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Conserved domains on  [gi|2796455230|ref|WP_373170015|]
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response regulator [Bacteroides ovatus]

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];
20-1058 5.33e-65

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


:

Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 239.12  E-value: 5.33e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230   20 YRYLGVEDGLSNRRVYCIQKDKTGYMWFLTHEGIDRYNGKEFKRYKLMDGDAEVNSLLNLNWLYIDQEGVLWeIGKKGKV 99
Cdd:COG3292     24 FRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNYIRALLEDSDGRLW-IGTDGGL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  100 FRYDQIHDCFSLVYKLPMESfseqPDPVTYAWLDQNKHIWLCNKDTIFLYNTDTKQVTHIKNDiseeitdieqideshff 179
Cdd:COG3292    103 SRYDPKTDKFTRYPLDPGLP----NNSIRSIAEDSDGNIWVGTSNGLYRYDPKTGKFKRFTLD----------------- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  180 igtemgihyaQLENNAlklincdklesvkaqVSDLHFDKKiRKLFIGtflrgimvydmntksvirpdynlkdisitrfkp 259
Cdd:COG3292    162 ----------GLPSNT---------------ITSLAEDAD-GNLWVD--------------------------------- 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  260 lNDKELLIATDGGGVHKINMDTYQIVPeIVADYNSNcGMNGNSINDIFVDDEERIWLANYPIGITIQNNRYTSYKWIKHs 339
Cdd:COG3292    183 -SDGNLWIGTDGNGLYRLDPNTGKFEH-ITHDPDPN-SLSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRH- 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  340 iGNKQSLINDQVNAIIEDREGDLWFatnngisffnsktgqwrsvlsafeesqgnkshiflticevapgIIWAGGYSSGAY 419
Cdd:COG3292    259 -NDPNGLSGNSVRSIAEDSDGNLWI-------------------------------------------RLWIGTYGGGLF 294
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  420 QIDKKTFSVSYFMPplythtNKRPDKYIRDIRTDMQGYIWSGGFYN-LKRINLKTQEVRFYDGLNS-----ITAIVEKDE 493
Cdd:COG3292    295 RLDPKTGKFKRYNP------NGLPSNSVYSILEDSDGNLWIGTSGGgLYRYDPKTGKFTKFSEDNGlsnnfIRSILEDSD 368
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  494 KSMWIGSATGLCLLDKESGKFERIKLPVE-----SNYIYSLYQAKNGSLYIATSGSGLLIYDINKKLFTHYHTENcALIS 568
Cdd:COG3292    369 GNLWVGTNGGLYRLDPKTGKFTNFTHDPDknglsSNYINSIFEDSDGRLWIGTDGGGLYRYDPKTGKFKHFTTKD-GLPS 447
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  569 NNIYTILSDADKDIimstesgLTSFYPNEKKFYNWTKDMGLMTTHFNALSGTLRKNNKFILGSSDGAVEFDKDMKLPRSY 648
Cdd:COG3292    448 NTIYSILEDDNGNL-------WNFNSASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLT 520
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  649 SSKMIFSDFKLFYQTIYpgdedspLKASINDTKVLKLKYNQNRFSLQVSSINYDYPSNILYSWRLEGFYDKWSKPGTENT 728
Cdd:COG3292    521 LLLLALLLLLSLLLLLL-------LLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLL 593
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  729 IRYTNLAPGKYTLRVRAISNEDKRIMLEERSMDIIIAQPFWLTFWAMLVYTAILCLIAIVLLRILILRKQRKVSDEKIHF 808
Cdd:COG3292    594 LLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAEL 673
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  809 FINTAHDIRTPLTLIKAPLEELREKEELSKEGISNmNTALRNVNALLRLTTNLINFERADVYSSELYISEHELNTFMNEI 888
Cdd:COG3292    674 ILELLLILLLLLLLLLLALLLLLLLLLALKLLLLL-LLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLL 752
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  889 FNAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANE 968
Cdd:COG3292    753 ANDIELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKID 832
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  969 QKKLFKLHFRGSNAINSKVTGSGIGL-MLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSKRFRKAHLATPSKQRIENT 1047
Cdd:COG3292    833 LLDILELILLELELGLLLGLLLLLLLeILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIE 912
                         1050
                   ....*....|.
gi 2796455230 1048 IDNVPPPSPEI 1058
Cdd:COG3292    913 LLLEEEVLLAL 923
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1071-1200 1.91e-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: 148.57  E-value: 1.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILL 1149
Cdd:COG0745      2 PRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPIIML 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRALLRSKFANL 1200
Cdd:COG0745     80 TARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDL 130
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1238-1326 1.58e-24

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 104.48  E-value: 1.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1238 ALTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSP 1317
Cdd:COG2207    168 LLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTP 247

                   ....*....
gi 2796455230 1318 SQYGKEKKA 1326
Cdd:COG2207    248 SEYRKRLRA 256
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
20-1058 5.33e-65

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 239.12  E-value: 5.33e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230   20 YRYLGVEDGLSNRRVYCIQKDKTGYMWFLTHEGIDRYNGKEFKRYKLMDGDAEVNSLLNLNWLYIDQEGVLWeIGKKGKV 99
Cdd:COG3292     24 FRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNYIRALLEDSDGRLW-IGTDGGL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  100 FRYDQIHDCFSLVYKLPMESfseqPDPVTYAWLDQNKHIWLCNKDTIFLYNTDTKQVTHIKNDiseeitdieqideshff 179
Cdd:COG3292    103 SRYDPKTDKFTRYPLDPGLP----NNSIRSIAEDSDGNIWVGTSNGLYRYDPKTGKFKRFTLD----------------- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  180 igtemgihyaQLENNAlklincdklesvkaqVSDLHFDKKiRKLFIGtflrgimvydmntksvirpdynlkdisitrfkp 259
Cdd:COG3292    162 ----------GLPSNT---------------ITSLAEDAD-GNLWVD--------------------------------- 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  260 lNDKELLIATDGGGVHKINMDTYQIVPeIVADYNSNcGMNGNSINDIFVDDEERIWLANYPIGITIQNNRYTSYKWIKHs 339
Cdd:COG3292    183 -SDGNLWIGTDGNGLYRLDPNTGKFEH-ITHDPDPN-SLSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRH- 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  340 iGNKQSLINDQVNAIIEDREGDLWFatnngisffnsktgqwrsvlsafeesqgnkshiflticevapgIIWAGGYSSGAY 419
Cdd:COG3292    259 -NDPNGLSGNSVRSIAEDSDGNLWI-------------------------------------------RLWIGTYGGGLF 294
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  420 QIDKKTFSVSYFMPplythtNKRPDKYIRDIRTDMQGYIWSGGFYN-LKRINLKTQEVRFYDGLNS-----ITAIVEKDE 493
Cdd:COG3292    295 RLDPKTGKFKRYNP------NGLPSNSVYSILEDSDGNLWIGTSGGgLYRYDPKTGKFTKFSEDNGlsnnfIRSILEDSD 368
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  494 KSMWIGSATGLCLLDKESGKFERIKLPVE-----SNYIYSLYQAKNGSLYIATSGSGLLIYDINKKLFTHYHTENcALIS 568
Cdd:COG3292    369 GNLWVGTNGGLYRLDPKTGKFTNFTHDPDknglsSNYINSIFEDSDGRLWIGTDGGGLYRYDPKTGKFKHFTTKD-GLPS 447
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  569 NNIYTILSDADKDIimstesgLTSFYPNEKKFYNWTKDMGLMTTHFNALSGTLRKNNKFILGSSDGAVEFDKDMKLPRSY 648
Cdd:COG3292    448 NTIYSILEDDNGNL-------WNFNSASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLT 520
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  649 SSKMIFSDFKLFYQTIYpgdedspLKASINDTKVLKLKYNQNRFSLQVSSINYDYPSNILYSWRLEGFYDKWSKPGTENT 728
Cdd:COG3292    521 LLLLALLLLLSLLLLLL-------LLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLL 593
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  729 IRYTNLAPGKYTLRVRAISNEDKRIMLEERSMDIIIAQPFWLTFWAMLVYTAILCLIAIVLLRILILRKQRKVSDEKIHF 808
Cdd:COG3292    594 LLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAEL 673
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  809 FINTAHDIRTPLTLIKAPLEELREKEELSKEGISNmNTALRNVNALLRLTTNLINFERADVYSSELYISEHELNTFMNEI 888
Cdd:COG3292    674 ILELLLILLLLLLLLLLALLLLLLLLLALKLLLLL-LLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLL 752
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  889 FNAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANE 968
Cdd:COG3292    753 ANDIELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKID 832
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  969 QKKLFKLHFRGSNAINSKVTGSGIGL-MLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSKRFRKAHLATPSKQRIENT 1047
Cdd:COG3292    833 LLDILELILLELELGLLLGLLLLLLLeILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIE 912
                         1050
                   ....*....|.
gi 2796455230 1048 IDNVPPPSPEI 1058
Cdd:COG3292    913 LLLEEEVLLAL 923
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1071-1200 1.91e-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: 148.57  E-value: 1.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILL 1149
Cdd:COG0745      2 PRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPIIML 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRALLRSKFANL 1200
Cdd:COG0745     80 TARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDL 130
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1073-1189 1.00e-34

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: 128.98  E-value: 1.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTA 1151
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLAN 1189
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYILVN 118
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
917-1026 9.45e-29

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 111.59  E-value: 9.45e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230   917 DKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAiNSKVTGSGIGLML 996
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGLGLSI 80
                            90       100       110
                    ....*....|....*....|....*....|
gi 2796455230   997 VWKLVRLHKGKINLSSIENQGSVIKITFPK 1026
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITLPL 110
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1073-1181 1.67e-27

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: 108.01  E-value: 1.67e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILLTA 1151
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKA 1181
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLA 108
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
921-1024 2.47e-27

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: 107.30  E-value: 2.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAinSKVTGSGIGLMLVWKL 1000
Cdd:cd00075      1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKS--REGGGTGLGLAIVRRI 78
                           90       100
                   ....*....|....*....|....
gi 2796455230 1001 VRLHKGKINLSSIENQGSVIKITF 1024
Cdd:cd00075     79 VEAHGGRITVESEPGGGTTFTVTL 102
pleD PRK09581
response regulator PleD; Reviewed
1072-1196 3.64e-25

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 110.76  E-value: 3.64e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLT 1150
Cdd:PRK09581     4 RILVVDDIPANVKLLEAKLLAEYYtVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVT 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLRSK 1196
Cdd:PRK09581    84 ALDDPEDRVRGLEAGADDFLTKPINDVALFARV------KSLTRLK 123
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1238-1326 1.58e-24

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 104.48  E-value: 1.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1238 ALTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSP 1317
Cdd:COG2207    168 LLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTP 247

                   ....*....
gi 2796455230 1318 SQYGKEKKA 1326
Cdd:COG2207    248 SEYRKRLRA 256
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1239-1320 2.33e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 98.01  E-value: 2.33e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  1239 LTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPS 1318
Cdd:smart00342    2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81

                    ..
gi 2796455230  1319 QY 1320
Cdd:smart00342   82 EY 83
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
917-1027 1.49e-23

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: 96.67  E-value: 1.49e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSEtSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNainSKVTGSGIGLML 996
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEITVTLSE-GGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLSI 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2796455230  997 VWKLVRLHKGKINLSSIENQGSVIKITFPKD 1027
Cdd:pfam02518   78 VRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
813-1029 1.60e-22

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 103.89  E-value: 1.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  813 AHDIRTPLTLIKAPLEELREKEELSKEGISnMNTALRNVNALLRLTTNLINFERAdvysSELYISEHELNTFMNEIFNAF 892
Cdd:PRK11360   398 AHEIRNPLTAIRGYVQIWRQQTSDPPSQEY-LSVVLREVDRLNKVIDQLLEFSRP----RESQWQPVSLNALVEEVLQLF 472
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  893 QQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFV-SETSDSWSVEVRDTGIGIPANEQKK 971
Cdd:PRK11360   473 QTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTwQYSDGQVAVSIEDNGCGIDPELLKK 552
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2796455230  972 LFKLHFrgsnaiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSK 1029
Cdd:PRK11360   553 IFDPFF------TTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQ 604
HTH_18 pfam12833
Helix-turn-helix domain;
1244-1320 1.20e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 90.34  E-value: 1.20e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796455230 1244 LCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDT-HSITEIAEMTGFSDAKYFREVFKKHYNVSPSQY 1320
Cdd:pfam12833    1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEY 78
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
1072-1186 2.11e-17

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: 83.69  E-value: 2.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEE---YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIkNNIETSHIP-VI 1147
Cdd:TIGR02875    4 RIVIADDNKEFCNLLKEYLAAQpdmEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKL-NEIELSARPrVI 82
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANL 1186
Cdd:TIGR02875   83 MLSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQL 121
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1072-1124 3.76e-14

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: 67.98  E-value: 3.76e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2796455230  1072 RILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMP 1124
Cdd:smart00448    2 RILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
808-1025 1.62e-13

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


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 74.73  E-value: 1.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  808 FFINTAHDIRTPLTLIKAPLEELREKEELSKEGISNMNTALRNVNALLRLTTNLINFERADVYSSELYISEHELNTFMNE 887
Cdd:TIGR01386  244 FSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELAK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  888 IFNAFQQYANIKHINFTYESNFRymnVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPAN 967
Cdd:TIGR01386  324 VAEYFEPLAEERGVRIRVEGEGL---VRGDPQMFRRAISNLLSNALRHTPDGGTITVRIERRSDEVRVSVSNPGPGIPPE 400
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2796455230  968 EQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKLVRLHKGKINLSSiENQGSVIKITFP 1025
Cdd:TIGR01386  401 HLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRFP 457
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
1225-1320 3.43e-11

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 65.82  E-value: 3.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1225 NVKKNVEDNIDNPALTVDVLCSLMGMSRTSFYnklRALTDQapGD----YIRLIRLKRAVQLLKE--DTHSITEIAEMTG 1298
Cdd:PRK09685   201 KVVALIDQSIQEEILRPEWIAGELGISVRSLY---RLFAEQ--GLvvaqYIRNRRLDRCADDLRPaaDDEKITSIAYKWG 275
                           90       100
                   ....*....|....*....|..
gi 2796455230 1299 FSDAKYFREVFKKHYNVSPSQY 1320
Cdd:PRK09685   276 FSDSSHFSTAFKQRFGVSPGEY 297
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
20-1058 5.33e-65

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 239.12  E-value: 5.33e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230   20 YRYLGVEDGLSNRRVYCIQKDKTGYMWFLTHEGIDRYNGKEFKRYKLMDGDAEVNSLLNLNWLYIDQEGVLWeIGKKGKV 99
Cdd:COG3292     24 FRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNYIRALLEDSDGRLW-IGTDGGL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  100 FRYDQIHDCFSLVYKLPMESfseqPDPVTYAWLDQNKHIWLCNKDTIFLYNTDTKQVTHIKNDiseeitdieqideshff 179
Cdd:COG3292    103 SRYDPKTDKFTRYPLDPGLP----NNSIRSIAEDSDGNIWVGTSNGLYRYDPKTGKFKRFTLD----------------- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  180 igtemgihyaQLENNAlklincdklesvkaqVSDLHFDKKiRKLFIGtflrgimvydmntksvirpdynlkdisitrfkp 259
Cdd:COG3292    162 ----------GLPSNT---------------ITSLAEDAD-GNLWVD--------------------------------- 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  260 lNDKELLIATDGGGVHKINMDTYQIVPeIVADYNSNcGMNGNSINDIFVDDEERIWLANYPIGITIQNNRYTSYKWIKHs 339
Cdd:COG3292    183 -SDGNLWIGTDGNGLYRLDPNTGKFEH-ITHDPDPN-SLSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRH- 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  340 iGNKQSLINDQVNAIIEDREGDLWFatnngisffnsktgqwrsvlsafeesqgnkshiflticevapgIIWAGGYSSGAY 419
Cdd:COG3292    259 -NDPNGLSGNSVRSIAEDSDGNLWI-------------------------------------------RLWIGTYGGGLF 294
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  420 QIDKKTFSVSYFMPplythtNKRPDKYIRDIRTDMQGYIWSGGFYN-LKRINLKTQEVRFYDGLNS-----ITAIVEKDE 493
Cdd:COG3292    295 RLDPKTGKFKRYNP------NGLPSNSVYSILEDSDGNLWIGTSGGgLYRYDPKTGKFTKFSEDNGlsnnfIRSILEDSD 368
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  494 KSMWIGSATGLCLLDKESGKFERIKLPVE-----SNYIYSLYQAKNGSLYIATSGSGLLIYDINKKLFTHYHTENcALIS 568
Cdd:COG3292    369 GNLWVGTNGGLYRLDPKTGKFTNFTHDPDknglsSNYINSIFEDSDGRLWIGTDGGGLYRYDPKTGKFKHFTTKD-GLPS 447
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  569 NNIYTILSDADKDIimstesgLTSFYPNEKKFYNWTKDMGLMTTHFNALSGTLRKNNKFILGSSDGAVEFDKDMKLPRSY 648
Cdd:COG3292    448 NTIYSILEDDNGNL-------WNFNSASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLT 520
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  649 SSKMIFSDFKLFYQTIYpgdedspLKASINDTKVLKLKYNQNRFSLQVSSINYDYPSNILYSWRLEGFYDKWSKPGTENT 728
Cdd:COG3292    521 LLLLALLLLLSLLLLLL-------LLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLL 593
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  729 IRYTNLAPGKYTLRVRAISNEDKRIMLEERSMDIIIAQPFWLTFWAMLVYTAILCLIAIVLLRILILRKQRKVSDEKIHF 808
Cdd:COG3292    594 LLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAEL 673
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  809 FINTAHDIRTPLTLIKAPLEELREKEELSKEGISNmNTALRNVNALLRLTTNLINFERADVYSSELYISEHELNTFMNEI 888
Cdd:COG3292    674 ILELLLILLLLLLLLLLALLLLLLLLLALKLLLLL-LLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLL 752
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  889 FNAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANE 968
Cdd:COG3292    753 ANDIELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKID 832
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  969 QKKLFKLHFRGSNAINSKVTGSGIGL-MLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSKRFRKAHLATPSKQRIENT 1047
Cdd:COG3292    833 LLDILELILLELELGLLLGLLLLLLLeILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIE 912
                         1050
                   ....*....|.
gi 2796455230 1048 IDNVPPPSPEI 1058
Cdd:COG3292    913 LLLEEEVLLAL 923
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
739-1026 1.56e-53

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 190.89  E-value: 1.56e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  739 YTLRVRAISNEDKRIMLEERSMDIIIAQPFWLTFWAMLVYTAILCLIAIVLLRILILRKQRKVSDEKIHFFINTAHDIRT 818
Cdd:COG0642     44 LLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRT 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  819 PLTLIKAplEELREKEELSKEGISNMNTALRNVNALLRLTTNLINFERADVYSSELYISEHELNTFMNEIFNAFQQYANI 898
Cdd:COG0642    124 PLTAIRG--YLELLLEELDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEE 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  899 KHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFR 978
Cdd:COG0642    202 KGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFR 281
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2796455230  979 GSNAINSKvtGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPK 1026
Cdd:COG0642    282 TDPSRRGG--GTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPL 327
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
795-1028 1.70e-51

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 181.64  E-value: 1.70e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  795 LRKQRKVSDEKIHFFINTAHDIRTPLTLIKAPLEELREKEELSKEGISNM-NTALRNVNALLRLTTNLINFERADVYSSE 873
Cdd:COG2205      6 LEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEERRELlEIIRESAERLLRLIEDLLDLSRLESGKLS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  874 LYISEHELNTFMNEIFNAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSW 953
Cdd:COG2205     86 LELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARREGDGV 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796455230  954 SVEVRDTGIGIPANEQKKLFKLHFRGSNaiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDS 1028
Cdd:COG2205    166 RISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
797-1029 2.04e-49

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 180.90  E-value: 2.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  797 KQRKVSDEKIHFFINTAHDIRTPLTLIKAPLEELREKEELSKEGISN-MNTALRNVNALLRLTTNLINFERADVYSSELY 875
Cdd:COG5002    157 ELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEERREyLEIILEEAERLSRLVNDLLDLSRLESGELKLE 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  876 ISEHELNTFMNEIFNAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSV 955
Cdd:COG5002    237 KEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREEDDQVRI 316
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796455230  956 EVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSK 1029
Cdd:COG5002    317 SVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1071-1200 1.91e-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: 148.57  E-value: 1.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILL 1149
Cdd:COG0745      2 PRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPIIML 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRALLRSKFANL 1200
Cdd:COG0745     80 TARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDL 130
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1070-1181 6.95e-38

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: 140.04  E-value: 6.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1070 HRRILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVIL 1148
Cdd:COG3706      1 PARILVVDDDPTNRKLLRRLLEAAGYeVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPFNIGILKA 1181
Cdd:COG3706     81 LTALDDEEDRARALEAGADDYLTKPFDPEELLA 113
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1071-1194 5.73e-37

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 139.14  E-value: 5.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:COG3437      7 PTVLIVDDDPENLELLRQLLRTLGYdVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFL 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRALLR 1194
Cdd:COG3437     87 TALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQR 131
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1073-1189 1.00e-34

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: 128.98  E-value: 1.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTA 1151
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLAN 1189
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYILVN 118
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1069-1191 1.28e-34

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 128.81  E-value: 1.28e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1069 NHRRILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVI 1147
Cdd:COG0784      4 GGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPII 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRA 1191
Cdd:COG0784     84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1072-1174 3.43e-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: 126.84  E-value: 3.43e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLT 1150
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEGYeVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPF 1174
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1074-1173 4.79e-33

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 123.29  E-value: 4.79e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1074 LIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLTAL 1152
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREK--GSDIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 2796455230 1153 NNEKDILSGLQIGADEYVVKP 1173
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1073-1174 4.22e-30

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: 114.92  E-value: 4.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDN-DELRnYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLT 1150
Cdd:cd19920      1 ILIVDDVpDNLR-LLSELLRAAgYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLT 79
                           90       100
                   ....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPF 1174
Cdd:cd19920     80 ALTDTEDKVKGFELGAVDYITKPF 103
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
813-1026 1.42e-29

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: 123.15  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  813 AHDIRTPLT--------LIKAPLEELREKEELSKEGIsnmNTALRNVNALLRLTTNLINFERadvySSELYISEHELNTF 884
Cdd:COG5000    209 AHEIKNPLTpiqlsaerLRRKLADKLEEDREDLERAL---DTIIRQVDRLKRIVDEFLDFAR----LPEPQLEPVDLNEL 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  885 MNEIFNAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGI 964
Cdd:COG5000    282 LREVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDGRVRIEVSDNGPGI 361
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796455230  965 PANEQKKLFKLHFrgsnaiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPK 1026
Cdd:COG5000    362 PEEVLERIFEPFF------TTKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPL 417
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
917-1026 9.45e-29

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 111.59  E-value: 9.45e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230   917 DKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAiNSKVTGSGIGLML 996
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGLGLSI 80
                            90       100       110
                    ....*....|....*....|....*....|
gi 2796455230   997 VWKLVRLHKGKINLSSIENQGSVIKITFPK 1026
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITLPL 110
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1074-1173 1.19e-28

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: 110.78  E-value: 1.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1074 LIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLTAL 1152
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLREL--PPDIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 2796455230 1153 NNEKDILSGLQIGADEYVVKP 1173
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1071-1202 1.25e-28

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: 120.45  E-value: 1.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILL 1149
Cdd:COG2204      3 ARILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVILL 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRALLRSKFANLDL 1202
Cdd:COG2204     81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGL 133
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1074-1194 2.07e-28

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: 110.83  E-value: 2.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1074 LIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTAL 1152
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEgYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2796455230 1153 NNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:cd19937     81 GEEFDKVLGLELGADDYITKPFSPRELLARV------KAVLR 116
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1073-1181 1.67e-27

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: 108.01  E-value: 1.67e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILLTA 1151
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKA 1181
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLA 108
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
921-1024 2.47e-27

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: 107.30  E-value: 2.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAinSKVTGSGIGLMLVWKL 1000
Cdd:cd00075      1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKS--REGGGTGLGLAIVRRI 78
                           90       100
                   ....*....|....*....|....
gi 2796455230 1001 VRLHKGKINLSSIENQGSVIKITF 1024
Cdd:cd00075     79 VEAHGGRITVESEPGGGTTFTVTL 102
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1074-1194 1.12e-26

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: 105.77  E-value: 1.12e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1074 LIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAI-KNNIETshiPVILLTA 1151
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLrEEGIET---PVLLLTA 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:cd17625     78 LDAVEDRVKGLDLGADDYLPKPFSLAELLARI------RALLR 114
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1071-1187 1.14e-26

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: 105.79  E-value: 1.14e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYFVQVC-SNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:cd17618      1 RTILIVEDEPAIREMIAFNLERAGFDVVEaEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLL 1187
Cdd:cd17618     81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
812-1028 2.08e-26

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 115.27  E-value: 2.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  812 TAHDIRTPL-------TLIKapleeLREKEELSKEGISNMNTALRNVNALLRLTTNLINFERADvySSELYISEHELNTF 884
Cdd:COG4251    289 ASHDLREPLrkisgfsQLLE-----EDYGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVG--RQELEFEPVDLNEL 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  885 MNEIFNAFQQYANIKHINFTYESNfryMNVWFDKEKMESIFKNIISNALKYTPEN--GNVQVFVSETSDSWSVEVRDTGI 962
Cdd:COG4251    362 LEEVLEDLEPRIEERGAEIEVGPL---PTVRGDPTLLRQVFQNLISNAIKYSRPGepPRIEIGAEREGGEWVFSVRDNGI 438
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796455230  963 GIPANEQKKLFKLHFRGSNaiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDS 1028
Cdd:COG4251    439 GIDPEYAEKIFEIFQRLHS--RDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAP 502
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1073-1173 8.37e-26

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: 102.52  E-value: 8.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLTA 1151
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLTEEgYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAA--GKQTPVLMLTA 78
                           90       100
                   ....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd19935     79 RDSVEDRVKGLDLGADDYLVKP 100
pleD PRK09581
response regulator PleD; Reviewed
1072-1196 3.64e-25

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 110.76  E-value: 3.64e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLT 1150
Cdd:PRK09581     4 RILVVDDIPANVKLLEAKLLAEYYtVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVT 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLRSK 1196
Cdd:PRK09581    84 ALDDPEDRVRGLEAGADDFLTKPINDVALFARV------KSLTRLK 123
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1072-1173 4.05e-25

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 101.00  E-value: 4.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQVC---SNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVIL 1148
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILEWEAGFEVVgeaENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE--LDPDTKIII 78
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKP 1173
Cdd:COG4753     79 LSGYSDFEYAQEAIKLGADDYLLKP 103
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1238-1326 1.58e-24

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 104.48  E-value: 1.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1238 ALTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSP 1317
Cdd:COG2207    168 LLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTP 247

                   ....*....
gi 2796455230 1318 SQYGKEKKA 1326
Cdd:COG2207    248 SEYRKRLRA 256
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1072-1195 1.62e-24

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 100.43  E-value: 1.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQVC---SNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVIL 1148
Cdd:COG4565      5 RVLIVEDDPMVAELLRRYLERLPGFEVVgvaSSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDVDVIV 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRALLRS 1195
Cdd:COG4565     83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1239-1320 2.33e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 98.01  E-value: 2.33e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  1239 LTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPS 1318
Cdd:smart00342    2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81

                    ..
gi 2796455230  1319 QY 1320
Cdd:smart00342   82 EY 83
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1073-1194 4.84e-24

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: 98.22  E-value: 4.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLS-EEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLTA 1151
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRfEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA--GNDLPILVLTA 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:cd17627     79 RDSVSDRVAGLDAGADDYLVKPFALEELLARV------RALLR 115
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1073-1194 5.55e-24

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: 97.94  E-value: 5.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLTA 1151
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQ--GQSLPVLILTA 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:cd17624     79 RDGVDDRVAGLDAGADDYLVKPFALEELLARL------RALLR 115
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
917-1027 1.49e-23

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: 96.67  E-value: 1.49e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSEtSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNainSKVTGSGIGLML 996
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEITVTLSE-GGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLSI 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2796455230  997 VWKLVRLHKGKINLSSIENQGSVIKITFPKD 1027
Cdd:pfam02518   78 VRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
924-1025 1.54e-23

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: 96.41  E-value: 1.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  924 IFKNIISNALKYTPEnGNVQVFVSETSDS-----WSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVW 998
Cdd:cd16922      4 ILLNLLGNAIKFTEE-GEVTLRVSLEEEEedgvqLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISK 82
                           90       100
                   ....*....|....*....|....*..
gi 2796455230  999 KLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16922     83 KLVELMGGDISVESEPGQGSTFTFTLP 109
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1071-1187 1.64e-23

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: 96.85  E-value: 1.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEE--YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVIL 1148
Cdd:cd17552      2 KRILVIDDEEDIREVVQACLEKLagWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVIL 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLL 1187
Cdd:cd17552     82 LTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
orf27 CHL00148
Ycf27; Reviewed
1065-1189 3.33e-23

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 100.18  E-value: 3.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1065 KENINHRRILIVEDNDELRNYLSQTLS-EEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNietSH 1143
Cdd:CHL00148     1 TMENSKEKILVVDDEAYIRKILETRLSiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE---SD 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2796455230 1144 IPVILLTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLAN 1189
Cdd:CHL00148    78 VPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRR 123
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1072-1194 6.32e-23

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 95.13  E-value: 6.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLT 1150
Cdd:cd19939      1 RILIVEDELELARLTRDYLIKAGLeVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR---EHSHVPILMLT 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:cd19939     78 ARTEEMDRVLGLEMGADDYLCKPFSPRELLARV------RALLR 115
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
813-1029 1.60e-22

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 103.89  E-value: 1.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  813 AHDIRTPLTLIKAPLEELREKEELSKEGISnMNTALRNVNALLRLTTNLINFERAdvysSELYISEHELNTFMNEIFNAF 892
Cdd:PRK11360   398 AHEIRNPLTAIRGYVQIWRQQTSDPPSQEY-LSVVLREVDRLNKVIDQLLEFSRP----RESQWQPVSLNALVEEVLQLF 472
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  893 QQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFV-SETSDSWSVEVRDTGIGIPANEQKK 971
Cdd:PRK11360   473 QTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTwQYSDGQVAVSIEDNGCGIDPELLKK 552
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2796455230  972 LFKLHFrgsnaiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSK 1029
Cdd:PRK11360   553 IFDPFF------TTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQ 604
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1073-1186 1.64e-22

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: 94.03  E-value: 1.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNnieTSHIPVILLTA 1151
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEgYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRK---TSNVPIIMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANV-ANL 1186
Cdd:cd17614     78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVkANL 113
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1073-1194 2.66e-22

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: 93.14  E-value: 2.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLTA 1151
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFnVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR---KTSQVPVLMLTA 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:cd17623     78 RGDDIDRILGLELGADDYLPKPFNPRELVARI------RAILR 114
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
1230-1320 3.53e-22

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: 99.08  E-value: 3.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1230 VEDNIDNPaLTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVF 1309
Cdd:COG4977    219 MEANLEEP-LSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAF 297
                           90
                   ....*....|.
gi 2796455230 1310 KKHYNVSPSQY 1320
Cdd:COG4977    298 RRRFGVSPSAY 308
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
927-1181 5.33e-22

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 103.10  E-value: 5.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  927 NIISNALKYTPEnGNVQVFVS-ETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSK-VTGSGIGLMLVWKLVRLH 1004
Cdd:PRK11091   405 NLISNAVKFTQQ-GGVTVRVRyEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKpATGTGIGLAVSKRLAQAM 483
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1005 KGKINLSSIENQGSVIKITFPKdskrfrkahlatpskqrientidnvpPPSPEIYENAQKKENINHR--RILIVEDnDEL 1082
Cdd:PRK11091   484 GGDITVTSEEGKGSCFTLTIHA--------------------------PAVAEEVEDAFDEDDMPLPalNILLVED-IEL 536
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1083 -----RNYLSQTLSEeyfVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHI-PVILLTAlNNEK 1156
Cdd:PRK11091   537 nvivaRSVLEKLGNS---VDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTA-NVLK 612
                          250       260
                   ....*....|....*....|....*
gi 2796455230 1157 DILSGLQIGADEYVVKPFNIGILKA 1181
Cdd:PRK11091   613 DKKEYLDAGMDDVLSKPLSVPALTA 637
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1072-1183 7.60e-22

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: 92.15  E-value: 7.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLT 1150
Cdd:cd17626      2 RILVVDDDAALAEMIGIVLRGEGFdPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR---AESGVPIVMLT 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANV 1183
Cdd:cd17626     79 AKSDTVDVVLGLESGADDYVAKPFKPKELVARI 111
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
812-1034 7.96e-22

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: 100.82  E-value: 7.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  812 TAHDIRTPLTLIKAplEELREKEELSKEG-------ISNMNTALRNVNALLRLTTN-LINFERADvysselyiseheLNT 883
Cdd:COG5809    277 IAHEIRNPLTSLKG--FIQLLKDTIDEEQktyldimLSELDRIESIISEFLVLAKPqAIKYEPKD------------LNT 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  884 FMNEIFNAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSW-SVEVRDTGI 962
Cdd:COG5809    343 LIEEVIPLLQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIETKAEDDDKvVISVTDEGC 422
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796455230  963 GIPANEQKKLFKLHFrgsnaiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSKRFRKA 1034
Cdd:COG5809    423 GIPEERLKKLGEPFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
HTH_18 pfam12833
Helix-turn-helix domain;
1244-1320 1.20e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 90.34  E-value: 1.20e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796455230 1244 LCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDT-HSITEIAEMTGFSDAKYFREVFKKHYNVSPSQY 1320
Cdd:pfam12833    1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEY 78
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
805-1208 1.94e-21

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 101.73  E-value: 1.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  805 KIHFFINTAHDIRTPLTLIKAPLEELREKEELSKEGISNMNTALRNVNALLRLTTNLINFERADVYSSELYISEHELNTF 884
Cdd:PRK09959   712 KSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTL 791
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  885 MNEIFNAFQQYANIKHINFTYESNF--RYMnVWFDKEKMESIFKNIISNALKYTPEnGNVQVFVS--ETSDSWSV---EV 957
Cdd:PRK09959   792 VQNTCHSFGAIAASKSIALSCSSTFpdHYL-VKIDPQAFKQVLSNLLSNALKFTTE-GAVKITTSlgHIDDNHAVikmTI 869
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  958 RDTGIGIPANEQKKLFKLHFRGSNAinSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSKRfRKAHLA 1037
Cdd:PRK09959   870 MDSGSGLSQEEQQQLFKRYSQTSAG--RQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQ-QVATVE 946
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1038 TPSKQrientidnvPPPSPEiyenaqkkeninHRRILIVEDNDELRNYLSQTLS-EEYFVQVCSNGKEALTIIPEYKPEL 1116
Cdd:PRK09959   947 AKAEQ---------PITLPE------------KLSILIADDHPTNRLLLKRQLNlLGYDVDEATDGVQALHKVSMQHYDL 1005
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1117 VISDIMMPEMRGDELCQAIKNniETSHIPVILLTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANlLANRALLRSK 1196
Cdd:PRK09959  1006 LITDVNMPNMDGFELTRKLRE--QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQ-LHQVAHIAPQ 1082
                          410
                   ....*....|..
gi 2796455230 1197 FANLDLNDEEND 1208
Cdd:PRK09959  1083 YRHLDIEALKNN 1094
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1072-1174 3.06e-21

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: 90.13  E-value: 3.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDE----LRNYLSQtlsEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVI 1147
Cdd:cd19938      1 RILIVEDEPKlaqlLIDYLRA---AGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR---RFSDVPII 74
                           90       100
                   ....*....|....*....|....*..
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVKPF 1174
Cdd:cd19938     75 MVTARVEEIDRLLGLELGADDYICKPY 101
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1072-1194 3.68e-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: 90.10  E-value: 3.68e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILLT 1150
Cdd:cd17615      1 RVLVVDDEPNITELLSMALRYEGWdVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFLT 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNigiLKANVANLlanRALLR 1194
Cdd:cd17615     79 AKDSVEDRIAGLTAGGDDYVTKPFS---LEEVVARL---RALLR 116
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1073-1175 5.42e-21

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: 89.44  E-value: 5.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTA 1151
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                           90       100
                   ....*....|....*....|....
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFN 1175
Cdd:cd17580     81 YGQPEDRERALEAGFDAHLVKPVD 104
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1071-1186 6.11e-21

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: 89.20  E-value: 6.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILL 1149
Cdd:cd17554      1 KKILVVDDEENIRELYKEELEDEgYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIIC 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2796455230 1150 TALNNEKDILSGLqiGADEYVVKPFNIGILKANVANL 1186
Cdd:cd17554     79 TAYSEYKSDFSSW--AADAYVVKSSDLTELKETIKRL 113
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1072-1194 4.92e-20

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: 86.66  E-value: 4.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLT 1150
Cdd:cd17622      2 RILLVEDDPKLARLIADFLESHGFnVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLR---PKYQGPILLLT 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:cd17622     79 ALDSDIDHILGLELGADDYVVKPVEPAVLLARL------RALLR 116
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1073-1173 7.86e-20

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: 85.89  E-value: 7.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTA 1151
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLEDQGFtVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                           90       100
                   ....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd19927     81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1073-1181 1.37e-19

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: 85.60  E-value: 1.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAI-KNNIETSHIPVILLT 1150
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYeVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIrELEGGGRRTPIIALT 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKA 1181
Cdd:cd17546     81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKE 111
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1072-1176 1.64e-19

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: 85.93  E-value: 1.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSE---EYFVQVCSNGKEALTII-------PEYKPELVISDIMMPEMRGDELCQAIKNNIET 1141
Cdd:cd17557      1 TILLVEDNPGDAELIQEAFKEagvPNELHVVRDGEEALDFLrgegeyaDAPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2796455230 1142 SHIPVILLTALNNEKDILSGLQIGADEYVVKPFNI 1176
Cdd:cd17557     81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDF 115
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1072-1194 1.90e-19

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 88.87  E-value: 1.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLT 1150
Cdd:PRK11083     5 TILLVEDEQAIADTLVYALQSEGFtVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAF--HPALPVIFLT 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:PRK11083    83 ARSDEVDRLVGLEIGADDYVAKPFSPREVAARV------RTILR 120
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1072-1184 4.37e-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: 84.13  E-value: 4.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLT 1150
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLeSAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2796455230 1151 AL----NNEKdILSGlqiGADEYVVKPFNIGILKANVA 1184
Cdd:cd17548     81 AYamkgDREK-ILEA---GCDGYISKPIDTREFLETVA 114
PRK11517 PRK11517
DNA-binding response regulator HprR;
1072-1208 8.63e-19

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 86.88  E-value: 8.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETshiPVILLT 1150
Cdd:PRK11517     2 KILLIEDNQRTQEWVTQGLSEAgYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT---PVICLT 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLRSK---FANLDLNDEEND 1208
Cdd:PRK11517    79 ARDSVDDRVRGLDSGANDYLVKPFSFSELLARV------RAQLRQHhalNSTLEISGLRMD 133
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1072-1181 1.09e-18

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: 83.16  E-value: 1.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF--VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:cd19923      2 KVLVVDDFSTMRRIIKNLLKELGFnnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKA 1181
Cdd:cd19923     82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKE 113
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1073-1176 1.24e-18

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 83.16  E-value: 1.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYF----VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVIL 1148
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIDWEELgfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRE--LYPDIKIII 78
                           90       100
                   ....*....|....*....|....*....
gi 2796455230 1149 LTALnNEKDIL-SGLQIGADEYVVKPFNI 1176
Cdd:cd17536     79 LSGY-DDFEYAqKAIRLGVVDYLLKPVDE 106
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
1073-1173 1.53e-18

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: 81.86  E-value: 1.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLTA 1151
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFeVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1073-1194 1.93e-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: 82.33  E-value: 1.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETshIPVILLTA 1151
Cdd:cd19934      1 LLLVEDDALLAAQLKEQLSDAgYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--TPVLILTA 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:cd19934     79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARL------RALIR 115
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1073-1173 3.08e-18

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: 80.95  E-value: 3.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLTA 1151
Cdd:cd19936      1 IALVDDDRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR---QKSTLPVIFLTS 77
                           90       100
                   ....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd19936     78 KDDEIDEVFGLRMGADDYITKP 99
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
921-1026 3.09e-18

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: 81.22  E-value: 3.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYTPENgnVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKL 1000
Cdd:cd16949      1 LARALENVLRNALRYSPSK--ILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERA 78
                           90       100
                   ....*....|....*....|....*.
gi 2796455230 1001 VRLHKGKINLSSIENQGSVIKITFPK 1026
Cdd:cd16949     79 IEQHGGKIKASNRKPGGLRVRIWLPA 104
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
813-1025 3.80e-18

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 87.98  E-value: 3.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  813 AHDIRTPLTLIK--APLEELREKEELSKEGISNMNTALRNVNallRLTTNLINFERadvySSELYISEHELNTFMNEIFN 890
Cdd:COG3852    143 AHEIRNPLTGIRgaAQLLERELPDDELREYTQLIIEEADRLN---NLVDRLLSFSR----PRPPEREPVNLHEVLERVLE 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  891 AFQQYANiKHINFTYEsnfrYM----NVWFDKEKMESIFKNIISNALKYTPENGNVQV----------FVSETSDSWSVE 956
Cdd:COG3852    216 LLRAEAP-KNIRIVRD----YDpslpEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIrtrverqvtlGGLRPRLYVRIE 290
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796455230  957 VRDTGIGIPANEQKKLFKLHFRGsnainsKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:COG3852    291 VIDNGPGIPEEILDRIFEPFFTT------KEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLP 353
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1072-1186 6.07e-18

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: 80.95  E-value: 6.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQV--CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:cd17551      2 RILIVDDNPTNLLLLEALLRSAGYLEVvsFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2796455230 1150 TAlNNEKDI-LSGLQIGADEYVVKPFNIGILKANVANL 1186
Cdd:cd17551     82 TA-DTDREVrLRALEAGATDFLTKPFDPVELLARVRNL 118
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1071-1183 7.41e-18

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 80.53  E-value: 7.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYF--VQVCSNGKEALTIIPEYKPELVISDIMMP-EMRGDELCQAIKNNietSHIPVI 1147
Cdd:cd17534      1 KKILIVEDEAIIALDLKEILESLGYevVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK---FDIPVI 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVKPFNIGILKANV 1183
Cdd:cd17534     78 FLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1072-1175 8.26e-18

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: 80.51  E-value: 8.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLT 1150
Cdd:cd17619      2 HILIVEDEPVTRATLKSYFEQEgYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR---EQSEVGIILVT 78
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFN 1175
Cdd:cd17619     79 GRDDEVDRIVGLEIGADDYVTKPFN 103
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1072-1192 9.01e-18

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: 80.39  E-value: 9.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnnIETSHIPVILLT 1150
Cdd:cd19919      2 TVWIVDDDSSIRWVLERALAGAGLtVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIK--QRHPDLPVIIMT 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIgilkaNVANLLANRAL 1192
Cdd:cd19919     80 AHSDLDSAVSAYQGGAFEYLPKPFDI-----DEAVALVERAI 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1073-1173 9.53e-18

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 79.52  E-value: 9.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLTA 1151
Cdd:cd17620      1 ILVIEDEPQIRRFLRTALEAHgYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSA 77
                           90       100
                   ....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd17620     78 RDEESDKIAALDAGADDYLTKP 99
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
924-1025 1.10e-17

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: 79.68  E-value: 1.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  924 IFKNIISNALKYT--PENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLF----KLHFRGSNAinskvtGSGIGLMLV 997
Cdd:cd16921      4 VLTNLLGNAIKFRrpRRPPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFgifqRLHSREEYE------GTGVGLAIV 77
                           90       100
                   ....*....|....*....|....*...
gi 2796455230  998 WKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16921     78 RKIIERHGGRIWLESEPGEGTTFYFTLP 105
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
1072-1186 2.11e-17

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: 83.69  E-value: 2.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEE---YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIkNNIETSHIP-VI 1147
Cdd:TIGR02875    4 RIVIADDNKEFCNLLKEYLAAQpdmEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKL-NEIELSARPrVI 82
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANL 1186
Cdd:TIGR02875   83 MLSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQL 121
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1071-1174 2.49e-17

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 79.24  E-value: 2.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYFVQV--CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVIL 1148
Cdd:cd17542      1 KKVLIVDDAAFMRMMLKDILTKAGYEVVgeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKK--IDPNAKVIM 78
                           90       100
                   ....*....|....*....|....*.
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPF 1174
Cdd:cd17542     79 CSAMGQEEMVKEAIKAGAKDFIVKPF 104
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1072-1194 2.89e-17

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 82.54  E-value: 2.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEyKPELVISDIMMPEMRGDELCQAIKNNIETshiPVILLT 1150
Cdd:PRK10955     3 KILLVDDDRELTSLLKELLEMEGFnVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTHQT---PVIMLT 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:PRK10955    79 ARGSELDRVLGLELGADDYLPKPFNDRELVARI------RAILR 116
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1071-1195 3.02e-17

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: 81.54  E-value: 3.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYF--VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIknnIETSHIPVIL 1148
Cdd:COG3707      4 LRVLVVDDEPLRRADLREGLREAGYevVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQI---SEERPAPVIL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRALLRS 1195
Cdd:COG3707     81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRA 127
PRK09303 PRK09303
histidine kinase;
913-1025 3.04e-17

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 85.39  E-value: 3.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  913 NVWFDKEKMESIFKNIISNALKYTPENGNVQVFV-SETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNaiNSKVTGSG 991
Cdd:PRK09303   265 SVYADQERIRQVLLNLLDNAIKYTPEGGTITLSMlHRTTQKVQVSICDTGPGIPEEEQERIFEDRVRLPR--DEGTEGYG 342
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2796455230  992 IGLMLVWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:PRK09303   343 IGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLP 376
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1073-1187 3.89e-17

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: 78.48  E-value: 3.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSE-EYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNnieTSHIPVILLTA 1151
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFISS 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVANLL 1187
Cdd:cd18159     78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1071-1192 4.42e-17

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 85.67  E-value: 4.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYFVQVC-SNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILL 1149
Cdd:PRK11361     5 NRILIVDDEDNVRRMLSTAFALQGFETHCaNNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRS--HETRTPVILM 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILkanvaNLLANRAL 1192
Cdd:PRK11361    83 TAYAEVETAVEALRCGAFDYVIKPFDLDEL-----NLIVQRAL 120
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1073-1172 4.94e-17

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: 78.32  E-value: 4.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDN----DELRNYLSQTLSEEyFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVIL 1148
Cdd:cd17535      1 VLIVDDHplvrEGLRRLLESEPDIE-VVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIV 77
                           90       100
                   ....*....|....*....|....
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVK 1172
Cdd:cd17535     78 LTAHDDPEYVLRALKAGAAGYLLK 101
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
924-1220 6.70e-17

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 86.44  E-value: 6.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  924 IFKNIISNALKYTpENGNVQVFVSETSDSWS-----VEVRDTGIGIPANEQKKLFKLhFRGSNA-INSKVTGSGIGLMLV 997
Cdd:PRK11107   412 IITNLVGNAIKFT-ESGNIDILVELRALSNTkvqleVQIRDTGIGISERQQSQLFQA-FRQADAsISRRHGGTGLGLVIT 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  998 WKLVRLHKGKINLSSIENQGSVIKITFPKD-------------------------------------------------- 1027
Cdd:PRK11107   490 QKLVNEMGGDISFHSQPNRGSTFWFHLPLDlnpnpiidglptdclagkrllyvepnsaaaqatldilsetplevtysptl 569
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1028 --------------------------SKRFRKA-------HLATPS---------KQR---------------IENTIDN 1050
Cdd:PRK11107   570 sqlpeahydilllglpvtfrepltmlHERLAKAksmtdflILALPCheqvlaeqlKQDgadaclskplshtrlLPALLEP 649
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1051 VP-PPSPEIYENAQKKENINhrrILIVEDND-ELRnyLSQTLSEEYFVQV--CSNGKEALTIIPEYKPELVISDIMMPEM 1126
Cdd:PRK11107   650 CHhKQPPLLPPTDESRLPLT---VMAVDDNPaNLK--LIGALLEEQVEHVvlCDSGHQAVEQAKQRPFDLILMDIQMPGM 724
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1127 RGDELCQAIKNNIETSHIPVILLTA--LNNEKDILsgLQIGADEYVVKPFNIGILKAnvanlLANRALLRSKFANLDLND 1204
Cdd:PRK11107   725 DGIRACELIRQLPHNQNTPIIAVTAhaMAGERERL--LSAGMDDYLAKPIDEAMLKQ-----VLLRYKPGPKFTSRVVAP 797
                          410
                   ....*....|....*.
gi 2796455230 1205 EENDEDCiNCSQDIDW 1220
Cdd:PRK11107   798 EPPEPVH-FPNATLDW 812
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
813-1030 6.95e-17

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 85.22  E-value: 6.95e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  813 AHDIRTPLTLIKAPLEELREKEELSKEGISNMNTALRNVNALLRLTTNLINFeradVYSSELYISEHELNTFMNEIFNAF 892
Cdd:PRK10364   245 AHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLEL----VKPTHLALQAVDLNDLINHSLQLV 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  893 QQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKL 972
Cdd:PRK10364   321 SQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEAI 400
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2796455230  973 FKLHFrgsnaiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSKR 1030
Cdd:PRK10364   401 FTPYF------TTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNITR 452
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1072-1174 1.22e-16

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 80.88  E-value: 1.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLT 1150
Cdd:PRK10710    12 RILIVEDEPKLGQLLIDYLqAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR---RFSDIPIVMVT 88
                           90       100
                   ....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPF 1174
Cdd:PRK10710    89 AKIEEIDRLLGLEIGADDYICKPY 112
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
917-1025 1.42e-16

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: 76.76  E-value: 1.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSET-SDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLM 995
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFrLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLS 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2796455230  996 LVWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16925     81 IVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
1073-1192 1.63e-16

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 77.14  E-value: 1.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLS-EEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLTA 1151
Cdd:cd17549      1 VLLVDDDADVREALQQTLElAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIREL--DPDLPVILITG 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2796455230 1152 lnnEKDI---LSGLQIGADEYVVKPFNIGILKANVANLLANRAL 1192
Cdd:cd17549     79 ---HGDVpmaVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRL 119
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
882-1029 1.95e-16

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 82.97  E-value: 1.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  882 NTFMNEIFNAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNAL----KYTPENGNVQVFVSETSDSWSVEV 957
Cdd:COG3290    243 NPVLAALLLGKAARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIeaveKLPEEERRVELSIRDDGDELVIEV 322
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796455230  958 RDTGIGIPANEQKKLFKLHFRgsnainSKV-TGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSK 1029
Cdd:COG3290    323 EDSGPGIPEELLEKIFERGFS------TKLgEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
PRK15479 PRK15479
transcriptional regulator TctD;
1072-1205 2.17e-16

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 79.77  E-value: 2.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETshIPVILLT 1150
Cdd:PRK15479     2 RLLLAEDNRELAHWLEKALVQNGFaVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQT--LPVLLLT 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR---------SKFANLDLNDE 1205
Cdd:PRK15479    80 ARSAVADRVKGLNVGADDYLPKPFELEELDARL------RALLRrsagqvqevQQLGELIFHDE 137
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
917-1025 2.50e-16

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: 75.96  E-value: 2.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLML 996
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAI 80
                           90       100
                   ....*....|....*....|....*....
gi 2796455230  997 VWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16946     81 CHNIALAHGGTISAEHSPLGGLRLVLTLP 109
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
1072-1174 2.96e-16

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: 75.72  E-value: 2.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEE---YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVIL 1148
Cdd:cd17561      3 KVLIADDNREFVQLLEEYLNSQpdmEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIM 82
                           90       100
                   ....*....|....*....|....*.
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPF 1174
Cdd:cd17561     83 LTAFGQEDITQRAVELGASYYILKPF 108
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1073-1192 3.33e-16

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: 76.08  E-value: 3.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELR----NYLSQtlsEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAI-KNNIETshiPVI 1147
Cdd:cd17572      1 VLLVEDSPSLAalyqEYLSD---EGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIqERSLPT---SVI 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2796455230 1148 LLTAlNNEKDI-LSGLQIGADEYVVKPFNIGILKANVANLLANRAL 1192
Cdd:cd17572     75 VITA-HGSVDIaVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKL 119
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
914-1024 5.69e-16

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: 75.13  E-value: 5.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  914 VWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSwSVEVRDTGIGIPANEQKKLFKLHFR--GSNAinskvTGSG 991
Cdd:cd16940      7 VQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGA-VIRVEDNGPGIDEEELEALFERFYRsdGQNY-----GGSG 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230  992 IGLMLVWKLVRLHKGKINLSSIENQGSVIKITF 1024
Cdd:cd16940     81 LGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
813-1025 1.08e-15

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 80.23  E-value: 1.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  813 AHDIRTPLTLIKA---PLEELREKEELSKEGISNMNTALRNVNALLRLTTNLINFERADvyssELYISEHELNTFMNEIF 889
Cdd:COG4191    150 AHEINNPLAAILGnaeLLRRRLEDEPDPEELREALERILEGAERAAEIVRSLRAFSRRD----EEEREPVDLNELIDEAL 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  890 NAFQQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPE--NGNVQVFVSETSDSWSVEVRDTGIGIPAN 967
Cdd:COG4191    226 ELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEgeGGRITISTRREGDYVVISVRDNGPGIPPE 305
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796455230  968 EQKKLFKLHFrgsnainskvT------GSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:COG4191    306 VLERIFEPFF----------TtkpvgkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
PRK15347 PRK15347
two component system sensor kinase;
814-1212 1.32e-15

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 82.38  E-value: 1.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  814 HDIRTPLT-LIKAPLEELREKEELSKEGIsnMNTALRNVNALLRLTTNLINFERADVYSSELYISEHELNTFMNEIFNAF 892
Cdd:PRK15347   407 HEIRTPLNgVLGALELLQNTPLTAEQMDL--ADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTI 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  893 QQYANIKHINFtyeSNFRYMNV----WFDKEKMESIFKNIISNALKYTpENGNVQVFVSETSDSWSVEVRDTGIGIPANE 968
Cdd:PRK15347   485 QGPAQSKSLTL---RTFVGAHVplylHLDSLRLRQILVNLLGNAVKFT-ETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQ 560
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  969 QKKLFKLHFRGSnaINSKvtGSGIGLMLVWKLVRLHKGKINLSSIENQGS-------VIKITFPKDSKrfrkAHLATPS- 1040
Cdd:PRK15347   561 QQQIFTPFYQAD--THSQ--GTGLGLTIASSLAKMMGGELTLFSTPGVGScfslvlpLNEYAPPEPLK----GELSAPLa 632
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1041 --KQ------RIENTIDNVPPPSPEI-------YENAQK---------KENIN----HRRILIVEDNDELRNYLSQTLSE 1092
Cdd:PRK15347   633 lhRQlsawgiTCQPGHQNPALLDPELaylpgrlYDLLQQiiqgapnepVINLPlqpwQLQILLVDDVETNRDIIGMMLVE 712
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1093 E-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKN--NIETSHIPVILLTALNNEKDILSGLQIGADEY 1169
Cdd:PRK15347   713 LgQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDdpNNLDPDCMIVALTANAAPEEIHRCKKAGMNHY 792
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2796455230 1170 VVKPFNIGILkANVANLLANRALLRskfaNLDLndEENDEDCI 1212
Cdd:PRK15347   793 LTKPVTLAQL-ARALELAAEYQLLR----GIEL--SPQDSSCS 828
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1073-1173 1.87e-15

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: 73.57  E-value: 1.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPE---------LVISDIMMPEMRGDELCQAIKNNIETS 1142
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFeIAEAVDGEEALNKLENLAKEgndlskeldLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2796455230 1143 HIPVILLTALNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1072-1202 2.22e-15

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 76.89  E-value: 2.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFV-QVCSNGKEA--LTIIPEYkpELVISDIMMPEMRGDELCQAIKNniETSHIPVIL 1148
Cdd:PRK09836     2 KLLIVEDEKKTGEYLTKGLTEAGFVvDLADNGLNGyhLAMTGDY--DLIILDIMLPDVNGWDIVRMLRS--ANKGMPILL 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLL--ANRALLRSKFANLDL 1202
Cdd:PRK09836    78 LTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLrrGAAVIIESQFQVADL 133
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
917-1025 5.70e-15

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: 72.32  E-value: 5.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKvTGSGIGLML 996
Cdd:cd16948      2 DAKWLSFIIGQIVSNALKYSKQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGRNFQ-ESTGMGLYL 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2796455230  997 VWKLV-RLHKgKINLSSIENQGSVIKITFP 1025
Cdd:cd16948     81 VKKLCdKLGH-KIDVESEVGEGTTFTITFP 109
ompR PRK09468
osmolarity response regulator; Provisional
1069-1194 6.15e-15

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 75.78  E-value: 6.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1069 NHRRILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVI 1147
Cdd:PRK09468     4 ENYKILVVDDDMRLRALLERYLTEQGFqVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQ--NNPTPII 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:PRK09468    82 MLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARI------RAVLR 122
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1071-1187 6.31e-15

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 72.33  E-value: 6.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:cd17562      1 KKILAVDDSASIRQMVSFTLRGAgYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLL 1187
Cdd:cd17562     81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1072-1175 8.07e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 75.24  E-value: 8.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQV---CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVIL 1148
Cdd:COG3279      3 KILIVDDEPLARERLERLLEKYPDLEVvgeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLREL--DPPPPIIF 80
                           90       100
                   ....*....|....*....|....*..
gi 2796455230 1149 LTAlnNEKDILSGLQIGADEYVVKPFN 1175
Cdd:COG3279     81 TTA--YDEYALEAFEVNAVDYLLKPID 105
PRK10643 PRK10643
two-component system response regulator PmrA;
1072-1194 1.42e-14

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 74.30  E-value: 1.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETshIPVILLT 1150
Cdd:PRK10643     2 KILIVEDDTLLLQGLILALQTEgYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYT--LPVLILT 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVanllanRALLR 1194
Cdd:PRK10643    80 ARDTLEDRVAGLDVGADDYLVKPFALEELHARI------RALIR 117
PRK11173 PRK11173
two-component response regulator; Provisional
1072-1187 2.14e-14

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 74.28  E-value: 2.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLT 1150
Cdd:PRK11173     5 HILIVEDELVTRNTLKSIFeAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR---EQANVALMFLT 81
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLL 1187
Cdd:PRK11173    82 GRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLL 118
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1072-1173 3.68e-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: 69.92  E-value: 3.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILLT 1150
Cdd:cd17555      2 TILVIDDDEVVRESIAAYLEDSGFqVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITK--ESPDTPVIVVS 79
                           90       100
                   ....*....|....*....|...
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd17555     80 GAGVMSDAVEALRLGAWDYLTKP 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1072-1124 3.76e-14

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: 67.98  E-value: 3.76e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2796455230  1072 RILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMP 1124
Cdd:smart00448    2 RILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
813-1026 4.37e-14

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: 76.69  E-value: 4.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  813 AHDIRTPLTLIKAPLEELREKEELSKEGISNMNTALRNVNALLrltTNLINFERADVYSSElyisEHELNTFMNEIFNAF 892
Cdd:COG5805    295 AHEIRNPLTSIKGFLQLLQPGIEDKEEYFDIMLSELDRIESII---SEFLALAKPQAVNKE----KENINELIQDVVTLL 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  893 QQYANIKHINFTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKL 972
Cdd:COG5805    368 ETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLKKL 447
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2796455230  973 FKLHFrgsnaiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPK 1026
Cdd:COG5805    448 GEPFF------TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
PRK10610 PRK10610
chemotaxis protein CheY;
1072-1180 5.20e-14

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 70.00  E-value: 5.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF--VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:PRK10610     7 KFLVVDDFSTMRRIVRNLLKELGFnnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILK 1180
Cdd:PRK10610    87 TAEAKKENIIAAAQAGASGYVVKPFTAATLE 117
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1073-1183 6.15e-14

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 72.53  E-value: 6.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVILLTA 1151
Cdd:PRK10529     4 VLIVEDEQAIRRFLRTALeGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR---QWSAIPVIVLSA 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANV 1183
Cdd:PRK10529    81 RSEESDKIAALDAGADDYLSKPFGIGELQARL 112
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1071-1187 1.25e-13

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 71.67  E-value: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYFVQV-CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:PRK10161     3 RRILVVEDEAPIREMVCFVLEQNGFQPVeAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVML 82
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLL 1187
Cdd:PRK10161    83 TARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
Y_Y_Y pfam07495
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ...
700-764 1.39e-13

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: 66.61  E-value: 1.39e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796455230  700 NYDYPSNILYSWRLEGFYDKWSKPGTENTIRYTNLAPGKYTLRVRAISNEDKRIMlEERSMDIII 764
Cdd:pfam07495    1 NYDGPENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSY-DDASLNFTI 64
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
921-1025 1.52e-13

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: 68.00  E-value: 1.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKL 1000
Cdd:cd16952      1 LRSAFSNLVSNAVKYTPPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHV 80
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1001 VRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16952     81 MSRHDARLLIASELGKGSRFTCLFP 105
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
808-1025 1.62e-13

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


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 74.73  E-value: 1.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  808 FFINTAHDIRTPLTLIKAPLEELREKEELSKEGISNMNTALRNVNALLRLTTNLINFERADVYSSELYISEHELNTFMNE 887
Cdd:TIGR01386  244 FSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELAK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  888 IFNAFQQYANIKHINFTYESNFRymnVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPAN 967
Cdd:TIGR01386  324 VAEYFEPLAEERGVRIRVEGEGL---VRGDPQMFRRAISNLLSNALRHTPDGGTITVRIERRSDEVRVSVSNPGPGIPPE 400
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2796455230  968 EQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKLVRLHKGKINLSSiENQGSVIKITFP 1025
Cdd:TIGR01386  401 HLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRFP 457
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
808-1012 2.23e-13

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 74.42  E-value: 2.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  808 FFINTAHDIRTPLTLIKAPLEELREKEELSKEGISNMNTALRNVNALLRLTTNLINFERADvySSELYISEHELNTF--M 885
Cdd:PRK09835   265 FSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQAD--NNQLIPEKKMLDLAdeV 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  886 NEIFNAFQQYANIKHInfTYESNFRYMNVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIP 965
Cdd:PRK09835   343 GKVFDFFEAWAEERGV--ELRFVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEAITVRCQEVDHQVQLVVENPGTPIA 420
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2796455230  966 ANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKLVRLHKGKINLSS 1012
Cdd:PRK09835   421 PEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTS 467
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1072-1173 2.41e-13

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 68.19  E-value: 2.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQVC---SNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVIL 1148
Cdd:cd17541      2 RVLIVDDSAVMRKLLSRILESDPDIEVVgtaRDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIM---AERPTPVVM 78
                           90       100
                   ....*....|....*....|....*..
gi 2796455230 1149 LTALNNE--KDILSGLQIGADEYVVKP 1173
Cdd:cd17541     79 VSSLTEEgaEITLEALELGAVDFIAKP 105
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1072-1175 3.28e-13

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: 67.54  E-value: 3.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFvQV--CSNGKEALTIIPEYkPE--LVISDIMMPEMRGDELCQAIKNNIETSHIPVI 1147
Cdd:cd17544      2 KVLVVDDSATSRNHLRALLRRHNF-QVleAANGQEALEVLEQH-PDikLVITDYNMPEMDGFELVREIRKKYSRDQLAII 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 2796455230 1148 LLTALNNEkdILSG--LQIGADEYVVKPFN 1175
Cdd:cd17544     80 GISASGDN--ALSArfIKAGANDFLTKPFL 107
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
919-1025 8.94e-13

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: 65.91  E-value: 8.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  919 EKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFrgsnaiNSKV--TGSGIGLML 996
Cdd:cd16943      2 SQLNQVLLNLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFF------TTKPvgEGTGLGLSL 75
                           90       100
                   ....*....|....*....|....*....
gi 2796455230  997 VWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16943     76 SYRIIQKHGGTIRVASVPGGGTRFTIILP 104
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1071-1176 9.73e-13

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: 66.28  E-value: 9.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYF--VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAI-KNNIetshIPVI 1147
Cdd:cd19932      1 VRVLIAEDEALIRMDLREMLEEAGYevVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIItSENI----APIV 76
                           90       100
                   ....*....|....*....|....*....
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVKPFNI 1176
Cdd:cd19932     77 LLTAYSQQDLVERAKEAGAMAYLVKPFSE 105
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
921-1025 1.01e-12

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: 65.49  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKvtGSGIGLMLVWKL 1000
Cdd:cd16923      1 LQRVFSNLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNTE--GAGLGLSIAKAI 78
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1001 VRLHKGKINLsSIENQGSVIKITFP 1025
Cdd:cd16923     79 IELHGGSASA-EYDDNHDLFKVRLP 102
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
917-1024 1.36e-12

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


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 65.18  E-value: 1.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKvTGSGIGLML 996
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GHYGMGLYI 79
                           90       100
                   ....*....|....*....|....*...
gi 2796455230  997 VWKLVRLHKGKINLSSIENQGSVIKITF 1024
Cdd:cd16975     80 AKNLVEKHGGSLIIENSQKGGAEVTVKI 107
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1072-1188 2.02e-12

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: 65.12  E-value: 2.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLS-EEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILLT 1150
Cdd:cd17569      2 TILLVDDEPNILKALKRLLRrEGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRE--RYPDTVRILLT 79
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2796455230 1151 ALNNEKDILSGLQIGA-DEYVVKPFNIGILKANVANLLA 1188
Cdd:cd17569     80 GYADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1073-1183 2.35e-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: 64.78  E-value: 2.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNietSHIPVILLTA 1151
Cdd:cd17594      2 VLVVDDDAAMRHLLILYLRERgFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR---SDVPIIIISG 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230 1152 -LNNEKDILSGLQIGADEYVVKPFNIGILKANV 1183
Cdd:cd17594     79 dRRDEIDRVVGLELGADDYLAKPFGLRELLARV 111
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
917-1133 2.83e-12

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 71.47  E-value: 2.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTpENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSnainSKVTGSGIGLML 996
Cdd:PRK11466   558 DPRRIRQVITNLLSNALRFT-DEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVS----GKRGGTGLGLTI 632
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  997 VWKLVRLHKGKINLSSIENQGSVIKITFPkdskrFRKAHlatpskqrientidnvpPPSPEIYENAQkkeNINHRRILIV 1076
Cdd:PRK11466   633 SSRLAQAMGGELSATSTPEVGSCFCLRLP-----LRVAT-----------------APVPKTVNQAV---RLDGLRLLLI 687
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796455230 1077 EDNDelrnyLSQTLSEEYF------VQVCSNGKEALTIIPEYKP-ELVISDIMMPEMRGDELCQ 1133
Cdd:PRK11466   688 EDNP-----LTQRITAEMLntsgaqVVAVGNAAQALETLQNSEPfAAALVDFDLPDYDGITLAR 746
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1073-1181 3.98e-12

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 64.19  E-value: 3.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPE--LVISDIMMPEMRGDELCQAIKnniETSHIPVILL 1149
Cdd:cd17584      1 VLVVDDDPTCLAILKRMLLRCgYQVTTCTDAEEALSMLRENKDEfdLVITDVHMPDMDGFEFLELIR---LEMDLPVIMM 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKA 1181
Cdd:cd17584     78 SADGSTSTVMKGLAHGACDYLLKPVSIEDLKN 109
envZ PRK09467
osmolarity sensor protein; Provisional
814-1025 7.03e-12

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 69.17  E-value: 7.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  814 HDIRTPLTLIKAPLEELREKEELSKEGISN----MNTALRNVNALLRlTTNLINFERADvysselyiseheLNTFMNEIF 889
Cdd:PRK09467   238 HDLRTPLTRIRLATEMMSEEDGYLAESINKdieeCNAIIEQFIDYLR-TGQEMPMEMAD------------LNALLGEVI 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  890 NAFQQYANIKHINFTYESnfryMNVWFDKEKMESIFKNIISNALKYTpeNGNVQVFVSETSDSWSVEVRDTGIGIPANEQ 969
Cdd:PRK09467   305 AAESGYEREIETALQPGP----IEVPMNPIAIKRALANLVVNAARYG--NGWIKVSSGTEGKRAWFQVEDDGPGIPPEQL 378
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2796455230  970 KKLFKLHFRGSNAINSkvTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:PRK09467   379 KHLFQPFTRGDSARGS--SGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLP 432
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1072-1172 9.32e-12

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 65.82  E-value: 9.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQV---CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIpvIL 1148
Cdd:PRK10651     8 TILLIDDHPMLRTGVKQLISMAPDITVvgeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRI--VV 85
                           90       100
                   ....*....|....*....|....
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVK 1172
Cdd:PRK10651    86 FSVSNHEEDVVTALKRGADGYLLK 109
PRK10816 PRK10816
two-component system response regulator PhoP;
1072-1187 1.14e-11

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 65.92  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETshIPVILLT 1150
Cdd:PRK10816     2 RVLVVEDNALLRHHLKVQLQDAgHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVLT 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLL 1187
Cdd:PRK10816    80 ARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALM 116
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
808-1026 1.91e-11

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 67.73  E-value: 1.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  808 FFINTAHDIRTPLTLIKAPLEELREKEELS---KEGISNMNTALRNVNALLR--LTTNLINF-------ERADVySSELY 875
Cdd:PRK11006   207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGalrEKALHTMREQTQRMEGLVKqlLTLSKIEAaptidlnEKVDV-PMMLR 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  876 ISEHELNTFMNEifnafQQyanikHINFTYESNFRymnVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSV 955
Cdd:PRK11006   286 VLEREAQTLSQG-----KH-----TITFEVDNSLK---VFGNEDQLRSAISNLVYNAVNHTPEGTHITVRWQRVPQGAEF 352
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796455230  956 EVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPK 1026
Cdd:PRK11006   353 SVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPE 423
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1072-1135 2.73e-11

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: 62.22  E-value: 2.73e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQV---CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAI 1135
Cdd:COG2197      3 RVLIVDDHPLVREGLRALLEAEPDIEVvgeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1072-1174 3.40e-11

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 61.49  E-value: 3.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDN----DELRNYLSQTlseEYFVQV--CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIEtsHIP 1145
Cdd:cd19925      2 NVLIVEDDpmvaEIHRAYVEQV---PGFTVIgtAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGH--DVD 76
                           90       100
                   ....*....|....*....|....*....
gi 2796455230 1146 VILLTALNNEKDILSGLQIGADEYVVKPF 1174
Cdd:cd19925     77 VIVVTAANDVETVREALRLGVVDYLIKPF 105
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
1225-1320 3.43e-11

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 65.82  E-value: 3.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1225 NVKKNVEDNIDNPALTVDVLCSLMGMSRTSFYnklRALTDQapGD----YIRLIRLKRAVQLLKE--DTHSITEIAEMTG 1298
Cdd:PRK09685   201 KVVALIDQSIQEEILRPEWIAGELGISVRSLY---RLFAEQ--GLvvaqYIRNRRLDRCADDLRPaaDDEKITSIAYKWG 275
                           90       100
                   ....*....|....*....|..
gi 2796455230 1299 FSDAKYFREVFKKHYNVSPSQY 1320
Cdd:PRK09685   276 FSDSSHFSTAFKQRFGVSPGEY 297
pleD PRK09581
response regulator PleD; Reviewed
1072-1173 3.75e-11

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 67.23  E-value: 3.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTA 1151
Cdd:PRK09581   157 RILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLVD 236
                           90       100
                   ....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKP 1173
Cdd:PRK09581   237 EDDDPRLVKALELGVNDYLMRP 258
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
1223-1320 6.16e-11

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: 65.85  E-value: 6.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1223 IANVKKNVEDNIDNPaLTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDThSITEIAEMTGFSDA 1302
Cdd:COG2169     86 VARACRLIEAGAEDR-PSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGL-SVTDAAYAAGFGSL 163
                           90
                   ....*....|....*...
gi 2796455230 1303 KYFREVFKKHYNVSPSQY 1320
Cdd:COG2169    164 SRFYEAFKKLLGMTPSAY 181
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1073-1175 7.29e-11

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 60.50  E-value: 7.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYFVQVCSN-GKEALTIIPEYKPELVISDIMMPEMRGDELCQAIK-NNIETshiPVILLT 1150
Cdd:cd17616      1 VLLIEDDSATAQSIELMLKSEGFNVYTTDlGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRlAKVKT---PILILS 77
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFN 1175
Cdd:cd17616     78 GLADIEDKVKGLGFGADDYMTKPFH 102
PRK10766 PRK10766
two-component system response regulator TorR;
1072-1212 1.20e-10

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 62.75  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDN----DELRNYLSQtlsEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPVI 1147
Cdd:PRK10766     4 HILVVEDEpvtrARLQGYFEQ---EGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR---SRSTVGII 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRALLRSKfanldLNDEENDEDCI 1212
Cdd:PRK10766    78 LVTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLLWRISLARQA-----QPHAQEEDNCY 137
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
1073-1176 1.38e-10

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 59.82  E-value: 1.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLTA 1151
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMISG 78
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNI 1176
Cdd:cd17550     79 HGTIETAVKATKLGAYDFIEKPLSL 103
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1073-1172 1.39e-10

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: 60.05  E-value: 1.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYFVQV---CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIpvILL 1149
Cdd:cd19931      1 VLLIDDHPLLRKGIKQLIELDPDFTVvgeASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARI--VIL 78
                           90       100
                   ....*....|....*....|...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVK 1172
Cdd:cd19931     79 TVSDAEDDVVTALRAGADGYLLK 101
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
917-1180 1.44e-10

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 66.15  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTpENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLML 996
Cdd:PRK10841   559 DPMRLQQVISNLLSNAIKFT-DTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAI 637
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  997 VWKLVRLHKGKINLSSIENQGSVIKITFP---------------KDSK-------------------------------- 1029
Cdd:PRK10841   638 CEKLINMMDGDISVDSEPGMGSQFTIRIPlygaqypqkkgveglQGKRcwlavrnasleqfletllqrsgiqvqryegqe 717
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1030 -----------------------RFRKAHLATPSKQ-----------------------RIENTIDNVPPPSPEIYENAQ 1063
Cdd:PRK10841   718 ptpedvlitddpvqkkwqgraviTFCRRHIGIPLEIapgewvhstatphelpallariyRIELESDDSANALPSTDKAVS 797
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1064 KKENInhrRILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETs 1142
Cdd:PRK10841   798 DNDDM---MILVVDDHPINRRLLADQLgSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLT- 873
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2796455230 1143 hIPVILLT--ALNNEKDilSGLQIGADEYVVKPFNIGILK 1180
Cdd:PRK10841   874 -LPVIGVTanALAEEKQ--RCLEAGMDSCLSKPVTLDVLK 910
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1073-1174 1.49e-10

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 59.86  E-value: 1.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDN----DELRnYLSQTLSEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIP-VI 1147
Cdd:cd17532      1 ALIVDDEplarEELR-YLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLS---KLAKPPlIV 76
                           90       100
                   ....*....|....*....|....*..
gi 2796455230 1148 LLTALnnEKDILSGLQIGADEYVVKPF 1174
Cdd:cd17532     77 FVTAY--DEYAVEAFELNAVDYLLKPF 101
ftrA PRK09393
transcriptional activator FtrA; Provisional
1240-1322 1.89e-10

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 63.83  E-value: 1.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1240 TVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPSQ 1319
Cdd:PRK09393   236 TVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAA 315

                   ...
gi 2796455230 1320 YGK 1322
Cdd:PRK09393   316 YRK 318
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
1071-1183 2.01e-10

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 59.49  E-value: 2.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnnIETSHIPVILL 1149
Cdd:cd17553      1 EKILIVDDQYGIRILLNEVFNKEgYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMK--VIDENIRVIIM 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANV 1183
Cdd:cd17553     79 TAYGELDMIQESKELGALTHFAKPFDIDEIRDAV 112
PRK10693 PRK10693
two-component system response regulator RssB;
1100-1173 3.43e-10

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 62.70  E-value: 3.43e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796455230 1100 SNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILLTALNNEKDILSGLQIGADEYVVKP 1173
Cdd:PRK10693     4 ANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRN--RGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75
PRK10490 PRK10490
sensor protein KdpD; Provisional
921-1025 5.46e-10

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 63.90  E-value: 5.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNaiNSKVTGSGIGLMLVWKL 1000
Cdd:PRK10490   779 FERVLINLLENAVKYAGAQAEIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNK--ESAIPGVGLGLAICRAI 856
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1001 VRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:PRK10490   857 VEVHGGTIWAENRPEGGACFRVTLP 881
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
923-1025 5.55e-10

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: 57.68  E-value: 5.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  923 SIFKNIISNALKYT----PENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKlhfRGsnaINSKVTGS-GIGLMLV 997
Cdd:cd16915      3 TIVGNLIDNALDALaatgAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFE---RG---VSTKGQGErGIGLALV 76
                           90       100
                   ....*....|....*....|....*...
gi 2796455230  998 WKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16915     77 RQSVERLGGSITVESEPGGGTTFSIRIP 104
PRK15115 PRK15115
response regulator GlrR; Provisional
1072-1191 5.97e-10

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 63.32  E-value: 5.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVILLT 1150
Cdd:PRK15115     7 HLLLVDDDPGLLKLLGMRLtSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKV--QPGMPVIILT 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2796455230 1151 ALNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLANRA 1191
Cdd:PRK15115    85 AHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSA 125
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
921-1025 6.25e-10

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: 57.46  E-value: 6.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYtpenGNVQVFVSETSDSWSV--EVRDTGIGIPANEQKKLFKLHFRGSNAINSKvtGSGIGLMLVW 998
Cdd:cd16950      1 LKRVLSNLVDNALRY----GGGWVEVSSDGEGNRTriQVLDNGPGIAPEEVDELFQPFYRGDNARGTS--GTGLGLAIVQ 74
                           90       100
                   ....*....|....*....|....*..
gi 2796455230  999 KLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16950     75 RISDAHGGSLTLANRAGGGLCARIELP 101
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1073-1176 8.72e-10

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 62.58  E-value: 8.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYFVQVC-SNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETshIPVILLTA 1151
Cdd:PRK10923     6 VWVVDDDSSIRWVLERALAGAGLTCTTfENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTA 83
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNI 1176
Cdd:PRK10923    84 HSDLDAAVSAYQQGAFDYLPKPFDI 108
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
911-1023 8.84e-10

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


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 57.91  E-value: 8.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  911 YMNVwfDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGS 990
Cdd:cd16947     13 YANA--NTEALQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGN 90
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230  991 GIGLMLVWKLVRLHKGKINLSSIENQGSVIKIT 1023
Cdd:cd16947     91 GLGLTITKRLAESMGGSIYVNSKPYEKTVFTVT 123
PRK10604 PRK10604
sensor protein RstB; Provisional
813-1043 1.22e-09

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 62.31  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  813 AHDIRTPLTLIKAPLEELREKEELSKEGISnmntalRNVNALLRLTTNLINFERADVYSSELYISEHELNTFMNEIFNAF 892
Cdd:PRK10604   220 AHELRTPLVRLRYRLEMSDNLSAAESQALN------RDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLADI 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  893 QQYANIKHINFTYESNFRYMNVwfDKEKMESIFKNIISNALKYTpeNGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKL 972
Cdd:PRK10604   294 QAVTPEKTVRLDTPHQGDYGAL--DMRLMERVLDNLLNNALRYA--HSRVRVSLLLDGNQACLIVEDDGPGIPPEERERV 369
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796455230  973 FKLHFRGSNAINSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPkdskrfrkAHLATPSKQR 1043
Cdd:PRK10604   370 FEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWP--------VWHNLPQFTS 432
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1073-1172 1.74e-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: 56.90  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYFVQV---CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILL 1149
Cdd:cd19930      1 VLIAEDQEMVRGALAALLELEDDLEVvaqASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE--ELPDTKVLIV 78
                           90       100
                   ....*....|....*....|...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVK 1172
Cdd:cd19930     79 TTFGRPGYFRRALAAGVDGYVLK 101
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1067-1181 1.77e-09

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: 58.39  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1067 NINHRRILIVEDNDELRNYLSQTLSE-EYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIEtsHIP 1145
Cdd:COG4567      1 SAEDRSLLLVDDDEAFARVLARALERrGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDP--DAR 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2796455230 1146 VILLTALNNEKDILSGLQIGADEYVVKPFNIG-ILKA 1181
Cdd:COG4567     79 IVVLTGYASIATAVEAIKLGADDYLAKPADADdLLAA 115
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
305-547 1.96e-09

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 60.03  E-value: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  305 DIFVDDEERIWLANY---PIG-ITIQNNRYTSYKWIKHSignkqslindQVNAIIEDREGDLWFAT--NNGISFFNSKTG 378
Cdd:COG4257     21 DVAVDPDGAVWFTDQgggRIGrLDPATGEFTEYPLGGGS----------GPHGIAVDPDGNLWFTDngNNRIGRIDPKTG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  379 QWRSVLSAFEESQGNkshiflTICEVAPGIIW-AGGYSSGAYQIDKKTFSVSYFMPPlythtnkRPDKYIRDIRTDMQGY 457
Cdd:COG4257     91 EITTFALPGGGSNPH------GIAFDPDGNLWfTDQGGNRIGRLDPATGEVTEFPLP-------TGGAGPYGIAVDPDGN 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  458 IWSGGFYN--LKRINLKTQEVRFYDGLNSIT-----AIVEKDekSMWIGSATG--LCLLDKESGKFERIKLPVESNYIYS 528
Cdd:COG4257    158 LWVTDFGAnaIGRIDPDTGTLTEYALPTPGAgprglAVDPDG--NLWVADTGSgrIGRFDPKTGTVTEYPLPGGGARPYG 235
                          250
                   ....*....|....*....
gi 2796455230  529 LYQAKNGSLYIATSGSGLL 547
Cdd:COG4257    236 VAVDGDGRVWFAESGANRI 254
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
1073-1173 2.87e-09

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: 55.59  E-value: 2.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILLTA 1151
Cdd:cd19928      1 ILVADDDRAIRTVLTQALGRAgYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKK--ARPDLPIIVMSA 78
                           90       100
                   ....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd19928     79 QNTLMTAVKAAERGAFEYLPKP 100
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
927-1028 2.95e-09

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 61.01  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  927 NIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHF---RGsnaiNSKVTGSGIGLMLVWKLVRL 1003
Cdd:PRK11100   375 NLLDNAIDFSPEGGTITLSAEVDGEQVALSVEDQGPGIPDYALPRIFERFYslpRP----ANGRKSTGLGLAFVREVARL 450
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1004 HKGKINLSSIENQGSVIKITFPKDS 1028
Cdd:PRK11100   451 HGGEVTLRNRPEGGVLATLTLPRHF 475
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1072-1172 3.36e-09

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 58.88  E-value: 3.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETshiPVILLT 1150
Cdd:PRK10701     3 KIVFVEDDAEVGSLIAAYLAKHDIdVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG---PIVLLT 79
                           90       100
                   ....*....|....*....|...
gi 2796455230 1151 ALNNEKD-ILSgLQIGADEYVVK 1172
Cdd:PRK10701    80 SLDSDMNhILA-LEMGACDYILK 101
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
793-1008 4.03e-09

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 60.72  E-value: 4.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  793 LILRKQRKVSDekihffinTAHDIRTPLTLIKAPLEELREKEELSKEgISNMNT-ALR---NVNALLRLTTNLINferad 868
Cdd:PRK09470   239 MMTSQQRLLSD--------ISHELRTPLTRLQLATALLRRRQGESKE-LERIETeAQRldsMINDLLVLSRNQQK----- 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  869 vysSELYISEHELNTFMNEIFNAFQQYANIKHINFTYESNF-RYMnVWFDKEKMESIFKNIISNALKYTpeNGNVQVFVS 947
Cdd:PRK09470   305 ---NHLERETFKANSLWSEVLEDAKFEAEQMGKSLTVSAPPgPWP-INGNPNALASALENIVRNALRYS--HTKIEVAFS 378
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796455230  948 ETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKLVRLHKGKI 1008
Cdd:PRK09470   379 VDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWV 439
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
1073-1173 6.18e-09

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: 55.40  E-value: 6.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTAL 1152
Cdd:cd17539      1 VLLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVADP 80
                           90       100
                   ....*....|....*....|.
gi 2796455230 1153 NNEKDILSGLQIGADEYVVKP 1173
Cdd:cd17539     81 GDRGRLIRALEIGVNDYLVRP 101
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1072-1181 6.48e-09

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: 55.24  E-value: 6.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQV--CSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIK-NNIETShipVIL 1148
Cdd:cd17593      2 KVLICDDSSMARKQLARALPADWDVEItfAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPvEQLETK---VIV 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPFNIGILKA 1181
Cdd:cd17593     79 VSGDVQPEAKERVLELGALAFLKKPFDPEKLAQ 111
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
929-1030 7.45e-09

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 59.92  E-value: 7.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  929 ISNALKY---TPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKlfklhfrgsnainskvTGSGIGLMLVWKLVRLHK 1005
Cdd:COG3920    408 VTNALKHaflSGEGGRIRVSWRREDGRLRLTVSDNGVGLPEDVDPP----------------ARKGLGLRLIRALVRQLG 471
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1006 GKINLSSieNQGSVIKITFPKDSKR 1030
Cdd:COG3920    472 GTLELDR--PEGTRVRITFPLAELA 494
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
1071-1181 9.73e-09

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: 54.37  E-value: 9.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIpvILL 1149
Cdd:cd17563      1 KSLLLVDDDEVFAERLARALERRGFeVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARI--VVL 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIG-ILKA 1181
Cdd:cd17563     79 TGYASIATAVEAIKLGADDYLAKPADADeILAA 111
PRK13557 PRK13557
histidine kinase; Provisional
917-1131 1.11e-08

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 59.30  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQV----FVSETSDSW-----------SVEVRDTGIGIPAneqkklfklhfrgsn 981
Cdd:PRK13557   274 DPTQAEVALLNVLINARDAMPEGGRVTIrtrnVEIEDEDLAmyhglppgryvSIAVTDTGSGMPP--------------- 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  982 AINSKVT-----------GSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSKRFRKAHLATPSKQRIENTidn 1050
Cdd:PRK13557   339 EILARVMdpffttkeegkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEPKARAIDRGGT--- 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1051 vpppspeiyenaqkkeninhRRILIVEDNDELRNyLSQTLSEE--YFVQVCSNGKEALTII-PEYKPELVISDIMMP-EM 1126
Cdd:PRK13557   416 --------------------ETILIVDDRPDVAE-LARMILEDfgYRTLVASNGREALEILdSHPEVDLLFTDLIMPgGM 474

                   ....*
gi 2796455230 1127 RGDEL 1131
Cdd:PRK13557   475 NGVML 479
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1073-1173 1.18e-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: 53.91  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYFVQVCSNGK-EALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTa 1151
Cdd:cd17602      1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPlRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLT- 79
                           90       100
                   ....*....|....*....|....*.
gi 2796455230 1152 lnnEKD-ILSGLQI---GADEYVVKP 1173
Cdd:cd17602     80 ---GKDgLVDRIRAkmaGASGYLTKP 102
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
1071-1153 2.43e-08

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: 53.60  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSqTLSEEYF---VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNieTSHIPVI 1147
Cdd:cd17530      1 LRVLVLDDDPFQCMMAA-TILEDLGpgnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAES--HSNAAVI 77

                   ....*.
gi 2796455230 1148 LLTALN 1153
Cdd:cd17530     78 LMSGLD 83
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
1073-1173 3.09e-08

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 52.79  E-value: 3.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSE-EYFVQVCSNGKEALTIIPEYKPE--LVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:cd17582      1 VLLVENDDSTRQIVTALLRKcSYEVTAASDGLQAWDVLEDEQNEidLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                           90       100
                   ....*....|....*....|....
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd17582     81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
1072-1131 4.39e-08

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 52.50  E-value: 4.39e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796455230 1072 RILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKP-ELVISDIMMPEMRGDEL 1131
Cdd:cd18160      1 TILLADDEPSVRKFIVTTLkKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIEL 62
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1073-1173 7.25e-08

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 52.37  E-value: 7.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEAL-----------TIIPEYKPELVISDIMMPEMRGDELCQAIKNNIE 1140
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLrISSCRVTAVDSGKRALeflgledeedsSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230 1141 TSHIPVILLTALNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd17581     81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
1244-1320 7.48e-08

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 55.68  E-value: 7.48e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796455230 1244 LCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPSQY 1320
Cdd:PRK13501   198 FCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDY 274
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
917-1025 7.81e-08

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 56.57  E-value: 7.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLML 996
Cdd:PRK10549   349 DPDRLMQLFNNLLENSLRYTDSGGSLHISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAI 428
                           90       100
                   ....*....|....*....|....*....
gi 2796455230  997 VWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:PRK10549   429 CLNIVEAHNGRIIAAHSPFGGVSITVELP 457
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
923-1032 8.53e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 56.46  E-value: 8.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  923 SIFKNIISNALKYTPENGNVQVFVS-ETSDSW-SVEVRDTGIGIPANEQKKLFKlhfrgsNAINSKVTGSGIGLMLVWKL 1000
Cdd:PRK11086   436 TILGNLIENALEAVGGEEGGEISVSlHYRNGWlHCEVSDDGPGIAPDEIDAIFD------KGYSTKGSNRGVGLYLVKQS 509
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2796455230 1001 VRLHKGKINLSSIENQGSVIKITFPKDSKRFR 1032
Cdd:PRK11086   510 VENLGGSIAVESEPGVGTQFFVQIPWDGERSN 541
PRK10336 PRK10336
two-component system response regulator QseB;
1072-1174 8.55e-08

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 54.52  E-value: 8.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDN----DELRNYLSQT-LSEEYFVQvCSNGKEALTIIPEykpELVISDIMMPEMRGDELCQAIKNNieTSHIPV 1146
Cdd:PRK10336     2 RILLIEDDmligDGIKTGLSKMgFSVDWFTQ-GRQGKEALYSAPY---DAVILDLTLPGMDGRDILREWREK--GQREPV 75
                           90       100
                   ....*....|....*....|....*...
gi 2796455230 1147 ILLTALNNEKDILSGLQIGADEYVVKPF 1174
Cdd:PRK10336    76 LILTARDALAERVEGLRLGADDYLCKPF 103
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
927-1025 9.57e-08

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: 51.24  E-value: 9.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  927 NIISNALK----YTPENGNVQV-FVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFrgsnaiNSKVTGSGIGLMLVWKLV 1001
Cdd:cd16920      7 NLVRNGIEamseGGCERRELTIrTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFY------TTKSEGLGMGLSICRSII 80
                           90       100
                   ....*....|....*....|....
gi 2796455230 1002 RLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16920     81 EAHGGRLSVESPAGGGATFQFTLP 104
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
1073-1183 1.47e-07

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: 50.89  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGK--EALTIIPEYkpELVISDIMMPEMRGDELCQAIKNNieTSHIPVILL 1149
Cdd:cd17573      1 ILLIEDDSTLGKEISKGLNEKgYQADVAESLKdgEYYIDIRNY--DLVLVSDKLPDGNGLSIVSRIKEK--HPSIVVIVL 76
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVKPFNIGILKANV 1183
Cdd:cd17573     77 SDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
927-1013 1.60e-07

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: 50.92  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  927 NIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAiNSKVTGSGIGLMLVWKLVRLHKG 1006
Cdd:cd16945     11 NLLDNAIDFSPEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRP-HSGQKSTGLGLAFVQEVAQLHGG 89

                   ....*..
gi 2796455230 1007 KINLSSI 1013
Cdd:cd16945     90 RITLRNR 96
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1073-1200 1.97e-07

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: 52.80  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTL-SEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVILLTA 1151
Cdd:COG4566      2 VYIVDDDEAVRDSLAFLLeSAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAA--RGSPLPVIFLTG 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796455230 1152 lnnEKDI---LSGLQIGADEYVVKPFNIGILKANVANLLA----------NRALLRSKFANL 1200
Cdd:COG4566     80 ---HGDVpmaVRAMKAGAVDFLEKPFDDQALLDAVRRALArdrarraeraRRAELRARLASL 138
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1073-1189 2.24e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 55.04  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSE-EYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnnIETSHIPVILLTA 1151
Cdd:PRK10365     8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK--ALNPAIPVLIMTA 85
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKPFNIGILKANVANLLAN 1189
Cdd:PRK10365    86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAH 123
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
926-1011 2.49e-07

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 54.59  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  926 KNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRgsnaINSKVTGSGIGLMLVWKLVRLHK 1005
Cdd:PRK10755   253 RNLVENAHRYSPEGSTITIKLSQEDGGAVLAVEDEGPGIDESKCGELSKAFVR----MDSRYGGIGLGLSIVSRITQLHH 328

                   ....*.
gi 2796455230 1006 GKINLS 1011
Cdd:PRK10755   329 GQFFLQ 334
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
921-1012 3.94e-07

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 49.71  E-value: 3.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYTPENGNVQVFVSETSDSWS-----------VEVRDTGIGIPANEQKKLFKlhfrgsNAINSKVTG 989
Cdd:cd16918      1 LIQVFLNLVRNAAQALAGSGGEIILRTRTQRQVTlghprhrlalrVSVIDNGPGIPPDLQDTIFY------PMVSGRENG 74
                           90       100
                   ....*....|....*....|...
gi 2796455230  990 SGIGLMLVWKLVRLHKGKINLSS 1012
Cdd:cd16918     75 TGLGLAIAQNIVSQHGGVIECDS 97
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
1072-1172 4.75e-07

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: 50.10  E-value: 4.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFV--QVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILL 1149
Cdd:cd17575      2 MVLLVDDQAIIGEAVRRALADEEDIdfHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVL 81
                           90       100
                   ....*....|....*....|...
gi 2796455230 1150 TALNNEKDILSGLQIGADEYVVK 1172
Cdd:cd17575     82 STKEEPEVKSEAFALGANDYLVK 104
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
924-1024 4.84e-07

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 49.49  E-value: 4.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  924 IFKNIISNALKYTP-ENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKLVR 1002
Cdd:cd16953      4 VLRNLIGNAISFSPpDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISRQIIE 83
                           90       100
                   ....*....|....*....|..
gi 2796455230 1003 LHKGKINLSSIENQGSVIKITF 1024
Cdd:cd16953     84 AHGGISVAENHNQPGQVIGARF 105
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
1208-1320 5.76e-07

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 50.10  E-value: 5.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1208 DEDCINCSQDIDWkfianvkknVEDNIDNPaLTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDT 1287
Cdd:PRK11511     5 NTDAITIHSILDW---------IEDNLESP-LSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESN 74
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230 1288 HSITEIAEMTGFSDAKYFREVFKKHYNVSPSQY 1320
Cdd:PRK11511    75 EPILYLAERYGFESQQTLTRTFKNYFDVPPHKY 107
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
921-1025 1.00e-06

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: 48.58  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALKYTpeNGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGSNAINSKVTGSGIGLMLVWKL 1000
Cdd:cd16939      1 MARALDNLLRNALRYA--HRTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRV 78
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1001 VRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16939     79 ALWHGGHVECDDSELGGACFRLTWP 103
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
1072-1173 1.10e-06

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: 49.29  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKnniETSHIPV-ILLT 1150
Cdd:cd17596      2 TILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVR---ERWPEVVrIIIS 78
                           90       100
                   ....*....|....*....|....
gi 2796455230 1151 ALNNEKDILSGL-QIGADEYVVKP 1173
Cdd:cd17596     79 GYTDSEDIIAGInEAGIYQYLTKP 102
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
1192-1317 1.23e-06

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 51.60  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1192 LLRSKfaNLDLNDEENDEDcINcsQDIDWkfianVKKNVEDNIDNPALTVDVLCSLMGMSRtsfynKLRALTDQAPGDYI 1271
Cdd:PRK13503   156 LLRKS--SLQENGENSDAR-LN--QLLAW-----LEDHFAEEVNWEALADQFSLSLRTLHR-----QLKQQTGLTPQRYL 220
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2796455230 1272 RLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSP 1317
Cdd:PRK13503   221 NRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSP 266
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
917-1025 1.25e-06

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 48.30  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPEN----GNVQVFVSETSDSW-SVEVRDTGIGIPANEQKKLFKLHfrgsnaINSKVTGSG 991
Cdd:cd16944      1 DTTQISQVLTNILKNAAEAIEGRpsdvGEVRIRVEADQDGRiVLIVCDNGKGFPREMRHRATEPY------VTTRPKGTG 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2796455230  992 IGLMLVWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16944     75 LGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
1073-1174 1.94e-06

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: 47.73  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEE-YFVQVCSNGKEALTIIPEY-KPELVISDIMMP-EMRGDELCQAIKnnIETSHIPVILL 1149
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLEDLgYTVLEAASGDEALDLLESGpDIDLLVTDVIMPgGMNGSQLAEEAR--RRRPDLKVLLT 78
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1150 TALnNEKDILSGLQIGADEYVVKPF 1174
Cdd:cd18161     79 SGY-AENAIEGGDLAPGVDVLSKPF 102
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
856-1029 2.20e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 51.94  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  856 RLTTNLINFERADVYSSELYISEHElntfmnEIFNAfQQYANIKHInfTYESNFRY-MNVwfDKEKME-SIFKNIIS--- 930
Cdd:COG2972    277 EMLEALSKLLRYSLSKGDELVTLEE------ELELI-KSYLEIQKL--RFGDRLEVeIEI--DEELLDlLIPKLILQplv 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  931 -NALKY----TPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFklhfrgsNAINSKVTGSGIGLMLVWKLVRLHK 1005
Cdd:COG2972    346 eNAIEHgiepKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLL-------EELSSKGEGRGIGLRNVRERLKLYY 418
                          170       180
                   ....*....|....*....|....*..
gi 2796455230 1006 GK---INLSSIENQGSVIKITFPKDSK 1029
Cdd:COG2972    419 GEeygLEIESEPGEGTTVTIRIPLEEE 445
PLN03029 PLN03029
type-a response regulator protein; Provisional
1111-1209 2.74e-06

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 50.03  E-value: 2.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1111 EYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPVILLTALNNEKDILSGLQIGADEYVVKPFNIGILkanvanllaNR 1190
Cdd:PLN03029    70 EVEVNLIITDYCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL---------NR 140
                           90       100
                   ....*....|....*....|..
gi 2796455230 1191 A---LLRSKFANLDLNDEENDE 1209
Cdd:PLN03029   141 LkphMMKTKSKNQKQENQEKQE 162
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1072-1196 3.11e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 50.92  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQVC---SNGKEALTIIPEYKPELVISDIMMPEMRGDElcqAIKNNIETSHIPVIL 1148
Cdd:PRK00742     5 RVLVVDDSAFMRRLISEILNSDPDIEVVgtaPDGLEAREKIKKLNPDVITLDVEMPVMDGLD---ALEKIMRLRPTPVVM 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2796455230 1149 LTALNNE--KDILSGLQIGADEYVVKPFnIGIL--KANVANLLAN--RALLRSK 1196
Cdd:PRK00742    82 VSSLTERgaEITLRALELGAVDFVTKPF-LGISlgMDEYKEELAEkvRAAARAR 134
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
913-1025 8.59e-06

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 50.07  E-value: 8.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  913 NVWFDKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEqkKLFKlHFrgsnaINSKVTGSGI 992
Cdd:COG4192    536 MVQGDQVLLEQVLVNLLVNALDAVATQPQISVDLLSNAENLRVAISDNGNGWPLVD--KLFT-PF-----TTTKEVGLGL 607
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2796455230  993 GLMLVWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:COG4192    608 GLSICRSIMQQFGGDLYLASTLERGAMVILEFN 640
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
917-1029 1.14e-05

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 49.83  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKY---TPE-NGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKlhfRGSNAINSKVTGSGI 992
Cdd:PRK15053   429 DSTEFAAIVGNLLDNAFEAslrSDEgNKIVELFLSDEGDDVVIEVADQGCGVPESLRDKIFE---QGVSTRADEPGEHGI 505
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2796455230  993 GLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSK 1029
Cdd:PRK15053   506 GLYLIASYVTRCGGVITLEDNDPCGTLFSIFIPKVKP 542
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
1275-1320 1.49e-05

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 48.52  E-value: 1.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2796455230 1275 RLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPSQY 1320
Cdd:PRK15186   233 RMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
1239-1320 1.88e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 48.13  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1239 LTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPS 1318
Cdd:PRK13502   193 FALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPS 272

                   ..
gi 2796455230 1319 QY 1320
Cdd:PRK13502   273 QW 274
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
1073-1173 2.29e-05

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 44.45  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIknNIETSHIPVILLTA 1151
Cdd:cd19926      1 VLVVDDEPDIRELLEITLGRMGLdVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHI--QQRLPQTPVAVITA 78
                           90       100
                   ....*....|....*....|..
gi 2796455230 1152 LNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd19926     79 YGSLDTAIEALKAGAFDFLTKP 100
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
929-1029 2.32e-05

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 47.31  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  929 ISNALKYTPENgNVQVFVSETSDSWSVEVRDTGIGIPANeqkklfklhfrgsnainsKVTGSGIGLMLVWKLVRLHKGKI 1008
Cdd:COG4585    171 LTNALKHAGAT-RVTVTLEVDDGELTLTVRDDGVGFDPE------------------AAPGGGLGLRGMRERAEALGGTL 231
                           90       100
                   ....*....|....*....|.
gi 2796455230 1009 NLSSIENQGSVIKITFPKDSK 1029
Cdd:COG4585    232 TIGSAPGGGTRVRATLPLAAA 252
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
1275-1320 2.79e-05

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 47.66  E-value: 2.79e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2796455230 1275 RLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPSQY 1320
Cdd:PRK10572   236 RISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEF 281
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
1283-1320 3.91e-05

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 42.14  E-value: 3.91e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2796455230 1283 LKEDTH---SITEIAEMTGFSdAKYFREVFKKHYNVSPSQY 1320
Cdd:pfam00165    1 LRENLStnlTIADIADELGFS-RSYFSRLFKKYTGVTPSQY 40
PRK11697 PRK11697
two-component system response regulator BtsR;
1072-1174 4.03e-05

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 46.76  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDN----DELRNYLSQTlSEEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCqaikNNIETSHIP-V 1146
Cdd:PRK11697     3 KVLIVDDEplarEELRELLQEE-GDIEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELV----GMLDPEHMPyI 77
                           90       100
                   ....*....|....*....|....*...
gi 2796455230 1147 ILLTALnnekdilsglqigaDEYVVKPF 1174
Cdd:PRK11697    78 VFVTAF--------------DEYAIKAF 91
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
1230-1326 4.62e-05

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 46.84  E-value: 4.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1230 VEDNIDNpALTVDVLCSLMGMSRTSFYNKLRAltdqAPGDYIRLI---RLKRAVQLLKEDTHSITEIAEMTGFSDAKYFR 1306
Cdd:PRK09978   151 INNNIAH-EWTLARIASELLMSPSLLKKKLRE----EETSYSQLLtecRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFI 225
                           90       100
                   ....*....|....*....|
gi 2796455230 1307 EVFKKHYNVSPSQYgKEKKA 1326
Cdd:PRK09978   226 YVFRNYYGMTPTEY-QERSA 244
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
954-1025 9.11e-05

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: 43.14  E-value: 9.11e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796455230  954 SVEVRDTGIGIPANEQKKLFKLHFR----GSnainskvtGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFP 1025
Cdd:cd16919     49 CLEVSDTGSGMPAEVLRRAFEPFFTtkevGK--------GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1072-1200 1.01e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.03  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEEYFVQVC---SNGKEALTIIPEYKPELVISDIMMPEMRGDElcqAIKNNIETSHIPVIL 1148
Cdd:PRK12555     2 RIGIVNDSPLAVEALRRALARDPDHEVVwvaTDGAQAVERCAAQPPDVILMDLEMPRMDGVE---ATRRIMAERPCPILI 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2796455230 1149 LTAL--NNEKDILSGLQIGADEYVVKPF-NIGilkanvANLLANRALLRSKFANL 1200
Cdd:PRK12555    79 VTSLteRNASRVFEAMGAGALDAVDTPTlGIG------AGLEEYAAELLAKIDQI 127
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
1073-1173 1.27e-04

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: 42.65  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQtLSEEYF----VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQAIKNniETSHIPVIL 1148
Cdd:cd17565      1 FYIVDDDKNIIKILSD-IIEDDDlgevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKD--TGSNGKFIM 77
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKP 1173
Cdd:cd17565     78 ISQVSDKEMIGKAYQAGIEFFINKP 102
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
917-1083 1.46e-04

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 46.21  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSETSDSWSVE---------------VRDTGIGIPANEQKKLFKLHFRGSN 981
Cdd:PRK13837   557 NPAELQQVLMNLCSNAAQAMDGAGRVDISLSRAKLRAPKVlshgvlppgryvllrVSDTGAGIDEAVLPHIFEPFFTTRA 636
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  982 AinskvtGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITFPKDSKrfrkahlatpskqrientidnvPPPSPEIYEN 1061
Cdd:PRK13837   637 G------GTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSK----------------------VPVAPQAFFG 688
                          170       180
                   ....*....|....*....|..
gi 2796455230 1062 AQKKENINHRRILIVEDNDELR 1083
Cdd:PRK13837   689 PGPLPRGRGETVLLVEPDDATL 710
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
899-1024 1.89e-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: 42.62  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  899 KHINFT--YESNFRYMnvwFDKEKMESIFKNIISNALKYTpeNGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKlh 976
Cdd:cd16954     17 KGVSISldISPELRFP---GERNDLMELLGNLLDNACKWC--LEFVEVTARQTDGGLHLIVDDDGPGVPESQRSKIFQ-- 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2796455230  977 fRGSNAiNSKVTGSGIGLMLVWKLVRLHKGKINLSSIENQGSVIKITF 1024
Cdd:cd16954     90 -RGQRL-DEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
PRK13560 PRK13560
hypothetical protein; Provisional
924-1025 1.96e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 45.82  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  924 IFKNIISNALKYT-PEN--GNVQVFVSETSD-SWSVEVRDTGIGIPANeqkklfkLHFRGSNAinskvtgsgIGLMLVWK 999
Cdd:PRK13560   715 IISELLSNALKHAfPDGaaGNIKVEIREQGDgMVNLCVADDGIGLPAG-------FDFRAAET---------LGLQLVCA 778
                           90       100
                   ....*....|....*....|....*.
gi 2796455230 1000 LVRLHKGKINLSSieNQGSVIKITFP 1025
Cdd:PRK13560   779 LVKQLDGEIALDS--RGGARFNIRFP 802
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
1073-1180 2.23e-04

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 42.25  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLSEEYF--VQVCSNGKEALTIIPEYKPELVISDIMMPEMR-GDELCQAIK-NNIETSHIPVIL 1148
Cdd:cd17589      1 FLIVDDQPTFRSMLKSMLRSLGVtrIDTASSGEEALRMCENKTYDIVLCDYNLGKGKnGQQLLEELRhKKLISPSTVFIM 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2796455230 1149 LTALNNEKDILSGLQIGADEYVVKPFNIGILK 1180
Cdd:cd17589     81 VTGESSRAMVLSALELEPDDYLLKPFTVSELR 112
PRK10371 PRK10371
transcriptional regulator MelR;
1269-1322 2.94e-04

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 44.43  E-value: 2.94e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2796455230 1269 DYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPSQYGK 1322
Cdd:PRK10371   238 QYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRK 291
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
1239-1320 3.00e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 44.71  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1239 LTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPS 1318
Cdd:PRK13500   223 FALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPS 302

                   ..
gi 2796455230 1319 QY 1320
Cdd:PRK13500   303 QW 304
glnL PRK11073
nitrogen regulation protein NR(II);
917-1012 5.99e-04

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 43.53  E-value: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  917 DKEKMESIFKNIISNALKYTPENGNVQVFVSETSD-----------SWSVEVRDTGIGIPANEQKKLFklhfrgSNAINS 985
Cdd:PRK11073   234 DPDQIEQVLLNIVRNALQALGPEGGTITLRTRTAFqltlhgeryrlAARIDIEDNGPGIPPHLQDTLF------YPMVSG 307
                           90       100
                   ....*....|....*....|....*..
gi 2796455230  986 KVTGSGIGLMLVWKLVRLHKGKINLSS 1012
Cdd:PRK11073   308 REGGTGLGLSIARNLIDQHSGKIEFTS 334
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1071-1176 7.72e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 42.88  E-value: 7.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1071 RRILIVEDNDELRNYLSQTLSEEYF-VQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELcqaIKNNIETSHIPVILL 1149
Cdd:PRK13856     2 KHVLVIDDDVAMRHLIVEYLTIHAFkVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEI---VRSLATKSDVPIIII 78
                           90       100
                   ....*....|....*....|....*...
gi 2796455230 1150 TALN-NEKDILSGLQIGADEYVVKPFNI 1176
Cdd:PRK13856    79 SGDRlEEADKVVALELGATDFIAKPFGT 106
PRK10337 PRK10337
sensor protein QseC; Provisional
926-1004 8.80e-04

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 43.48  E-value: 8.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  926 KNIISNALKYTPENGNVQVFVSETsdswSVEVRDTGIGIPANEQKKLFKLHFR--GSNAinskvTGSGIGLMLVWKLVRL 1003
Cdd:PRK10337   358 RNLLDNAIRYSPQGSVVDVTLNAR----NFTVRDNGPGVTPEALARIGERFYRppGQEA-----TGSGLGLSIVRRIAKL 428

                   .
gi 2796455230 1004 H 1004
Cdd:PRK10337   429 H 429
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
448-545 1.54e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 41.93  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  448 RDIRTDMQGYIW----SGGfyNLKRINLKTQEVRFYD--GLNSITAIVEKDEKSMWIGSATG--LCLLDKESGKFERIKL 519
Cdd:COG4257     20 RDVAVDPDGAVWftdqGGG--RIGRLDPATGEFTEYPlgGGSGPHGIAVDPDGNLWFTDNGNnrIGRIDPKTGEITTFAL 97
                           90       100
                   ....*....|....*....|....*.
gi 2796455230  520 PVESNYIYSLYQAKNGSLYIATSGSG 545
Cdd:COG4257     98 PGGGSNPHGIAFDPDGNLWFTDQGGN 123
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
1073-1176 1.57e-03

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


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 39.38  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1073 ILIVEDNDELRNYLSQTLS-EEYFVQVCSNGKEALTIIPEYKPELVISDIMMPEMRGDELCQaiknniETSHI-PVILLT 1150
Cdd:cd19922      1 ILLLEKERNLAHFLSLELQkEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAE------KLSRIkPASVII 74
                           90       100
                   ....*....|....*....|....*....
gi 2796455230 1151 ALNNEKDI---LSGLQIGADEYVVKPFNI 1176
Cdd:cd19922     75 VLDHWEDLqeeLEEVQRFAVSYVVKPVLI 103
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
1275-1322 1.70e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 42.29  E-value: 1.70e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2796455230 1275 RLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPSQYGK 1322
Cdd:PRK15185   258 RMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPSTFIK 305
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
1231-1320 1.90e-03

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 41.92  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1231 EDNIDNPaLTVDVLCSLMGMSRTSFYNKLRALTDQAPGDYIRLIRLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFK 1310
Cdd:PRK15121    15 EGHLDQP-LSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRFDSQQTFTRAFK 93
                           90
                   ....*....|
gi 2796455230 1311 KHYNVSPSQY 1320
Cdd:PRK15121    94 KQFAQTPALY 103
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
921-1019 2.28e-03

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: 38.98  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MESIFKNIISNALK--YTPENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFrgsnaiNSKVTGSGIGLMLV- 997
Cdd:cd16976      1 IQQVLMNLLQNALDamGKVENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFF------TTKPVGKGTGLGLSi 74
                           90       100
                   ....*....|....*....|...
gi 2796455230  998 -WKLVRLHKGKINLSSIENQGSV 1019
Cdd:cd16976     75 sYGIVEEHGGRLSVANEEGAGAR 97
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
345-368 3.34e-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: 36.14  E-value: 3.34e-03
                           10        20
                   ....*....|....*....|....
gi 2796455230  345 SLINDQVNAIIEDREGDLWFATNN 368
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTNG 24
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
921-1024 3.42e-03

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 41.54  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230  921 MEsIFKNIISNALKYTPENgnVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKlhfRGSNAiNSKVTGSGIGLMLVWKL 1000
Cdd:PRK10815   380 ME-VMGNVLDNACKYCLEF--VEISARQTDEHLHIVVEDDGPGIPESKRELIFD---RGQRA-DTLRPGQGLGLSVAREI 452
                           90       100
                   ....*....|....*....|....
gi 2796455230 1001 VRLHKGKINLSSIENQGSVIKITF 1024
Cdd:PRK10815   453 TEQYEGKISAGDSPLGGARMEVIF 476
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
802-866 4.46e-03

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: 36.81  E-value: 4.46e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796455230  802 SDEKIHFFINTAHDIRTPLTLIKAPLEELREKEELSKEGISNMNTALRNVNALLRLTTNLINFER 866
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1072-1172 4.68e-03

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


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 38.31  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNYLSQTLSEE--YFVQVCSNGKEALTIIPEYKPELV-ISDIMMPEM-RGdelcQAIKNNIEtSHIPVI 1147
Cdd:cd19921      1 KVLIVEDSKTFSKVLKHLIAQElgLEVDVAETLAEAKALLEEGDDYFAaLVDLNLPDApNG----EAVDLVLE-KGIPVI 75
                           90       100
                   ....*....|....*....|....*
gi 2796455230 1148 LLTALNNEKDILSGLQIGADEYVVK 1172
Cdd:cd19921     76 VLTGSFDEDKRETLLSKGVVDYVLK 100
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
1072-1173 5.87e-03

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 38.15  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455230 1072 RILIVEDNDELRNY---LSQTLSEEyfVQVCSNGKEALTII--PEYKPELVISDIMMPEMRGDELCQAIKNNIETSHIPV 1146
Cdd:cd19933      2 KVLLVDDNAVNRMVtkgLLEKLGCE--VTTVSSGEECLNLLasAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPL 79
                           90       100
                   ....*....|....*....|....*...
gi 2796455230 1147 ILLTALNNEKDILSG-LQIGADEYVVKP 1173
Cdd:cd19933     80 IVALTANTDDSTREKcLSLGMNGVITKP 107
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
928-1001 7.72e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 37.97  E-value: 7.72e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796455230  928 IISNALKYT---PENGNVQVFVSETSDSWSVEVRDTGIGIPANEQKKLFKLHFRGsnainskvtgsGIGLMLVWKLV 1001
Cdd:COG2172     42 AVTNAVRHAyggDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYSTLAEG-----------GRGLFLIRRLM 107
PRK15044 PRK15044
transcriptional regulator SirC; Provisional
1275-1320 9.62e-03

transcriptional regulator SirC; Provisional


Pssm-ID: 185004 [Multi-domain]  Cd Length: 295  Bit Score: 39.63  E-value: 9.62e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2796455230 1275 RLKRAVQLLKEDTHSITEIAEMTGFSDAKYFREVFKKHYNVSPSQY 1320
Cdd:PRK15044   244 RMNQAIKLLRMGAGNISQVATMCGYDTPSYFIAIFKRHFKITPLSF 289
 
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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