFG 1024
Cdd:cd16954     15 QRKGVSISLdISPELRFPG--ERNDlMEL-LGNLLDNACKWCLEF--VEVTARQTDGGLHLIVDDDGPGVPESQRSKIFQ 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1735101206 1025 KFYQLQNSAPlagGFGIGLYLVKAFIEHHKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16954     90 RGQRLDEQRP---GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
1131-1232 1.05e-04

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: 42.72  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSGEFEIFEADNGTDGLELV-YHLVPDIVISDVMMQG-LSGIEVCSRIKedAVLNHIPVILLT 1208
Cdd:cd18161      2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLeSGPDIDLLVTDVIMPGgMNGSQLAEEAR--RRRPDLKVLLTS 79
                           90       100
                   ....*....|....*....|....
gi 1735101206 1209 ASSSPEIKLKGIEGGAdDYISKPF 1232
Cdd:cd18161     80 GYAENAIEGGDLAPGV-DVLSKPF 102
PRK10360 PRK10360
transcriptional regulator UhpA;
1130-1305 1.05e-04

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 44.97  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIFSGEFE---IFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavlnhIPVIL 1206
Cdd:PRK10360     3 TVALIDDHLIVRSGFAQLLGLEPDlqvVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQLPKG-----MATIM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1207 LTASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSrnnlQKYFYNEITlnksndLKISQEYKEFLEKCLQIVEQ 1286
Cdd:PRK10360    78 LSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTVATG----GCYLTPDIA------IKLASGRQDPLTKRERQVAE 147
                          170
                   ....*....|....*....
gi 1735101206 1287 HLTDpDFSIKTLAAEIGMS 1305
Cdd:PRK10360   148 KLAQ-GMAVKEIAAELGLS 165
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
854-903 1.07e-04

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 41.43  E-value: 1.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1735101206  854 RKLSFFTNISHEFRTPLTLIINPVKdMLFGKSEATDDAGNLHIIYKNARR 903
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLE-LLRDEKLDEEQREYLETILRSAER 49
PRK10693 PRK10693
two-component system response regulator RssB;
1156-1231 1.65e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 45.37  E-value: 1.65e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735101206 1156 EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAvlNHIPVILLTASSS-PEIKlKGIEGGADDYISKP 1231
Cdd:PRK10693     2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRG--DQTPVLVISATENmADIA-KALRLGVQDVLLKP 75
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
1292-1385 2.24e-04

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 44.92  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1292 DFSIKTLAAEIGMSHSNLYKRIKSiSGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKLFGINP 1371
Cdd:PRK09978   158 EWTLARIASELLMSPSLLKKKLRE-EETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTP 236
                           90
                   ....*....|....
gi 1735101206 1372 SDYIKKYRKPFHNN 1385
Cdd:PRK09978   237 TEYQERSAQGLPNR 250
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
719-797 2.63e-04

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 40.94  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  719 ITLGPDQSVFSIQYASLNYTYPDKGGF---AYKLDGLDKTWNYVGDQRlATYRYLEPGVYTFRVKASNQDGLWFDNCATL 795
Cdd:cd00146      1 PTASVSAPPVAELGASVTFSASDSSGGsivSYKWDFGDGEVSSSGEPT-VTHTYTKPGTYTVTLTVTNAVGSSSTKTTTV 79

                   ..
gi 1735101206  796 QV 797
Cdd:cd00146     80 VV 81
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
1297-1373 3.98e-04

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 43.90  E-value: 3.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735101206 1297 TLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKLFGINPSD 1373
Cdd:PRK13503   192 ALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRD 268
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1129-1262 4.08e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 43.65  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1129 KTMLLIDDNQQIRTYLKQIFSgeFEIFEADNGTDGLELVYHLVP---DIVISDVMMQGLSGIEVcsrIKEDAVLNHIPVI 1205
Cdd:PRK13856     2 KHVLVIDDDVAMRHLIVEYLT--IHAFKVTAVADSQQFNRVLASetvDVVVVDLNLGREDGLEI---VRSLATKSDVPII 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735101206 1206 LLTASSSPEI-KLKGIEGGADDYISKPFEKEILVARVNGILKSRNNLQK------YFYNEITLN 1262
Cdd:PRK13856    77 IISGDRLEEAdKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVVRtkdrrsFCFADWTLN 140
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1151-1240 4.58e-04

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 43.47  E-value: 4.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1151 EFEIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCS--RIKEDAvlnhiPVILLTASSSPEIKLKGIEGGADDYI 1228
Cdd:PRK10701    25 DIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRdlRPKWQG-----PIVLLTSLDSDMNHILALEMGACDYI 99
                           90
                   ....*....|..
gi 1735101206 1229 SKPFEKEILVAR 1240
Cdd:PRK10701   100 LKTTPPAVLLAR 111
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
854-903 4.99e-04

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 39.86  E-value: 4.99e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1735101206   854 RKLSFFTNISHEFRTPLTLIINPVKdmLFGKSEATDDAGN-LHIIYKNARR 903
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLE--LLLDTELSEEQREyLETILREAER 49
PRK15369 PRK15369
two component system response regulator;
1131-1249 5.51e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 42.76  E-value: 5.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1131 MLLIDDNQQIRTYLKQIFSG--EFEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDavLNHIPVILL 1207
Cdd:PRK15369     6 ILLVDDHELIINGIKNMLAPypRYKIVgQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQR--WPAMNILVL 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVNGILKSRN 1249
Cdd:PRK15369    84 TARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKR 125
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1073 8.60e-04

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 40.13  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  975 LFNLISNALKFTPDF--GLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFYqlqNSAPLAGGFGIGLYLVKAFIEH 1052
Cdd:cd16976      5 LMNLLQNALDAMGKVenPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFF---TTKPVGKGTGLGLSISYGIVEE 81
                           90       100
                   ....*....|....*....|.
gi 1735101206 1053 HKGTITYTSKQDQGTTFHVSL 1073
Cdd:cd16976     82 HGGRLSVANEEGAGARFTFDL 102
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
1130-1239 9.57e-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: 40.50  E-value: 9.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIR----TYLKQIFSGEfeIFEADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEdavlNHIPVI 1205
Cdd:cd17530      2 RVLVLDDDPFQCmmaaTILEDLGPGN--VDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAE----SHSNAA 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1735101206 1206 LLTASSSPEIKLKGIEGGADDY-------ISKPFEKEILVA 1239
Cdd:cd17530     76 VILMSGLDGGILESAETLAGANglnllgtLSKPFSPEELTE 116
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
1130-1255 1.08e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 41.80  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1130 TMLLIDDNQQIRTYLKQIF-SGEFEIF-EADNGTDGLELVYHLVPDIVISDVMMQGLSGIEVCSRIKEDAVLNHIpvILL 1207
Cdd:PRK09958     2 NAIIIDDHPLAIAAIRNLLiKNDIEILaELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGII--IIV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1735101206 1208 TASSSPEIKLKGIEGGADDYISKPFEKEILVARVNgilkSRNNLQKYF 1255
Cdd:PRK09958    80 SAKNDHFYGKHCADAGANGFVSKKEGMNNIIAAIE----AAKNGYCYF 123
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
1277-1379 1.31e-03

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 42.27  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1277 LEKClQIVEQHLTDpDFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDL 1356
Cdd:PRK10572   186 REAC-QYISDHLAS-EFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQ 263
                           90       100
                   ....*....|....*....|...
gi 1735101206 1357 KYFREQFNKLFGINPSDYIKKYR 1379
Cdd:PRK10572   264 LYFSRVFKKCTGASPSEFRARCE 286
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
1251-1374 1.58e-03

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 41.96  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1251 LQKYFYneitlnKSNDLKISQeYKEFLEKCLQIVEQHLTDPdFSIKTLAAEIGMSHSNLYKRIKSISGQSANSFIRFIRL 1330
Cdd:PRK13502   159 LKRHRY------ATDDLPATS-RETLLDKLITALANSLECP-FALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRI 230
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1735101206 1331 RKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKLFGINPSDY 1374
Cdd:PRK13502   231 CHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQW 274
glnL PRK11073
nitrogen regulation protein NR(II);
963-1061 1.77e-03

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 42.38  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  963 EIYADREKMEIALFNLISNALK-FTPDFGLVTCTINdTGNGIT-----------INIKDSGCGIAEGTGDELFgkfYqlq 1030
Cdd:PRK11073   230 ELAHDPDQIEQVLLNIVRNALQaLGPEGGTITLRTR-TAFQLTlhgeryrlaarIDIEDNGPGIPPHLQDTLF---Y--- 302
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1735101206 1031 nsaPLA----GGFGIGLYLVKAFIEHHKGTITYTS 1061
Cdd:PRK11073   303 ---PMVsgreGGTGLGLSIARNLIDQHSGKIEFTS 334
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
978-1073 2.03e-03

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 42.31  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  978 LISNA----LKFTPDFGLVTCTINDTGNGITINIKDSGCGIAEGTGDELFGKFyqlqnsAPLAGGFGIGLYLVKAFIEHH 1053
Cdd:COG2972    344 LVENAiehgIEPKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEEL------SSKGEGRGIGLRNVRERLKLY 417
                           90       100
                   ....*....|....*....|...
gi 1735101206 1054 ---KGTITYTSKQDQGTTFHVSL 1073
Cdd:COG2972    418 ygeEYGLEIESEPGEGTTVTIRI 440
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
932-1068 2.06e-03

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 42.26  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  932 VSLCHEVFLC----FNHQARTKHIQFDFISEKDTIEIYADREKMEIALFNLISNALKFTPDFGLVTCTINDTGNGITINI 1007
Cdd:PRK10755   205 VKLLEDVILPsqdeLSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTITIKLSQEDGGAVLAV 284
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735101206 1008 KDSGCGIAEGTGDELFGKFYQLQNSaplAGGFGIGLYLVKAFIEHHKGTITYTSKQDQGTT 1068
Cdd:PRK10755   285 EDEGPGIDESKCGELSKAFVRMDSR---YGGIGLGLSIVSRITQLHHGQFFLQNRQERSGT 342
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
1304-1383 2.15e-03

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 41.81  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1304 MSHSNLYKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKLFGINPSDYIKKY-RKPF 1382
Cdd:PRK13501   204 LVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRFiRSPV 283

                   .
gi 1735101206 1383 H 1383
Cdd:PRK13501   284 L 284
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
1289-1376 2.60e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 41.52  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206 1289 TDPD--FSIKTLAAEIGMSHSNLyKRIKSISGQSANSFIRFIRLRKAAEILLTTDSTVYETAYKVGLNDLKYFREQFNKL 1366
Cdd:PRK15185   217 SSPSrqWKLTDVADHIFMSTSTL-KRKLAEEGTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKY 295
                           90
                   ....*....|
gi 1735101206 1367 FGINPSDYIK 1376
Cdd:PRK15185   296 FKTTPSTFIK 305
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
967-1068 3.15e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 39.13  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  967 DREKMEIALFNLISNALKFTPDF---GLVTCTINDTGNGITINIKDSGCGIAegtgdelfgkFYQLQNSAPLAGGFGIGL 1043
Cdd:COG2172     31 DADDLVLAVSEAVTNAVRHAYGGdpdGPVEVELELDPDGLEIEVRDEGPGFD----------PEDLPDPYSTLAEGGRGL 100
                           90       100
                   ....*....|....*....|....*
gi 1735101206 1044 YLVKAFIEHhkgtITYTSkQDQGTT 1068
Cdd:COG2172    101 FLIRRLMDE----VEYES-DPGGTT 120
envZ PRK09467
osmolarity sensor protein; Provisional
974-1066 4.05e-03

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 41.43  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  974 ALFNLISNALKFTPDFGLVTCtiNDTGNGITINIKDSGCGIAEGTGDELFGKFYQlQNSAPLAGGFGIGLYLVKAFIEHH 1053
Cdd:PRK09467   335 ALANLVVNAARYGNGWIKVSS--GTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTR-GDSARGSSGTGLGLAIVKRIVDQH 411
                           90
                   ....*....|...
gi 1735101206 1054 KGTITYTSKQDQG 1066
Cdd:PRK09467   412 NGKVELGNSEEGG 424
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
307-491 4.91e-03

SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.


Pssm-ID: 462480 [Multi-domain]  Cd Length: 246  Bit Score: 40.32  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  307 LQPVTGDDGFYLTQRSVqTLFIDKDKNVWVGTYGDGIYMISSIKEKFSLITKkkYETSGESPIRFYGMCQDRDGFLWLGT 386
Cdd:pfam08450   27 LDPATGKETVWDTPGPV-GAIAPRDDGGLIVALKDGVALLDLATGELTPLAD--PEDDDWPLNRFNDGKVDPDGRFWFGT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735101206  387 DGEGLFKTSRNGTLIKqYKADGRAGSITDNAILygytdSNGNVWfgtYAKGLLLYNKKTDSFTSYAHNASDSKSLGGNdV 466
Cdd:pfam08450  104 MGDDEAPGGDPGALYR-LDPDGKLTRVLDGLTI-----SNGLAW---SPDGRTLYFADSPARKIWAYDYDLDGGLISN-R 173
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1735101206  467 RVIYQ-------------DSRKNIWIGT-NGGGLSLFDP 491
Cdd:pfam08450  174 RVFADfkpglgrpdgmavDAEGNVWVARwGGGKVVRFDP 212
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
460-483 5.17e-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: 35.75  E-value: 5.17e-03
                           10        20
                   ....*....|....*....|....
gi 1735101206  460 SLGGNDVRVIYQDSRKNIWIGTNG 483
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTNG 24
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
505-528 5.48e-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: 35.75  E-value: 5.48e-03
                           10        20
                   ....*....|....*....|....
gi 1735101206  505 GLTAYDVRAITEDEQGNLWIGTYG 528
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTNG 24
 
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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