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Conserved domains on  [gi|1119624474|ref|WP_072546034|]
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two-component regulator propeller domain-containing protein [Mediterranea massiliensis]

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];
3-1186 5.15e-86

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


:

Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 302.68  E-value: 5.15e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474    3 QRWLLWMLAVLTAAVLKAQPEGSFTHYSSDDGLSENTVMDMLQDSRGNMWFSTWNGINKFDGYTFKTFKARQDNQIALTS 82
Cdd:COG3292      1 KRLLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474   83 NRVDNMKLDRYGFIWLQTyDDRAFRFDPRTEVFESVPAEGEPgSQTAISSIKVLPDGTVWLLTrregavrittdstdyrl 162
Cdd:COG3292     81 NYIRALLEDSDGRLWIGT-DGGLSRYDPKTDKFTRYPLDPGL-PNNSIRSIAEDSDGNIWVGT----------------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  163 tsvwyspaserlrvsrvfdvcqadgaewvlsdnglvcftpdgaepviyfenaeegkdsfkkrqsfyvmedcgdcllfgsg 242
Cdd:COG3292        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  243 ngtvwvyrkkdrtfrpvqldaasrisgikhlkklsqvvvatvSDGFFVYDLPTGRTEHYAASRLPAEKVKSIYRDLSDEI 322
Cdd:COG3292    142 ------------------------------------------SNGLYRYDPKTGKFKRFTLDGLPSNTITSLAEDADGNL 179
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  323 WFEQDvvgevahfnpytrklkcekvyaeptntdrsrpafhihedifGTLWVHPYGGGFSYFDRKNNCLRPFYNSmTGENW 402
Cdd:COG3292    180 WVDSD-----------------------------------------GNLWIGTDGNGLYRLDPNTGKFEHITHD-PDPNS 217
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  403 RFSNKIHSAFSDRQGNLWMCTHSKGLEKVTFRTDRFRLKVPVNHsyESLS-NEVRALCEDKDGNMWVglkdgmlrvynrh 481
Cdd:COG3292    218 LSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRHNDP--NGLSgNSVRSIAEDSDGNLWI------------- 282
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  482 reeigylteagtvshsgkplfgntyfvmqdshdNLWIATKGAGVVKAEPLPGTLRyrltryRYSADdvySLSDDNVYCLY 561
Cdd:COG3292    283 ---------------------------------RLWIGTYGGGLFRLDPKTGKFK------RYNPN---GLPSNSVYSIL 320
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  562 EDRRGRIWVATFANGISYLTRNADGkevfISHRNNLKGFPIKYcskVRCITGDADGHIWIGTTVGLLMVDdgfdrPEDAR 641
Cdd:COG3292    321 EDSDGNLWIGTSGGGLYRYDPKTGK----FTKFSEDNGLSNNF---IRSILEDSDGNLWVGTNGGLYRLD-----PKTGK 388
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  642 FYHYLRAPEKaNALSNNDIHWVKPTREGELYVATFGGGLNQlvdLNAEGQaRFKAYTVRDGLPSDILLSIQEDKKGQLWI 721
Cdd:COG3292    389 FTNFTHDPDK-NGLSSNYINSIFEDSDGRLWIGTDGGGLYR---YDPKTG-KFKHFTTKDGLPSNTIYSILEDDNGNLWN 463
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  722 STENGLSKFTPGLGRFENFQNKYSNSSIRFSeaasayasdgNILFGTNHGIFYFNPDSIQKSVYVPPIvltqlllanesv 801
Cdd:COG3292    464 FNSASNLGLLSLLGGLLGGLNLGNAIKLPLS----------NLGLLLTLLLLGINLSLVRSLISLLTL------------ 521
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  802 kpgphsVLKYTLDDTRELTLSHQENIFSIQYAALDYTNPSDIQYAYMLDGFEKNWNYVGKQRTATYTNLPKGHYVFKVRS 881
Cdd:COG3292    522 ------LLLALLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLL 595
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  882 TNADGVWSDNVRTLDIEVLPSFWETPLAYFLYVLFFLLIIVTAVYILFTIYRLKHRVAMEQQLTHMKLRFFTDISHELRT 961
Cdd:COG3292    596 LLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELIL 675
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  962 PLTLITGPLEYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQ-VQRLEIVAFVRKIMDNFEAVAE 1040
Cdd:COG3292    676 ELLLILLLLLLLLLLALLLLLLLLLALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLlLLILLIILLLLILLEELLLAND 755
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1041 EHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFE 1120
Cdd:COG3292    756 IELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLD 835
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1121 NLVDSSLFNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDFQKGKEHYDETVEFLQNDVE 1186
Cdd:COG3292    836 ILELILLELELGLLLGLLLLLLLEILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLA 901
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1219-1341 2.40e-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: 2.40e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1219 RSTMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVL 1297
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPIIM 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKK 1341
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAA 122
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1396-1483 8.75e-24

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 102.55  E-value: 8.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1396 VDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEY 1475
Cdd:COG2207    171 LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250

                   ....*...
gi 1119624474 1476 RDRKAGKN 1483
Cdd:COG2207    251 RKRLRARA 258
Vgb super family cl26743
Streptogramin lyase [Defense mechanisms];
91-340 4.03e-05

Streptogramin lyase [Defense mechanisms];


The actual alignment was detected with superfamily member COG4257:

Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 46.94  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474   91 DRYGFIWL-QTYDDRAFRFDPRTEVFESVPaegePGSQTAISSIKVLPDGTVWLLTRREGAV-RITTDSTDYRLTSVwys 168
Cdd:COG4257     25 DPDGAVWFtDQGGGRIGRLDPATGEFTEYP----LGGGSGPHGIAVDPDGNLWFTDNGNNRIgRIDPKTGEITTFAL--- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  169 PASERLRVSRVFDvcqADGAEWVLSDNG--------------------------LVCFTPDGAepvIYFenAEEGKDSFK 222
Cdd:COG4257     98 PGGGSNPHGIAFD---PDGNLWFTDQGGnrigrldpatgevtefplptggagpyGIAVDPDGN---LWV--TDFGANAIG 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  223 KrqsfyvmedcgdcllFGSGNGTVWVYRKKDRTFRPVQLDAAS--RIsgikhlkklsqVVVATVSDGFFVYDLPTGRTEH 300
Cdd:COG4257    170 R---------------IDPDTGTLTEYALPTPGAGPRGLAVDPdgNL-----------WVADTGSGRIGRFDPKTGTVTE 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1119624474  301 YAASRLPAEKVkSIYRDLSDEIWFEQDVVGEVAHFNPYTR 340
Cdd:COG4257    224 YPLPGGGARPY-GVAVDGDGRVWFAESGANRIVRFDPDTE 262
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
3-1186 5.15e-86

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 302.68  E-value: 5.15e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474    3 QRWLLWMLAVLTAAVLKAQPEGSFTHYSSDDGLSENTVMDMLQDSRGNMWFSTWNGINKFDGYTFKTFKARQDNQIALTS 82
Cdd:COG3292      1 KRLLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474   83 NRVDNMKLDRYGFIWLQTyDDRAFRFDPRTEVFESVPAEGEPgSQTAISSIKVLPDGTVWLLTrregavrittdstdyrl 162
Cdd:COG3292     81 NYIRALLEDSDGRLWIGT-DGGLSRYDPKTDKFTRYPLDPGL-PNNSIRSIAEDSDGNIWVGT----------------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  163 tsvwyspaserlrvsrvfdvcqadgaewvlsdnglvcftpdgaepviyfenaeegkdsfkkrqsfyvmedcgdcllfgsg 242
Cdd:COG3292        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  243 ngtvwvyrkkdrtfrpvqldaasrisgikhlkklsqvvvatvSDGFFVYDLPTGRTEHYAASRLPAEKVKSIYRDLSDEI 322
Cdd:COG3292    142 ------------------------------------------SNGLYRYDPKTGKFKRFTLDGLPSNTITSLAEDADGNL 179
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  323 WFEQDvvgevahfnpytrklkcekvyaeptntdrsrpafhihedifGTLWVHPYGGGFSYFDRKNNCLRPFYNSmTGENW 402
Cdd:COG3292    180 WVDSD-----------------------------------------GNLWIGTDGNGLYRLDPNTGKFEHITHD-PDPNS 217
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  403 RFSNKIHSAFSDRQGNLWMCTHSKGLEKVTFRTDRFRLKVPVNHsyESLS-NEVRALCEDKDGNMWVglkdgmlrvynrh 481
Cdd:COG3292    218 LSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRHNDP--NGLSgNSVRSIAEDSDGNLWI------------- 282
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  482 reeigylteagtvshsgkplfgntyfvmqdshdNLWIATKGAGVVKAEPLPGTLRyrltryRYSADdvySLSDDNVYCLY 561
Cdd:COG3292    283 ---------------------------------RLWIGTYGGGLFRLDPKTGKFK------RYNPN---GLPSNSVYSIL 320
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  562 EDRRGRIWVATFANGISYLTRNADGkevfISHRNNLKGFPIKYcskVRCITGDADGHIWIGTTVGLLMVDdgfdrPEDAR 641
Cdd:COG3292    321 EDSDGNLWIGTSGGGLYRYDPKTGK----FTKFSEDNGLSNNF---IRSILEDSDGNLWVGTNGGLYRLD-----PKTGK 388
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  642 FYHYLRAPEKaNALSNNDIHWVKPTREGELYVATFGGGLNQlvdLNAEGQaRFKAYTVRDGLPSDILLSIQEDKKGQLWI 721
Cdd:COG3292    389 FTNFTHDPDK-NGLSSNYINSIFEDSDGRLWIGTDGGGLYR---YDPKTG-KFKHFTTKDGLPSNTIYSILEDDNGNLWN 463
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  722 STENGLSKFTPGLGRFENFQNKYSNSSIRFSeaasayasdgNILFGTNHGIFYFNPDSIQKSVYVPPIvltqlllanesv 801
Cdd:COG3292    464 FNSASNLGLLSLLGGLLGGLNLGNAIKLPLS----------NLGLLLTLLLLGINLSLVRSLISLLTL------------ 521
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  802 kpgphsVLKYTLDDTRELTLSHQENIFSIQYAALDYTNPSDIQYAYMLDGFEKNWNYVGKQRTATYTNLPKGHYVFKVRS 881
Cdd:COG3292    522 ------LLLALLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLL 595
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  882 TNADGVWSDNVRTLDIEVLPSFWETPLAYFLYVLFFLLIIVTAVYILFTIYRLKHRVAMEQQLTHMKLRFFTDISHELRT 961
Cdd:COG3292    596 LLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELIL 675
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  962 PLTLITGPLEYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQ-VQRLEIVAFVRKIMDNFEAVAE 1040
Cdd:COG3292    676 ELLLILLLLLLLLLLALLLLLLLLLALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLlLLILLIILLLLILLEELLLAND 755
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1041 EHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFE 1120
Cdd:COG3292    756 IELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLD 835
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1121 NLVDSSLFNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDFQKGKEHYDETVEFLQNDVE 1186
Cdd:COG3292    836 ILELILLELELGLLLGLLLLLLLEILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLA 901
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
941-1163 4.37e-42

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 164.54  E-value: 4.37e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  941 EQQLTHMKLR-FFTDISHELRTPLTLITGPLEYV----LQNTKLpaeAREQLQVVERNSNRMLRLVNQILDFRKIQNKKM 1015
Cdd:NF033092   364 EQEKIEQERReFVANVSHELRTPLTTMRSYLEALadgaWKDPEL---APRFLGVTQNETERMIRLVNDLLQLSRMDSKDY 440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1016 KMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQT 1095
Cdd:NF033092   441 KLNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGTITFRLLETHNR 520
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1096 VSVGVQDQGIGIAENKKKSLFVRFENlVD---SSlfNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCF 1163
Cdd:NF033092   521 IIISISDQGLGIPKKDLDKIFDRFYR-VDkarSR--KMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTI 588
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
942-1167 3.71e-41

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


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 155.06  E-value: 3.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  942 QQLTHMKLRFFTDISHELRTPLTLITGPLEYVLQNTKLPAEAREQ-LQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQ 1020
Cdd:TIGR02966  108 RRLEQMRRDFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWNRaLEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDE 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1021 RLEIVAFVRKIMDNFEAVAEEHHIDFVFETEkEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGV 1100
Cdd:TIGR02966  188 PVDMPALLDHLRDEAEALSQGKNHQITFEID-GGVDVLGDEDELRSAFSNLVSNAIKYTPEGGTITVRWRRDGGGAEFSV 266
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119624474 1101 QDQGIGIAENKKKSLFVRFENlVDSSLFNQSS-SGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:TIGR02966  267 TDTGIGIAPEHLPRLTERFYR-VDKSRSRDTGgTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1219-1341 2.40e-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: 2.40e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1219 RSTMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVL 1297
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPIIM 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKK 1341
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAA 122
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
945-1335 1.15e-34

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 144.88  E-value: 1.15e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  945 THMKLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAR-EQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLE 1023
Cdd:PRK09959   709 TVAKSQFLATMSHEIRTPISSIMGFLE-LLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVD 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1024 IVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLW-VDADKFEKIVYNLLSNAFKYTPEG--KMITVFVH--DNGQTVSV 1098
Cdd:PRK09959   788 IPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVkIDPQAFKQVLSNLLSNALKFTTEGavKITTSLGHidDNHAVIKM 867
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1099 GVQDQGIGIAENKKKSLFVRFENlvDSSLFNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDFqkgkehydeTV 1178
Cdd:PRK09959   868 TIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI---------PV 936
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1179 EFLQNdVEQGGAKQEQQTAVEDngasegnkgeegtentdvRSTMLLVEDNTELRTFL-RSIFASEFRVVEAANGAEGLEK 1257
Cdd:PRK09959   937 EISQQ-VATVEAKAEQPITLPE------------------KLSILIADDHPTNRLLLkRQLNLLGYDVDEATDGVQALHK 997
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119624474 1258 ALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNI 1335
Cdd:PRK09959   998 VSMQHYDLLITDVNMPNMDGFELTRKLREQ--NSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1223-1322 3.13e-33

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 124.06  E-value: 3.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMttSHIPMVLLTAK 1301
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1119624474 1302 TAIESMLEGLEYGADDYITKP 1322
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1060-1167 1.32e-28

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 111.20  E-value: 1.32e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  1060 DADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENlVDSSLFNQSSSGIGLSL 1139
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFR-TDKRSRKIGGTGLGLSI 80
                            90       100
                    ....*....|....*....|....*...
gi 1119624474  1140 VKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITL 108
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1223-1333 6.65e-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: 106.47  E-value: 6.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTAK 1301
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRR--DPTTPVIILTAH 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1119624474 1302 TAIESMLEGLEYGADDYITKPFSATYLKARVR 1333
Cdd:pfam00072   80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
1220-1387 1.46e-26

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


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 109.34  E-value: 1.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1220 STMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLL 1298
Cdd:TIGR02154    3 RRILVVEDEPAIRELIAYNLEKAgYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPIIML 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEMYREKLMNMATSPDEPTVEESKAP-EMSPNDRKF 1377
Cdd:TIGR02154   83 TARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLRRIRPQLSDEVIEVGDLSLDPVAHRVFRGGQPlSLGPTEFRL 162
                          170
                   ....*....|
gi 1119624474 1378 MDKLMALMEK 1387
Cdd:TIGR02154  163 LHFFMTHPER 172
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1396-1483 8.75e-24

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 102.55  E-value: 8.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1396 VDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEY 1475
Cdd:COG2207    171 LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250

                   ....*...
gi 1119624474 1476 RDRKAGKN 1483
Cdd:COG2207    251 RKRLRARA 258
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1396-1476 2.33e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 95.31  E-value: 2.33e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  1396 VDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEY 1475
Cdd:smart00342    4 LEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEY 83

                    .
gi 1119624474  1476 R 1476
Cdd:smart00342   84 R 84
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
1064-1168 3.46e-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: 95.64  E-value: 3.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1064 FEKIVYNLLSNAFKYTPEGKmITVFVH-----DNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSGIGLS 1138
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGE-VTLRVSleeeeEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLA 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1119624474 1139 LVKELVEMHKASITVDSKLGEGSCFKVDFQ 1168
Cdd:cd16922     80 ISKKLVELMGGDISVESEPGQGSTFTFTLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
1060-1165 1.81e-22

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: 93.59  E-value: 1.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1060 DADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQtVSVGVQDQGIGIAENKKKSLFVRFenlVDSSLFNQSSSGIGLSL 1139
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEITVTLSEGGE-LTLTVEDNGIGIPPEDLPRIFEPF---STADKRGGGGTGLGLSI 77
                           90       100
                   ....*....|....*....|....*.
gi 1119624474 1140 VKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:pfam02518   78 VRKLVELLGGTITVESEPGGGTTVTL 103
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
1223-1339 8.96e-22

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 95.32  E-value: 8.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTAK 1301
Cdd:NF040689     2 LVVDDDPALAEMLGIVLRAEgFETVFCADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIR---AESGVPIIMLTAK 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1302 TAIESMLEGLEYGADDYITKPFSATYLKARVRNILERR 1339
Cdd:NF040689    79 SDTVDVVRGLEAGADDYVVKPFKPKELVARIRARLRRS 116
pleD PRK09581
response regulator PleD; Reviewed
1243-1342 1.14e-21

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 99.98  E-value: 1.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1243 FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTAKTAIESMLEGLEYGADDYITKP 1322
Cdd:PRK09581    27 YTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKP 106
                           90       100
                   ....*....|....*....|
gi 1119624474 1323 FSATYLKARVRNiLERRKKL 1342
Cdd:PRK09581   107 INDVALFARVKS-LTRLKMV 125
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
934-1165 4.14e-21

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 98.94  E-value: 4.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  934 LKHRVAMEQQLTHMKLRFFTDISHELRTPLTLI--TGPLEYvLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQ 1011
Cdd:NF040691   257 LQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIrmAADVIH-DSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFD 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1012 NKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTpEGKMITVFVHD 1091
Cdd:NF040691   336 AGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHG-EGKPVVVTVAQ 414
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1092 NGQTVSVGVQDQGIGIAENKKKSLFVRFENlVDSSLFNQS-SSGIGLSLVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:NF040691   415 DDTAVAVTVRDHGVGLKPGEVALVFDRFWR-ADPARARTTgGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRL 488
HTH_18 pfam12833
Helix-turn-helix domain;
1399-1478 8.06e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 84.95  E-value: 8.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1399 LVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQ-LIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEYRD 1477
Cdd:pfam12833    1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRlLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80

                   .
gi 1119624474 1478 R 1478
Cdd:pfam12833   81 R 81
resp_reg_YycF NF040534
response regulator YycF;
1243-1352 9.53e-20

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 89.78  E-value: 9.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1243 FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTAK-TAIESMLeGLEYGADDYITK 1321
Cdd:NF040534    25 YEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVR---KKYDMPIIMLTAKdSEIDKVL-GLELGADDYVTK 100
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1119624474 1322 PFSATYLKARVRNILERRKKLQEMYREKLMN 1352
Cdd:NF040534   101 PFSTRELIARVKANLRRHQQQNTEEEEEENN 131
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
955-1165 6.45e-18

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 87.36  E-value: 6.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLEYVLQNTKLPAEA--REQLQVVERNSNrmlrLVNQILDFRKIQNKKMKMQVQRLEIVAFVRKIM 1032
Cdd:NF012226   145 IAHELRTPITILQGRLQGILDGVFEPDPAlfKSLLNQVEGLSH----LVEDLRTLSLVENQQLRLNYESVDLKDSIEKVL 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1033 DNFEAVAEEHHIDFVFETEKEAVYlwVDADKFEKIVYNLLSNAFKYTPEGKM-ITVFVHDNGQTVSvgVQDQGIGIAENK 1111
Cdd:NF012226   221 KMFEDRLEQAQLTIVLNLTATPVF--CDRRRIEQVLIALIDNAIRYANAGKLkISSSVIQDDWILQ--IEDEGPGIAEEY 296
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1119624474 1112 KKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMHKASITVdSKLGEGSCFKV 1165
Cdd:NF012226   297 QQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFTI 349
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
947-1162 2.22e-17

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 86.80  E-value: 2.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  947 MKLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEaREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVA 1026
Cdd:NF012163   239 MRRDFMADISHELRTPLAVLRAELE-AIQDGIRKFT-PESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVP 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1027 FVRKIMDNFEAVAEEHHIDFVFETEkEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIG 1106
Cdd:NF012163   317 LLEVEGGAFRERFASAGLELEVSLP-DSSLVFGDRDRLMQLFNNLLENSLRYTDSGGSLHISASQRPKEVTLTVADSAPG 395
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1119624474 1107 IAENKKKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMHKASITVD-SKLGEGSC 1162
Cdd:NF012163   396 VSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAhSPLGGLRI 452
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1223-1273 1.81e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 63.36  E-value: 1.81e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1119624474  1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMP 1273
Cdd:smart00448    4 LVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
1430-1483 1.32e-08

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 58.06  E-value: 1.32e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1119624474 1430 RINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEYRDRKAGKN 1483
Cdd:PRK10572   236 RISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEKN 289
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
91-340 4.03e-05

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 46.94  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474   91 DRYGFIWL-QTYDDRAFRFDPRTEVFESVPaegePGSQTAISSIKVLPDGTVWLLTRREGAV-RITTDSTDYRLTSVwys 168
Cdd:COG4257     25 DPDGAVWFtDQGGGRIGRLDPATGEFTEYP----LGGGSGPHGIAVDPDGNLWFTDNGNNRIgRIDPKTGEITTFAL--- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  169 PASERLRVSRVFDvcqADGAEWVLSDNG--------------------------LVCFTPDGAepvIYFenAEEGKDSFK 222
Cdd:COG4257     98 PGGGSNPHGIAFD---PDGNLWFTDQGGnrigrldpatgevtefplptggagpyGIAVDPDGN---LWV--TDFGANAIG 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  223 KrqsfyvmedcgdcllFGSGNGTVWVYRKKDRTFRPVQLDAAS--RIsgikhlkklsqVVVATVSDGFFVYDLPTGRTEH 300
Cdd:COG4257    170 R---------------IDPDTGTLTEYALPTPGAGPRGLAVDPdgNL-----------WVADTGSGRIGRFDPKTGTVTE 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1119624474  301 YAASRLPAEKVkSIYRDLSDEIWFEQDVVGEVAHFNPYTR 340
Cdd:COG4257    224 YPLPGGGARPY-GVAVDGDGRVWFAESGANRIVRFDPDTE 262
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
3-1186 5.15e-86

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 302.68  E-value: 5.15e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474    3 QRWLLWMLAVLTAAVLKAQPEGSFTHYSSDDGLSENTVMDMLQDSRGNMWFSTWNGINKFDGYTFKTFKARQDNQIALTS 82
Cdd:COG3292      1 KRLLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474   83 NRVDNMKLDRYGFIWLQTyDDRAFRFDPRTEVFESVPAEGEPgSQTAISSIKVLPDGTVWLLTrregavrittdstdyrl 162
Cdd:COG3292     81 NYIRALLEDSDGRLWIGT-DGGLSRYDPKTDKFTRYPLDPGL-PNNSIRSIAEDSDGNIWVGT----------------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  163 tsvwyspaserlrvsrvfdvcqadgaewvlsdnglvcftpdgaepviyfenaeegkdsfkkrqsfyvmedcgdcllfgsg 242
Cdd:COG3292        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  243 ngtvwvyrkkdrtfrpvqldaasrisgikhlkklsqvvvatvSDGFFVYDLPTGRTEHYAASRLPAEKVKSIYRDLSDEI 322
Cdd:COG3292    142 ------------------------------------------SNGLYRYDPKTGKFKRFTLDGLPSNTITSLAEDADGNL 179
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  323 WFEQDvvgevahfnpytrklkcekvyaeptntdrsrpafhihedifGTLWVHPYGGGFSYFDRKNNCLRPFYNSmTGENW 402
Cdd:COG3292    180 WVDSD-----------------------------------------GNLWIGTDGNGLYRLDPNTGKFEHITHD-PDPNS 217
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  403 RFSNKIHSAFSDRQGNLWMCTHSKGLEKVTFRTDRFRLKVPVNHsyESLS-NEVRALCEDKDGNMWVglkdgmlrvynrh 481
Cdd:COG3292    218 LSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRHNDP--NGLSgNSVRSIAEDSDGNLWI------------- 282
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  482 reeigylteagtvshsgkplfgntyfvmqdshdNLWIATKGAGVVKAEPLPGTLRyrltryRYSADdvySLSDDNVYCLY 561
Cdd:COG3292    283 ---------------------------------RLWIGTYGGGLFRLDPKTGKFK------RYNPN---GLPSNSVYSIL 320
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  562 EDRRGRIWVATFANGISYLTRNADGkevfISHRNNLKGFPIKYcskVRCITGDADGHIWIGTTVGLLMVDdgfdrPEDAR 641
Cdd:COG3292    321 EDSDGNLWIGTSGGGLYRYDPKTGK----FTKFSEDNGLSNNF---IRSILEDSDGNLWVGTNGGLYRLD-----PKTGK 388
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  642 FYHYLRAPEKaNALSNNDIHWVKPTREGELYVATFGGGLNQlvdLNAEGQaRFKAYTVRDGLPSDILLSIQEDKKGQLWI 721
Cdd:COG3292    389 FTNFTHDPDK-NGLSSNYINSIFEDSDGRLWIGTDGGGLYR---YDPKTG-KFKHFTTKDGLPSNTIYSILEDDNGNLWN 463
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  722 STENGLSKFTPGLGRFENFQNKYSNSSIRFSeaasayasdgNILFGTNHGIFYFNPDSIQKSVYVPPIvltqlllanesv 801
Cdd:COG3292    464 FNSASNLGLLSLLGGLLGGLNLGNAIKLPLS----------NLGLLLTLLLLGINLSLVRSLISLLTL------------ 521
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  802 kpgphsVLKYTLDDTRELTLSHQENIFSIQYAALDYTNPSDIQYAYMLDGFEKNWNYVGKQRTATYTNLPKGHYVFKVRS 881
Cdd:COG3292    522 ------LLLALLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLL 595
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  882 TNADGVWSDNVRTLDIEVLPSFWETPLAYFLYVLFFLLIIVTAVYILFTIYRLKHRVAMEQQLTHMKLRFFTDISHELRT 961
Cdd:COG3292    596 LLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELIL 675
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  962 PLTLITGPLEYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQ-VQRLEIVAFVRKIMDNFEAVAE 1040
Cdd:COG3292    676 ELLLILLLLLLLLLLALLLLLLLLLALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLlLLILLIILLLLILLEELLLAND 755
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1041 EHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFE 1120
Cdd:COG3292    756 IELEGILLLILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLD 835
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1121 NLVDSSLFNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDFQKGKEHYDETVEFLQNDVE 1186
Cdd:COG3292    836 ILELILLELELGLLLGLLLLLLLEILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLA 901
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
361-1293 6.49e-77

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 275.71  E-value: 6.49e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  361 FHIHEDIFGTLWVhpyG--GGFSYFDRKNncLRPFYNSMTGENWRFSNKIHSAFSDRQGNLWMCThSKGLEKVTFRTDRF 438
Cdd:COG3292     39 NSIAQDSDGFLWI---GteDGLNRYDGYE--FKVFRHDPGDPNSLPSNYIRALLEDSDGRLWIGT-DGGLSRYDPKTDKF 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  439 RlkvPVNHSYESLSNEVRALCEDKDGNMWVGLKDGMLRvYNRHREEIGYLTEAGTVSHSGKPLF---GNTYFVmqDSHDN 515
Cdd:COG3292    113 T---RYPLDPGLPNNSIRSIAEDSDGNIWVGTSNGLYR-YDPKTGKFKRFTLDGLPSNTITSLAedaDGNLWV--DSDGN 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  516 LWIATKGAGVVKAEPLPGtlryRLTRYRYSaDDVYSLSDDNVYCLYEDRRGRIWVATFANGISYLTRNadgKEVFISHRN 595
Cdd:COG3292    187 LWIGTDGNGLYRLDPNTG----KFEHITHD-PDPNSLSSNSIYSLFEDREGNLWVGTYGGGLNYLDPN---NSKFKSYRH 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  596 NLK-GFPIKYcskVRCITGDADG----HIWIGT-TVGLLMVDdgfdrPEDARFYHYlrapeKANALSNNDIHWVKPTREG 669
Cdd:COG3292    259 NDPnGLSGNS---VRSIAEDSDGnlwiRLWIGTyGGGLFRLD-----PKTGKFKRY-----NPNGLPSNSVYSILEDSDG 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  670 ELYVATFGGGLNQLVdlnaEGQARFKAYTVRDGLPSDILLSIQEDKKGQLWISTENGLSKFTPGLGRFENFQNKYSNSSI 749
Cdd:COG3292    326 NLWIGTSGGGLYRYD----PKTGKFTKFSEDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKTGKFTNFTHDPDKNGL 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  750 RFSEAASAY-ASDGNILFGTN-HGIFYFNPDSIQKSVYvppivLTQLLLANESVkpgpHSVLKytlDDtreltlshQENI 827
Cdd:COG3292    402 SSNYINSIFeDSDGRLWIGTDgGGLYRYDPKTGKFKHF-----TTKDGLPSNTI----YSILE---DD--------NGNL 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  828 FsIQYAALDYTNPSDIQYAYMLDGFEKNWNYVGKQRTATYTNLPKGHYVFKVRSTNADGVWSDNVRTLDIEVLPSFWETp 907
Cdd:COG3292    462 W-NFNSASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLALLLLLSLLLLLLLL- 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  908 LAYFLYVLFFLLIIVTAVYILFTIYRLKHRVAMEQQLTHMKLRFFTDISHELRTPLTLITGPLEYVLQNTKLPAEAREQL 987
Cdd:COG3292    540 LLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLL 619
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  988 QVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKI 1067
Cdd:COG3292    620 ILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLL 699
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1068 VYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMH 1147
Cdd:COG3292    700 LALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLELLLELALGL 779
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1148 KASITVDSKLGEGSCFKVDFQKGKEHYDETVEFLQNDVEqGGAKQEQQTAVEDNGASEGNKGEEGTENTDVRSTMLLVED 1227
Cdd:COG3292    780 ILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELA-ESVLIALEGLGKIDLLDILELILLELELGLLLGLLLLLLL 858
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1228 NTELRTFLRSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHI 1293
Cdd:COG3292    859 EILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALLIELLLEEEVLLALI 924
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
887-1167 1.21e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 240.20  E-value: 1.21e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  887 VWSDNVRTLDIEVLPSFWETPLAYFLYVLFFLLIIVTAVYILFTIYRLKHRVAMEQQlTHMKLRFFTDISHELRTPLTLI 966
Cdd:COG0642     50 LLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEA-NEAKSRFLANVSHELRTPLTAI 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  967 TGPLEYVLQNtkLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDF 1046
Cdd:COG0642    129 RGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIEL 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1047 VFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSS 1126
Cdd:COG0642    207 ELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSR 286
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1119624474 1127 lfNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:COG0642    287 --RGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
933-1167 1.47e-69

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 233.65  E-value: 1.47e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  933 RLKHRVAMEQQLTHMKLRFFTDISHELRTPLTLITGPLEYVLQNTKL-PAEAREQLQVVERNSNRMLRLVNQILDFRKIQ 1011
Cdd:COG2205      1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLsPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1012 NKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHD 1091
Cdd:COG2205     81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARR 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1092 NGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSlfNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:COG2205    161 EGDGVRISVSDNGPGIPEEELERIFERFYRGDNSR--GEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
883-1167 1.07e-66

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 230.98  E-value: 1.07e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  883 NADGVWSDNVRTLDIEVLPSFWETPLAYFLYVLFFLLIIVTAVYILFTIYRLKHR-VAMEQQLTHMKLRFFTDISHELRT 961
Cdd:COG5002     99 LALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERdITELERLEQMRREFVANVSHELRT 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  962 PLTLITGPLEYVLQN-TKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAFVRKIMDNFEAVAE 1040
Cdd:COG5002    179 PLTSIRGYLELLLDGaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAE 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1041 EHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFE 1120
Cdd:COG5002    259 EKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFY 338
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1119624474 1121 NlVDSSLFNQSS-SGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:COG5002    339 R-VDKSRSRETGgTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
941-1163 4.37e-42

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 164.54  E-value: 4.37e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  941 EQQLTHMKLR-FFTDISHELRTPLTLITGPLEYV----LQNTKLpaeAREQLQVVERNSNRMLRLVNQILDFRKIQNKKM 1015
Cdd:NF033092   364 EQEKIEQERReFVANVSHELRTPLTTMRSYLEALadgaWKDPEL---APRFLGVTQNETERMIRLVNDLLQLSRMDSKDY 440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1016 KMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQT 1095
Cdd:NF033092   441 KLNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGTITFRLLETHNR 520
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1096 VSVGVQDQGIGIAENKKKSLFVRFENlVD---SSlfNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCF 1163
Cdd:NF033092   521 IIISISDQGLGIPKKDLDKIFDRFYR-VDkarSR--KMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTI 588
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
942-1167 3.71e-41

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


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 155.06  E-value: 3.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  942 QQLTHMKLRFFTDISHELRTPLTLITGPLEYVLQNTKLPAEAREQ-LQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQ 1020
Cdd:TIGR02966  108 RRLEQMRRDFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWNRaLEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDE 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1021 RLEIVAFVRKIMDNFEAVAEEHHIDFVFETEkEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGV 1100
Cdd:TIGR02966  188 PVDMPALLDHLRDEAEALSQGKNHQITFEID-GGVDVLGDEDELRSAFSNLVSNAIKYTPEGGTITVRWRRDGGGAEFSV 266
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119624474 1101 QDQGIGIAENKKKSLFVRFENlVDSSLFNQSS-SGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:TIGR02966  267 TDTGIGIAPEHLPRLTERFYR-VDKSRSRDTGgTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1219-1341 2.40e-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: 2.40e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1219 RSTMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVL 1297
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPIIM 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKK 1341
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAA 122
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1215-1357 4.74e-38

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: 142.61  E-value: 4.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1215 NTDVRSTMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHI 1293
Cdd:COG3437      2 RTGQAPTVLIVDDDPENLELLRQLLRTLgYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119624474 1294 PMVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEMYREKLMNMATSP 1357
Cdd:COG3437     82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAP 145
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
934-1372 4.73e-37

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 152.24  E-value: 4.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  934 LKHRVAMEQ--QLTHMKLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQ 1011
Cdd:TIGR02956  448 KNHAKARAEaeEANRAKSAFLATMSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIE 526
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1012 NKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWV-DADKFEKIVYNLLSNAFKYTPEGKM-ITVFV 1089
Cdd:TIGR02956  527 AGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQgDGPRIRQVLINLVGNAIKFTDRGSVvLRVSL 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1090 HDNGQtVSVGVQDQGIGIAENKKKSLFVRFenlvdSSLFNQSSS---GIGLSLVKELVEMHKASITVDSKLGEGSCFKVd 1166
Cdd:TIGR02956  607 NDDSS-LLFEVEDTGCGIAEEEQATLFDAF-----TQADGRRRSggtGLGLAISQRLVEAMDGELGVESELGVGSCFWF- 679
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1167 fqkgkehydeTVEFLQNDVEQGGAkqeQQTAVEDNGASegnkgeegtentdvrstMLLVEDNTelrtfLRSIFASEF--- 1243
Cdd:TIGR02956  680 ----------TLPLTRGKPAEDSA---TLTVIDLPPQR-----------------VLLVEDNE-----VNQMVAQGFltr 724
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1244 ---RVVEAANGAEGLEKALSLVPDIIISDVMMPEKDG---LQMMRELHDnmTTSHIPMVLLTAKTAIESMLEGLEYGADD 1317
Cdd:TIGR02956  725 lghKVTLAESGQSALECFHQHAFDLALLDINLPDGDGvtlLQQLRAIYG--AKNEVKFIAFSAHVFNEDVAQYLAAGFDG 802
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1318 YITKPFSATYLKARVRNILErRKKLQEmyREKLMNMATSPDEPTVEESKAPEMSP 1372
Cdd:TIGR02956  803 FLAKPVVEEQLTAMIAVILA-GGKSNT--EAPVLSASPSFDSASVIENAQADDIP 854
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1219-1332 3.04e-36

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: 135.81  E-value: 3.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1219 RSTMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVL 1297
Cdd:COG3706      1 PARILVVDDDPTNRKLLRRLLEAAgYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARV 1332
Cdd:COG3706     81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
955-1172 3.42e-36

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 144.93  E-value: 3.42e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLEYVLQ--NTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVafVRKIM 1032
Cdd:COG4251    289 ASHDLREPLRKISGFSQLLEEdyGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQELEFEPVDLNEL--LEEVL 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1033 DNFEAVAEEHHIDFVFETEKEavyLWVDADKFEKIVYNLLSNAFKYTPEGKM--ITVFVHDNGQTVSVGVQDQGIGIAEN 1110
Cdd:COG4251    367 EDLEPRIEERGAEIEVGPLPT---VRGDPTLLRQVFQNLISNAIKYSRPGEPprIEIGAEREGGEWVFSVRDNGIGIDPE 443
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119624474 1111 KKKSLFVRFENLVDSSLFnqSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDFQKGKE 1172
Cdd:COG4251    444 YAEKIFEIFQRLHSRDEY--EGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAPA 503
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
955-1167 4.38e-35

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 139.71  E-value: 4.38e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLE-----YVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFrkiqNKKMKMQVQRLEIVAFVR 1029
Cdd:COG5000    208 IAHEIKNPLTPIQLSAErlrrkLADKLEEDREDLERALDTIIRQVDRLKRIVDEFLDF----ARLPEPQLEPVDLNELLR 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1030 KIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAE 1109
Cdd:COG5000    284 EVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDGRVRIEVSDNGPGIPE 363
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1110 NKKKSLFVRFenlvdsslF--NQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:COG5000    364 EVLERIFEPF--------FttKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL 415
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
945-1335 1.15e-34

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 144.88  E-value: 1.15e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  945 THMKLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAR-EQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLE 1023
Cdd:PRK09959   709 TVAKSQFLATMSHEIRTPISSIMGFLE-LLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVD 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1024 IVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLW-VDADKFEKIVYNLLSNAFKYTPEG--KMITVFVH--DNGQTVSV 1098
Cdd:PRK09959   788 IPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVkIDPQAFKQVLSNLLSNALKFTTEGavKITTSLGHidDNHAVIKM 867
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1099 GVQDQGIGIAENKKKSLFVRFENlvDSSLFNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDFqkgkehydeTV 1178
Cdd:PRK09959   868 TIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI---------PV 936
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1179 EFLQNdVEQGGAKQEQQTAVEDngasegnkgeegtentdvRSTMLLVEDNTELRTFL-RSIFASEFRVVEAANGAEGLEK 1257
Cdd:PRK09959   937 EISQQ-VATVEAKAEQPITLPE------------------KLSILIADDHPTNRLLLkRQLNLLGYDVDEATDGVQALHK 997
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119624474 1258 ALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNI 1335
Cdd:PRK09959   998 VSMQHYDLLITDVNMPNMDGFELTRKLREQ--NSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1223-1341 5.39e-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: 127.27  E-value: 5.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTAK 1301
Cdd:COG0784      9 LVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALTAY 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1119624474 1302 TAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKK 1341
Cdd:COG0784     89 ADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1223-1322 3.13e-33

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 124.06  E-value: 3.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMttSHIPMVLLTAK 1301
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1119624474 1302 TAIESMLEGLEYGADDYITKP 1322
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
948-1324 5.36e-32

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 135.07  E-value: 5.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  948 KLRFFTDISHELRTPLTLITGpLEYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAF 1027
Cdd:PRK11091   283 KTTFISTISHELRTPLNGIVG-LSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDF 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1028 VRKiMDNFEAV-AEEHHIDFVFE-TEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGI 1105
Cdd:PRK11091   362 LAD-LENLSGLqAEQKGLRFDLEpLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGI 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1106 GIAENKKKSLFVRFENlVDSSLFNQSS--SGIGLSLVKELVEMHKASITVDSKLGEGSCFkvdfqkgkehydeTVEFLQN 1183
Cdd:PRK11091   441 GIPEDELDKIFAMYYQ-VKDSHGGKPAtgTGIGLAVSKRLAQAMGGDITVTSEEGKGSCF-------------TLTIHAP 506
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1184 DVeqggAKQEQQTAVEDngasegnkgeegteNTDVRS-TMLLVEDnTELR-TFLRSIFASEFRVVEAA-NGAEGLEKALS 1260
Cdd:PRK11091   507 AV----AEEVEDAFDED--------------DMPLPAlNILLVED-IELNvIVARSVLEKLGNSVDVAmTGKEALEMFDP 567
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1261 LVPDIIISDVMMPEKDGLQMMRELHDNMTTSHI-PMVLLTAkTAIESMLEGLEYGADDYITKPFS 1324
Cdd:PRK11091   568 DEYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTA-NVLKDKKEYLDAGMDDVLSKPLS 631
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
940-1167 2.68e-31

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: 129.43  E-value: 2.68e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  940 MEQQLTHM---------KL-RFFTDISHELRTPLTLITGPLEYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRK 1009
Cdd:TIGR01386  223 LAQSFNAMlgrledafqRLsQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLESNLEELERLSRMVSDMLFLAR 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1010 IQNKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVylwVDADKFEKIVYNLLSNAFKYTPEGKMITVFV 1089
Cdd:TIGR01386  303 ADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR---GDPQMFRRAISNLLSNALRHTPDGGTITVRI 379
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119624474 1090 HDNGQTVSVGVQDQGIGIAENKKKSLFVRFENlVDSSLFN-QSSSGIGLSLVKELVEMHKASITVDSKLGEgSCFKVDF 1167
Cdd:TIGR01386  380 ERRSDEVRVSVSNPGPGIPPEHLSRLFDRFYR-VDPARSNsGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILRF 456
PRK15347 PRK15347
two component system sensor kinase;
948-1344 9.77e-31

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 131.69  E-value: 9.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  948 KLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAF 1027
Cdd:PRK15347   398 KSEHLTTISHEIRTPLNGVLGALE-LLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPL 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1028 VRKIMDNFEAVAEEHHIDF-VFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKmITVFVHDNGQTVSVGVQDQGIG 1106
Cdd:PRK15347   477 LDQAMLTIQGPAQSKSLTLrTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG-IRLRVKRHEQQLCFTVEDTGCG 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1107 IAENKKKSLFVRFENLVDsslfNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVD--FQKGKEHYDETVEF---- 1180
Cdd:PRK15347   556 IDIQQQQQIFTPFYQADT----HSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVlpLNEYAPPEPLKGELsapl 631
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1181 -LQNDVEQGGAKQE---QQTAVEDNGASE-------------GNKGEEGTENTDV---RSTMLLVEDNTELRTFLRSIFA 1240
Cdd:PRK15347   632 aLHRQLSAWGITCQpghQNPALLDPELAYlpgrlydllqqiiQGAPNEPVINLPLqpwQLQILLVDDVETNRDIIGMMLV 711
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1241 SEFRVVE-AANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHD--NMTTSHIPMVLLTAKTAIESMLEGLEYGADD 1317
Cdd:PRK15347   712 ELGQQVTtAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDdpNNLDPDCMIVALTANAAPEEIHRCKKAGMNH 791
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1119624474 1318 YITKPFS----ATYLKARVRNILERRKKLQE 1344
Cdd:PRK15347   792 YLTKPVTlaqlARALELAAEYQLLRGIELSP 822
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1221-1323 1.63e-29

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: 113.75  E-value: 1.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPF 1323
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
951-1157 1.92e-29

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 124.11  E-value: 1.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  951 FFTDISHELRTPLTLITGPLEYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAFVRK 1030
Cdd:PRK09835   265 FSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADEVGK 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1031 IMDNFEAVAEEHHIDFVFETEKEAVylWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAEN 1110
Cdd:PRK09835   345 VFDFFEAWAEERGVELRFVGDPCQV--AGDPLMLRRAISNLLSNALRYTPAGEAITVRCQEVDHQVQLVVENPGTPIAPE 422
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1119624474 1111 KKKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMHKASITVDSKL 1157
Cdd:PRK09835   423 HLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA 469
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1223-1322 2.14e-29

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: 113.09  E-value: 2.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTAK 1301
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLREL--PPDIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1119624474 1302 TAIESMLEGLEYGADDYITKP 1322
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
933-1165 2.81e-29

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 121.06  E-value: 2.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  933 RLKHRVAMEQQLTHM-KL----RFFTDISHELRTPLTLITGPLEYV---LQNTKLPAEAREQLQVVERNSNRMLRLVNQI 1004
Cdd:COG4191    122 AEEELRELQEQLVQSeKLaalgELAAGIAHEINNPLAAILGNAELLrrrLEDEPDPEELREALERILEGAERAAEIVRSL 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1005 LDFrkiqNKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGK- 1083
Cdd:COG4191    202 RAF----SRRDEEEREPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEGEg 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1084 -MITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFenlvdsslF----NQSSSGIGLSLVKELVEMHKASITVDSKLG 1158
Cdd:COG4191    278 gRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPF--------FttkpVGKGTGLGLSISYGIVEKHGGRIEVESEPG 349

                   ....*..
gi 1119624474 1159 EGSCFKV 1165
Cdd:COG4191    350 GGTTFTI 356
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1219-1344 3.82e-29

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: 121.99  E-value: 3.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1219 RSTMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVL 1297
Cdd:COG2204      2 MARILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRAL--DPDLPVIL 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQE 1344
Cdd:COG2204     80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRE 126
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
955-1177 8.09e-29

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 122.39  E-value: 8.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLEYVLQNTKlpAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMkmqvQRLEIVAFVRKIMDN 1034
Cdd:COG5809    277 IAHEIRNPLTSLKGFIQLLKDTID--EEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKY----EPKDLNTLIEEVIPL 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1035 FEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITV--FVHDNGQtVSVGVQDQGIGIAENKK 1112
Cdd:COG5809    351 LQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIetKAEDDDK-VVISVTDEGCGIPEERL 429
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119624474 1113 KSLFVRF----ENlvdsslfnqsSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDFQKGKEHYDET 1177
Cdd:COG5809    430 KKLGEPFyttkEK----------GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1060-1167 1.32e-28

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 111.20  E-value: 1.32e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  1060 DADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENlVDSSLFNQSSSGIGLSL 1139
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFR-TDKRSRKIGGTGLGLSI 80
                            90       100
                    ....*....|....*....|....*...
gi 1119624474  1140 VKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITL 108
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1223-1336 1.01e-27

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: 108.90  E-value: 1.01e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTAK 1301
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEgYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474 1302 -TAIESMLeGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd19937     81 gEEFDKVL-GLELGADDYITKPFSPRELLARVKAVL 115
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1223-1338 2.84e-27

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: 107.69  E-value: 2.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDN--MTtshiPMVLLT 1299
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEgiET----PVLLLT 76
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:cd17625     77 ALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRALLRR 115
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
926-1165 4.96e-27

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 114.56  E-value: 4.96e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  926 YILFTIYRLKHRVAMEQQLTHM-KLRFFTD----ISHELRTPLTLITGPLEYVLQNTKlPAEAREQLQVVERNSNRMLRL 1000
Cdd:COG3852    108 GVLLVLRDITERKRLERELRRAeKLAAVGElaagLAHEIRNPLTGIRGAAQLLERELP-DDELREYTQLIIEEADRLNNL 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1001 VNQILDFrkiqNKKMKMQVQRLEIVAFVRKIMDNFEAVAEeHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTP 1080
Cdd:COG3852    187 VDRLLSF----SRPRPPEREPVNLHEVLERVLELLRAEAP-KNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMP 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1081 EGKMITV----------FVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFenlvdsslF--NQSSSGIGLSLVKELVEMHK 1148
Cdd:COG3852    262 EGGTITIrtrverqvtlGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPF--------FttKEKGTGLGLAIVQKIVEQHG 333
                          250
                   ....*....|....*..
gi 1119624474 1149 ASITVDSKLGEGSCFKV 1165
Cdd:COG3852    334 GTIEVESEPGKGTTFRI 350
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
938-1163 6.06e-27

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 115.88  E-value: 6.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  938 VAMEQQLTHMKLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAREQ-LQVVERNSNRMLRLVNQILDFRKIQNKKMK 1016
Cdd:PRK11006   194 VTQMHQLEGARRNFFANVSHELRTPLTVLQGYLE-MMQDQPLEGALREKaLHTMREQTQRMEGLVKQLLTLSKIEAAPTI 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1017 MQVQRLEIVAFVRKIMDNFEAVAEEHHiDFVFETEKEavyLWV--DADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQ 1094
Cdd:PRK11006   273 DLNEKVDVPMMLRVLEREAQTLSQGKH-TITFEVDNS---LKVfgNEDQLRSAISNLVYNAVNHTPEGTHITVRWQRVPQ 348
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1095 TVSVGVQDQGIGIAENKKKSLFVRFENlVDSSLFNQS-SSGIGLSLVKELVEMHKASITVDSKLGEGSCF 1163
Cdd:PRK11006   349 GAEFSVEDNGPGIAPEHIPRLTERFYR-VDKARSRQTgGSGLGLAIVKHALSHHDSRLEIESEVGKGTRF 417
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1223-1333 6.65e-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: 106.47  E-value: 6.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTAK 1301
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRR--DPTTPVIILTAH 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1119624474 1302 TAIESMLEGLEYGADDYITKPFSATYLKARVR 1333
Cdd:pfam00072   80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
1220-1387 1.46e-26

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


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 109.34  E-value: 1.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1220 STMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLL 1298
Cdd:TIGR02154    3 RRILVVEDEPAIRELIAYNLEKAgYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPIIML 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEMYREKLMNMATSPDEPTVEESKAP-EMSPNDRKF 1377
Cdd:TIGR02154   83 TARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLRRIRPQLSDEVIEVGDLSLDPVAHRVFRGGQPlSLGPTEFRL 162
                          170
                   ....*....|
gi 1119624474 1378 MDKLMALMEK 1387
Cdd:TIGR02154  163 LHFFMTHPER 172
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1220-1336 1.65e-25

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: 102.71  E-value: 1.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1220 STMLLVEDNTELRTFLR-SIFASEFRVVEAANGaeglEKALSLV----PDIIISDVMMPEKDGLQMMRELHDNMTTSHIP 1294
Cdd:cd17618      1 RTILIVEDEPAIREMIAfNLERAGFDVVEAEDA----ESAVNLIveprPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIP 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1119624474 1295 MVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd17618     77 IIMLTARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1222-1338 2.56e-25

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 102.08  E-value: 2.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFL-RSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmTTSHIPMVLLTA 1300
Cdd:cd17627      1 ILVVDDDRAVRESLrRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:cd17627     79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALLRR 116
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1223-1323 3.47e-25

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: 101.05  E-value: 3.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTE----LRTFLRsifASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLL 1298
Cdd:cd19920      2 LIVDDVPDnlrlLSELLR---AAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFL 78
                           90       100
                   ....*....|....*....|....*
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPF 1323
Cdd:cd19920     79 TALTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1222-1338 3.51e-25

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: 101.61  E-value: 3.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmttSHIPMVLLTA 1300
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEgFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT---SQVPVLMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1301 K-TAIESMLeGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:cd17623     78 RgDDIDRIL-GLELGADDYLPKPFNPRELVARIRAILRR 115
PRK09303 PRK09303
histidine kinase;
931-1163 3.95e-25

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 109.27  E-value: 3.95e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  931 IYRLKH-RVAMEQQLtHMKLRFFTDISHELRTPLT-----LITGPLEYVLQNTKLPAEAREQLQVVERNSNR-MLRLVNQ 1003
Cdd:PRK09303   134 LFVLRQeNETLLEQL-KFKDRVLAMLAHDLRTPLTaaslaLETLELGQIDEDTELKPALIEQLQDQARRQLEeIERLITD 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1004 ILDFRKIQNKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGK 1083
Cdd:PRK09303   213 LLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGG 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1084 MITVFV-HDNGQTVSVGVQDQGIGIAENKKKSLFvrfENLV----DSSlfnQSSSGIGLSLVKELVEMHKASITVDSKLG 1158
Cdd:PRK09303   293 TITLSMlHRTTQKVQVSICDTGPGIPEEEQERIF---EDRVrlprDEG---TEGYGIGLSVCRRIVRVHYGQIWVDSEPG 366

                   ....*
gi 1119624474 1159 EGSCF 1163
Cdd:PRK09303   367 QGSCF 371
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1223-1322 4.60e-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: 4.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE--FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMttSHIPMVLLT 1299
Cdd:COG4753      3 LIVDDEPLIREGLKRILEWEagFEVVgEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELD--PDTKIIILS 80
                           90       100
                   ....*....|....*....|...
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKP 1322
Cdd:COG4753     81 GYSDFEYAQEAIKLGADDYLLKP 103
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1221-1338 1.19e-24

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: 100.12  E-value: 1.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLT 1299
Cdd:cd17615      1 RVLVVDDEPNITELLSMALRYEgWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:cd17615     79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLRR 117
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1223-1322 1.46e-24

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: 99.44  E-value: 1.46e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASEFRVVEAA-NGAEGLEKALSLVPDIIISDVMMPEKDGLQMMREL--HDNMTtshiPMVLLT 1299
Cdd:cd19935      2 LVVEDEKKLAEYLKKGLTEEGYAVDVAyDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLraAGKQT----PVLMLT 77
                           90       100
                   ....*....|....*....|...
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKP 1322
Cdd:cd19935     78 ARDSVEDRVKGLDLGADDYLVKP 100
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1222-1338 1.60e-24

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: 100.10  E-value: 1.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE---FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMttSHIPMVL 1297
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIDWEelgFEVVgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELY--PDIKIII 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1119624474 1298 LT-------AKTAIesmleglEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:cd17536     79 LSgyddfeyAQKAI-------RLGVVDYLLKPVDEEELEEALEKAKEE 119
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1222-1336 2.30e-24

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: 99.32  E-value: 2.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTA 1300
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1222-1338 3.77e-24

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: 98.65  E-value: 3.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmtTSHIPMVLLTA 1300
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEgYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRK---TSNVPIIMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1301 K-TAIESMLeGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:cd17614     78 KdSEVDKVL-GLELGADDYVTKPFSNRELLARVKANLRR 115
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1223-1336 6.05e-24

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: 98.39  E-value: 6.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLR---SIFASeFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:cd17552      5 LVIDDEEDIREVVQaclEKLAG-WEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd17552     84 AKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
933-1165 6.67e-24

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 108.52  E-value: 6.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  933 RLKHRVAMEQQLTHMKlRFFTDISHELRTPLTLITGPLEYVLQNTKLPaEAREQLQVVERNSNRMLRLVNQILDFrkiqN 1012
Cdd:PRK11360   376 RLQRRVARQERLAALG-ELVAGVAHEIRNPLTAIRGYVQIWRQQTSDP-PSQEYLSVVLREVDRLNKVIDQLLEF----S 449
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1013 KKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDN 1092
Cdd:PRK11360   450 RPRESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQY 529
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1093 GQT-VSVGVQDQGIGIAENKKKSLFVRFenlvdsslFN--QSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:PRK11360   530 SDGqVAVSIEDNGCGIDPELLKKIFDPF--------FTtkAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1396-1483 8.75e-24

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 102.55  E-value: 8.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1396 VDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEY 1475
Cdd:COG2207    171 LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250

                   ....*...
gi 1119624474 1476 RDRKAGKN 1483
Cdd:COG2207    251 RKRLRARA 258
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1223-1334 9.33e-24

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: 97.51  E-value: 9.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDN----TELRTFLRSIfaSEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLL 1298
Cdd:cd17551      4 LIVDDNptnlLLLEALLRSA--GYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRN 1334
Cdd:cd17551     82 TADTDREVRLRALEAGATDFLTKPFDPVELLARVRN 117
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
1396-1476 2.33e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 95.31  E-value: 2.33e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  1396 VDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEY 1475
Cdd:smart00342    4 LEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEY 83

                    .
gi 1119624474  1476 R 1476
Cdd:smart00342   84 R 84
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
1064-1168 3.46e-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: 95.64  E-value: 3.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1064 FEKIVYNLLSNAFKYTPEGKmITVFVH-----DNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSGIGLS 1138
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGE-VTLRVSleeeeEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLA 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1119624474 1139 LVKELVEMHKASITVDSKLGEGSCFKVDFQ 1168
Cdd:cd16922     80 ISKKLVELMGGDISVESEPGQGSTFTFTLP 109
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
957-1154 3.98e-23

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 104.93  E-value: 3.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  957 HELRTPLTLITGPLEyVLQnTKLPAEAREQ-LQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAFVRKIMDNF 1035
Cdd:PRK11100   265 HELKSPLAAIRGAAE-LLQ-EDPPPEDRARfTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAR 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1036 EAVAEEHHIDFVFETEKeavyLWVDADKF--EKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKK 1113
Cdd:PRK11100   343 EAQAAAKGITLRLRPDD----ARVLGDPFllRQALGNLLDNAIDFSPEGGTITLSAEVDGEQVALSVEDQGPGIPDYALP 418
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1119624474 1114 SLFVRFENLV--DSSlfnQSSSGIGLSLVKELVEMHKASITVD 1154
Cdd:PRK11100   419 RIFERFYSLPrpANG---RKSTGLGLAFVREVARLHGGEVTLR 458
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1223-1350 6.16e-23

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 96.19  E-value: 6.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFA--SEFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLT 1299
Cdd:COG4565      7 LIVEDDPMVAELLRRYLErlPGFEVVgVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRAR--GPDVDVIVIT 84
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEMYREKL 1350
Cdd:COG4565     85 AARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDL 135
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
1060-1165 1.81e-22

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: 93.59  E-value: 1.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1060 DADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQtVSVGVQDQGIGIAENKKKSLFVRFenlVDSSLFNQSSSGIGLSL 1139
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEITVTLSEGGE-LTLTVEDNGIGIPPEDLPRIFEPF---STADKRGGGGTGLGLSI 77
                           90       100
                   ....*....|....*....|....*.
gi 1119624474 1140 VKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:pfam02518   78 VRKLVELLGGTITVESEPGGGTTVTL 103
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
1223-1339 8.96e-22

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 95.32  E-value: 8.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTAK 1301
Cdd:NF040689     2 LVVDDDPALAEMLGIVLRAEgFETVFCADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIR---AESGVPIIMLTAK 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1302 TAIESMLEGLEYGADDYITKPFSATYLKARVRNILERR 1339
Cdd:NF040689    79 SDTVDVVRGLEAGADDYVVKPFKPKELVARIRARLRRS 116
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1221-1336 9.57e-22

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: 91.67  E-value: 9.57e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRS-IFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmtTSHIPMVLLT 1299
Cdd:cd19938      1 RILIVEDEPKLAQLLIDyLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRR---FSDVPIIMVT 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd19938     78 ARVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
pleD PRK09581
response regulator PleD; Reviewed
1243-1342 1.14e-21

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 99.98  E-value: 1.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1243 FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTAKTAIESMLEGLEYGADDYITKP 1322
Cdd:PRK09581    27 YTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKP 106
                           90       100
                   ....*....|....*....|
gi 1119624474 1323 FSATYLKARVRNiLERRKKL 1342
Cdd:PRK09581   107 INDVALFARVKS-LTRLKMV 125
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1220-1338 1.88e-21

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 94.49  E-value: 1.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1220 STMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmtTSHIPMVLL 1298
Cdd:PRK10529     2 TNVLIVEDEQAIRRFLRTALEGDgMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQ---WSAIPVIVL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK10529    79 SARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRR 118
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
1060-1165 1.88e-21

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: 91.01  E-value: 1.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1060 DADKFEKIVYNLLSNAFKYTPEGKMITVFVH-DNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSGIGLS 1138
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEkFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLS 80
                           90       100
                   ....*....|....*....|....*..
gi 1119624474 1139 LVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:cd16925     81 IVKEFVELHGGTVTVSDAPGGGALFQV 107
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
934-1165 4.14e-21

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 98.94  E-value: 4.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  934 LKHRVAMEQQLTHMKLRFFTDISHELRTPLTLI--TGPLEYvLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQ 1011
Cdd:NF040691   257 LQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIrmAADVIH-DSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFD 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1012 NKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTpEGKMITVFVHD 1091
Cdd:NF040691   336 AGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHG-EGKPVVVTVAQ 414
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1092 NGQTVSVGVQDQGIGIAENKKKSLFVRFENlVDSSLFNQS-SSGIGLSLVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:NF040691   415 DDTAVAVTVRDHGVGLKPGEVALVFDRFWR-ADPARARTTgGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRL 488
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
937-1333 5.85e-21

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 100.05  E-value: 5.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  937 RVAMEQQLTHM----------KLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILD 1006
Cdd:PRK10841   426 RVKMEESLQEMaqaaeqasqsKSMFLATVSHELRTPLYGIIGNLD-LLQTKELPKGVDRLVTAMNNSSSLLLKIISDILD 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1007 FRKIQNKKMKMQVQRLEIVAFVRKIMDNFEA-VAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGkMI 1085
Cdd:PRK10841   505 FSKIESEQLKIEPREFSPREVINHITANYLPlVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTG-CI 583
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1086 TVFVHDNGQTVSVGVQDQGIGIAEnkkKSLFVRFENLVDSSLFNQSSS---GIGLSLVKELVEMHKASITVDSKLGEGSC 1162
Cdd:PRK10841   584 VLHVRVDGDYLSFRVRDTGVGIPA---KEVVRLFDPFFQVGTGVQRNFqgtGLGLAICEKLINMMDGDISVDSEPGMGSQ 660
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1163 FKV-------DFQKGKEHYDET-------------VEFLQ--------------------NDV----------------- 1185
Cdd:PRK10841   661 FTIriplygaQYPQKKGVEGLQgkrcwlavrnaslEQFLEtllqrsgiqvqryegqeptpEDVlitddpvqkkwqgravi 740
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1186 ----EQGGAKQEQQT-------------------------AVEDNGASEGNKGEEGTENTDVRstMLLVEDNTELRTFLR 1236
Cdd:PRK10841   741 tfcrRHIGIPLEIAPgewvhstatphelpallariyrielESDDSANALPSTDKAVSDNDDMM--ILVVDDHPINRRLLA 818
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1237 SIFAS-EFRVVEAANGAEGLEkALSLVP-DIIISDVMMPEKDGL---QMMRELhdNMTtshIPMVLLTAKTAIESMLEGL 1311
Cdd:PRK10841   819 DQLGSlGYQCKTANDGVDALN-VLSKNHiDIVLTDVNMPNMDGYrltQRLRQL--GLT---LPVIGVTANALAEEKQRCL 892
                          490       500
                   ....*....|....*....|....*....
gi 1119624474 1312 EYGADDYITKPFSATYLK-------ARVR 1333
Cdd:PRK10841   893 EAGMDSCLSKPVTLDVLKqtltvyaERVR 921
PRK11173 PRK11173
two-component response regulator; Provisional
1223-1365 5.94e-21

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 93.54  E-value: 5.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEgLEKALSLVP-DIIISDVMMPEKDGLQMMRELHDNmttSHIPMVLLTA 1300
Cdd:PRK11173     7 LIVEDELVTRNTLKSIFEAEgYDVFEATDGAE-MHQILSENDiNLVIMDINLPGKNGLLLARELREQ---ANVALMFLTG 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1301 K-TAIESMLeGLEYGADDYITKPFSATYLKARVRNILERrkklqemyrekLMNMATSPDEPTVEES 1365
Cdd:PRK11173    83 RdNEVDKIL-GLEIGADDYITKPFNPRELTIRARNLLSR-----------TMNLGTVSEERRSVES 136
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1223-1326 7.24e-21

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: 89.76  E-value: 7.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFAS--EFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELhdnMTTSHIPMVLLT 1299
Cdd:cd17541      4 LIVDDSAVMRKLLSRILESdpDIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRI---MAERPTPVVMVS 80
                           90       100
                   ....*....|....*....|....*....
gi 1119624474 1300 AKTAIESM--LEGLEYGADDYITKPFSAT 1326
Cdd:cd17541     81 SLTEEGAEitLEALELGAVDFIAKPSGGI 109
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1223-1336 8.01e-21

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: 89.08  E-value: 8.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTAK 1301
Cdd:cd17624      2 LLVEDDALLGDGLKTGLRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQ--GQSLPVLILTAR 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1119624474 1302 TAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd17624     80 DGVDDRVAGLDAGADDYLVKPFALEELLARLRALL 114
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1222-1338 9.90e-21

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 92.94  E-value: 9.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGaeglEKALSLVP---DIIISDVMMPEKDGLQMMRELHDNMTTshiPMVL 1297
Cdd:PRK10955     4 ILLVDDDRELTSLLKELLEMEgFNVIVAHDG----EQALDLLDdsiDLLLLDVMMPKKNGIDTLKELRQTHQT---PVIM 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK10955    77 LTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRR 117
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1223-1322 2.32e-20

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: 87.22  E-value: 2.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTAK 1301
Cdd:cd17620      2 LVIEDEPQIRRFLRTALEAHgYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSAR 78
                           90       100
                   ....*....|....*....|.
gi 1119624474 1302 TAIESMLEGLEYGADDYITKP 1322
Cdd:cd17620     79 DEESDKIAALDAGADDYLTKP 99
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1222-1336 2.86e-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: 87.82  E-value: 2.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFAS-EFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmtTSHIPMVLLTA 1300
Cdd:cd17622      3 ILLVEDDPKLARLIADFLEShGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRP---KYQGPILLLTA 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd17622     80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
Y_Y_Y pfam07495
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ...
836-900 2.93e-20

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: 85.87  E-value: 2.93e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474  836 DYTNPSDIQYAYMLDGFEKNWNYVGKQRTATYTNLPKGHYVFKVRSTNADGVWSDNVRTLDIEVL 900
Cdd:pfam07495    1 NYDGPENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSYDDASLNFTIL 65
orf27 CHL00148
Ycf27; Reviewed
1222-1341 3.32e-20

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 91.32  E-value: 3.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFA-SEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTA 1300
Cdd:CHL00148     9 ILVVDDEAYIRKILETRLSiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR---KESDVPIIMLTA 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKK 1341
Cdd:CHL00148    86 LGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNK 126
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
939-1172 3.76e-20

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 94.53  E-value: 3.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  939 AMEQQLTHMK-----LRFFTdisHELRTPLTLITGPLEyvlqnTKLPAEAREQLQVVERNSNRMLRLVnqildFRKIQNK 1013
Cdd:COG3290    178 RLEEELEGVKelaeaLRAQR---HDFRNHLHTISGLLQ-----LGEYDEALEYIDEISEELQELIDSL-----LSRIGNP 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1014 kmkmqvqrlEIVAFV-RKImdnfeAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAF----KYTPEGKMITVF 1088
Cdd:COG3290    245 ---------VLAALLlGKA-----ARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIeaveKLPEEERRVELS 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1089 VHDNGQTVSVGVQDQGIGIAENKKKSLFVRfenlvdsslfNQSS-----SGIGLSLVKELVEMHKASITVDSKLGEGSCF 1163
Cdd:COG3290    311 IRDDGDELVIEVEDSGPGIPEELLEKIFER----------GFSTklgegRGLGLALVKQIVEKYGGTIEVESEEGEGTVF 380

                   ....*....
gi 1119624474 1164 KVDFQKGKE 1172
Cdd:COG3290    381 TVRLPKEGE 389
ompR PRK09468
osmolarity response regulator; Provisional
1215-1339 5.04e-20

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 90.80  E-value: 5.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1215 NTDVRSTMLLVEDNTELRTFLRSIFASE-FRVVEAANgAEGLEKALSL-VPDIIISDVMMPEKDGLQMMRELHDNmtTSH 1292
Cdd:PRK09468     1 MMQENYKILVVDDDMRLRALLERYLTEQgFQVRSAAN-AEQMDRLLTReSFHLMVLDLMLPGEDGLSICRRLRSQ--NNP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1119624474 1293 IPMVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERR 1339
Cdd:PRK09468    78 TPIIMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQ 124
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1221-1324 6.22e-20

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: 86.44  E-value: 6.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                           90       100
                   ....*....|....*....|....*...
gi 1119624474 1300 A---KTAIESMLEGleyGADDYITKPFS 1324
Cdd:cd17548     81 AyamKGDREKILEA---GCDGYISKPID 105
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
1380-1478 6.28e-20

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: 92.53  E-value: 6.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1380 KLMALMEKNLDNgDLIVDDLVKDMAVSRSVF---FKKLkslTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGIND 1456
Cdd:COG4977    214 RAQAWMEANLEE-PLSVDELARRAGMSPRTLerrFRAA---TGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGS 289
                           90       100
                   ....*....|....*....|..
gi 1119624474 1457 PRYFSKCFKQKMGMTPTEYRDR 1478
Cdd:COG4977    290 ASHFRRAFRRRFGVSPSAYRRR 311
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1215-1344 7.68e-20

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 90.51  E-value: 7.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1215 NTDVRSTMLLVEDNTELRTFLRSIF-ASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHI 1293
Cdd:PRK10710     6 IDENTPRILIVEDEPKLGQLLIDYLqAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR---RFSDI 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1294 PMVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQE 1344
Cdd:PRK10710    83 PIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRE 133
HTH_18 pfam12833
Helix-turn-helix domain;
1399-1478 8.06e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 84.95  E-value: 8.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1399 LVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQ-LIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEYRD 1477
Cdd:pfam12833    1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRlLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80

                   .
gi 1119624474 1478 R 1478
Cdd:pfam12833   81 R 81
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1222-1334 9.22e-20

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: 86.29  E-value: 9.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmttSHIPMVLLTA 1300
Cdd:cd17619      3 ILIVEDEPVTRATLKSYFEQEgYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ---SEVGIILVTG 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRN 1334
Cdd:cd17619     80 RDDEVDRIVGLEIGADDYVTKPFNPRELLVRAKN 113
resp_reg_YycF NF040534
response regulator YycF;
1243-1352 9.53e-20

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 89.78  E-value: 9.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1243 FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTAK-TAIESMLeGLEYGADDYITK 1321
Cdd:NF040534    25 YEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVR---KKYDMPIIMLTAKdSEIDKVL-GLELGADDYVTK 100
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1119624474 1322 PFSATYLKARVRNILERRKKLQEMYREKLMN 1352
Cdd:NF040534   101 PFSTRELIARVKANLRRHQQQNTEEEEEENN 131
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1222-1338 2.28e-19

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 85.03  E-value: 2.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASEFRVVE-AANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTshIPMVLLTA 1300
Cdd:cd19934      1 LLLVEDDALLAAQLKEQLSDAGYVVDvAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--TPVLILTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:cd19934     79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALIRR 116
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1220-1333 3.08e-19

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 84.83  E-value: 3.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1220 STMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmtTSHIPMVLL 1298
Cdd:cd17626      1 ARILVVDDDAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA---ESGVPIVML 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVR 1333
Cdd:cd17626     78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1222-1387 3.74e-19

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 88.24  E-value: 3.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTA 1300
Cdd:PRK10161     5 ILVVEDEAPIREMVCFVLEQNgFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERrkkLQEMYREKLMNMATSPDEPT---VEESKAP-EMSPNDRK 1376
Cdd:PRK10161    85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRR---ISPMAVEEVIEMQGLSLDPTshrVMAGEEPlEMGPTEFK 161
                          170
                   ....*....|.
gi 1119624474 1377 FMDKLMALMEK 1387
Cdd:PRK10161   162 LLHFFMTHPER 172
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1222-1338 5.04e-19

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 83.96  E-value: 5.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRS-IFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmttSHIPMVLLTA 1300
Cdd:cd19939      2 ILIVEDELELARLTRDyLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILMLTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:cd19939     79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR 116
PRK11517 PRK11517
DNA-binding response regulator HprR;
1222-1338 8.91e-19

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 86.88  E-value: 8.91e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASEFRVVEAA-NGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTA 1300
Cdd:PRK11517     3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVsDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR---TAKQTPVICLTA 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK11517    80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQ 117
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1221-1336 1.37e-18

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: 82.73  E-value: 1.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:cd17562      2 KILAVDDSASIRQMVSFTLRGAgYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd17562     82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
cztR_silR_copR TIGR01387
heavy metal response regulator; Members of this family contain a response regulator receiver ...
1222-1338 1.42e-18

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


Pssm-ID: 130454 [Multi-domain]  Cd Length: 218  Bit Score: 86.01  E-value: 1.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASEFRVVEAA-NGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTShiPMVLLTA 1300
Cdd:TIGR01387    1 ILVVEDEQKTAEYLQQGLSESGYVVDAAsNGRDGLHLALKDDYDLIILDVMLPGMDGWQILQTLRRSGKQT--PVLFLTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:TIGR01387   79 RDSVADKVKGLDLGADDYLVKPFSFSELLARVRTLLRR 116
PRK10766 PRK10766
two-component system response regulator TorR;
1221-1338 1.66e-18

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 85.86  E-value: 1.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLT 1299
Cdd:PRK10766     4 HILVVEDEPVTRARLQGYFEQEgYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR---SRSTVGIILVT 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1119624474 1300 AKT-AIESMLeGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK10766    81 GRTdSIDRIV-GLEMGADDYVTKPLELRELLVRVKNLLWR 119
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
947-1012 2.74e-18

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 80.33  E-value: 2.74e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474  947 MKLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQN 1012
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLE-LLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEA 65
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1223-1330 2.83e-18

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 81.75  E-value: 2.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDN----TELRTFLRSIFaseFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELH-DNMTTSHIPMVL 1297
Cdd:cd17546      2 LVVDDNpvnrKVLKKLLEKLG---YEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIReLEGGGRRTPIIA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKA 1330
Cdd:cd17546     79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKE 111
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
955-1169 3.00e-18

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: 89.79  E-value: 3.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLEyVLQNTKlpAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQvqrlEIVAFVRKIMDN 1034
Cdd:COG5805    294 IAHEIRNPLTSIKGFLQ-LLQPGI--EDKEEYFDIMLSELDRIESIISEFLALAKPQAVNKEKE----NINELIQDVVTL 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1035 FEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKS 1114
Cdd:COG5805    367 LETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLKK 446
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1115 LFVRFENLvdsslfNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVDFQK 1169
Cdd:COG5805    447 LGEPFFTT------KEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
1367-1482 4.83e-18

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: 87.80  E-value: 4.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1367 APEMSPNDRKFMDKLMALMEKNLDnGDLIVDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEySMT 1446
Cdd:COG2169     75 LAPGSPPRADLVARACRLIEAGAE-DRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGL-SVT 152
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474 1447 QIAYMVGINDPRYFSKCFKQKMGMTPTEYRDRKAGK 1482
Cdd:COG2169    153 DAAYAAGFGSLSRFYEAFKKLLGMTPSAYRRGGAGA 188
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1222-1322 5.73e-18

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: 80.50  E-value: 5.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTA 1300
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLEDQgFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                           90       100
                   ....*....|....*....|..
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKP 1322
Cdd:cd19927     81 KGMTSDRIKGYNAGCDGYLSKP 102
PRK10490 PRK10490
sensor protein KdpD; Provisional
955-1165 5.93e-18

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 90.10  E-value: 5.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLEYVLQNtkLPAEAREQLQVVERNSNRML---RLVNQILDFRKIQNK--KMKMQVQRL-EIVAFV 1028
Cdd:PRK10490   671 LSHDLRTPLTVLFGQAEILTLD--LASEGSPHARQASEIRQQVLnttRLVNNLLDMARIQSGgfNLRKEWLTLeEVVGSA 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1029 RKIMDNFEAvaeEHHIDFvfETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIA 1108
Cdd:PRK10490   749 LQMLEPGLS---GHPINL--SLPEPLTLIHVDGPLFERVLINLLENAVKYAGAQAEIGIDAHVEGERLQLDVWDNGPGIP 823
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1109 ENKKKSLFVRFenlvdsSLFNQSSS----GIGLSLVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:PRK10490   824 PGQEQLIFDKF------ARGNKESAipgvGLGLAICRAIVEVHGGTIWAENRPEGGACFRV 878
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
947-1012 5.98e-18

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 79.15  E-value: 5.98e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474   947 MKLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQN 1012
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLE-LLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEA 65
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1221-1336 6.21e-18

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: 81.17  E-value: 6.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELhdNMTTSHIPMVLL 1298
Cdd:cd17542      2 KVLIVDDAAFMRMMLKDILTKAgYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEI--KKIDPNAKVIMC 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd17542     80 SAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
955-1165 6.45e-18

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 87.36  E-value: 6.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLEYVLQNTKLPAEA--REQLQVVERNSNrmlrLVNQILDFRKIQNKKMKMQVQRLEIVAFVRKIM 1032
Cdd:NF012226   145 IAHELRTPITILQGRLQGILDGVFEPDPAlfKSLLNQVEGLSH----LVEDLRTLSLVENQQLRLNYESVDLKDSIEKVL 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1033 DNFEAVAEEHHIDFVFETEKEAVYlwVDADKFEKIVYNLLSNAFKYTPEGKM-ITVFVHDNGQTVSvgVQDQGIGIAENK 1111
Cdd:NF012226   221 KMFEDRLEQAQLTIVLNLTATPVF--CDRRRIEQVLIALIDNAIRYANAGKLkISSSVIQDDWILQ--IEDEGPGIAEEY 296
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1119624474 1112 KKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMHKASITVdSKLGEGSCFKV 1165
Cdd:NF012226   297 QQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFTI 349
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1222-1337 1.04e-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: 80.25  E-value: 1.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE--FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmTTSHIPMVLL 1298
Cdd:cd17535      1 VLIVDDHPLVREGLRRLLESEpdIEVVgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIVL 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILE 1337
Cdd:cd17535     79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1223-1324 1.43e-17

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: 79.81  E-value: 1.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTAK 1301
Cdd:cd17580      2 LVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTGY 81
                           90       100
                   ....*....|....*....|...
gi 1119624474 1302 TAIESMLEGLEYGADDYITKPFS 1324
Cdd:cd17580     82 GQPEDRERALEAGFDAHLVKPVD 104
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
1223-1339 1.53e-17

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: 80.23  E-value: 1.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFA-SEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmTTSHIPMVLLTA- 1300
Cdd:cd17549      2 LLVDDDADVREALQQTLElAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRE--LDPDLPVILITGh 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1119624474 1301 ---KTAIESMLEgleyGADDYITKPFSATYLKARVRNILERR 1339
Cdd:cd17549     80 gdvPMAVEAMRA----GAYDFLEKPFDPERLLDVVRRALEKR 117
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
947-1162 2.22e-17

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 86.80  E-value: 2.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  947 MKLRFFTDISHELRTPLTLITGPLEyVLQNTKLPAEaREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVA 1026
Cdd:NF012163   239 MRRDFMADISHELRTPLAVLRAELE-AIQDGIRKFT-PESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVP 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1027 FVRKIMDNFEAVAEEHHIDFVFETEkEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIG 1106
Cdd:NF012163   317 LLEVEGGAFRERFASAGLELEVSLP-DSSLVFGDRDRLMQLFNNLLENSLRYTDSGGSLHISASQRPKEVTLTVADSAPG 395
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1119624474 1107 IAENKKKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMHKASITVD-SKLGEGSC 1162
Cdd:NF012163   396 VSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAhSPLGGLRI 452
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1223-1348 2.37e-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: 81.93  E-value: 2.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmttSHIPMVLLTA 1300
Cdd:COG3707      7 LVVDDEPLRRADLREGLREAgYEVVaEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEE---RPAPVILLTA 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEMYRE 1348
Cdd:COG3707     84 YSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRALRRE 131
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1222-1338 1.20e-16

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 80.74  E-value: 1.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFL-RSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmTTSHIPMVLLTA 1300
Cdd:PRK09836     3 LLIVEDEKKTGEYLtKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLLTA 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK09836    81 LGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRR 118
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
910-1166 1.76e-16

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 84.07  E-value: 1.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  910 YFLYVLFFLLIIVTAVYILFTIYRlKHRVAMEQQLTHMKLR--------FFTDISHELRTPLTLITGPLEYVLQNTKLPA 981
Cdd:PRK10364   192 NTLIILFALATVLLASLLAFFWYR-RYLRSRQLLQDEMKRKeklvalghLAAGVAHEIRNPLSSIKGLAKYFAERAPAGG 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  982 EAREQLQVVERNSNRMLRLVNQILDFrkiqNKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVYLWVDA 1061
Cdd:PRK10364   271 EAHQLAQVMAKEADRLNRVVSELLEL----VKPTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLPEIQADP 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1062 DKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFenlvdsslFNQSS--SGIGLSL 1139
Cdd:PRK10364   347 DRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPY--------FTTKAegTGLGLAV 418
                          250       260
                   ....*....|....*....|....*..
gi 1119624474 1140 VKELVEMHKASITVDSKLGEGSCFKVD 1166
Cdd:PRK10364   419 VHNIVEQHGGTIQVASQEGKGATFTLW 445
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1051-1160 2.08e-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: 76.68  E-value: 2.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1051 EKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVhDNGQTVSVGVQDQGIGIAENKKKSLFVRFenlVDSSLFNQ 1130
Cdd:cd16940      1 SAADIQVQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKL-SADDGAVIRVEDNGPGIDEEELEALFERF---YRSDGQNY 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 1119624474 1131 SSSGIGLSLVKELVEMHKASITVDSKLGEG 1160
Cdd:cd16940     77 GGSGLGLSIVKRIVELHGGQIFLGNAQGGG 106
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
1223-1363 5.79e-16

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


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 79.46  E-value: 5.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFAS--EFRVVEAA-NGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:COG5801      8 LIADDNREFCELLEEYLSSqpDMEVVGVAyNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLREMNLEKRPKVIMLT 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEMYREKLMNMATSPDEPTVE 1363
Cdd:COG5801     88 AFGQEDITQRAVELGADYYILKPFDLDVLAERIRQLAGGKAESETSKKKSSPETASVDKARDLE 151
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
947-1009 5.83e-16

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: 73.40  E-value: 5.83e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119624474  947 MKLRFFTDISHELRTPLTLITGPLEYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRK 1009
Cdd:cd00082      3 AKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
948-1163 6.35e-16

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 83.75  E-value: 6.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  948 KLRFFTDISHELRTPLTLITGPLEYVLQnTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMKmqvqrLEIVAF 1027
Cdd:PRK11107   293 KSEFLANMSHELRTPLNGVIGFTRQTLK-TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLV-----LENIPF 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1028 -VRKIMDnfEAV------AEEHHIDFVFETEKEAVYLWV-DADKFEKIVYNLLSNAFKYTPEGkMITVFVH-----DNGQ 1094
Cdd:PRK11107   367 sLRETLD--EVVtllahsAHEKGLELTLNIDPDVPDNVIgDPLRLQQIITNLVGNAIKFTESG-NIDILVElralsNTKV 443
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1095 TVSVGVQDQGIGIAENKKKSLFVRFeNLVDSSLfnqssS----GIGLSLV--KELVEMHKASITVDSKLGEGSCF 1163
Cdd:PRK11107   444 QLEVQIRDTGIGISERQQSQLFQAF-RQADASI-----SrrhgGTGLGLVitQKLVNEMGGDISFHSQPNRGSTF 512
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1221-1333 6.86e-16

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: 75.18  E-value: 6.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLT 1299
Cdd:cd17594      1 HVLVVDDDAAMRHLLILYLRERgFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR---ARSDVPIIIIS 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1119624474 1300 AKTAIES-MLEGLEYGADDYITKPFSATYLKARVR 1333
Cdd:cd17594     78 GDRRDEIdRVVGLELGADDYLAKPFGLRELLARVR 112
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1223-1349 8.06e-16

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 78.32  E-value: 8.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFA--SEFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIpmVLLT 1299
Cdd:COG3279      5 LIVDDEPLARERLERLLEkyPDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPI--IFTT 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1300 AKTaiESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEMYREK 1349
Cdd:COG3279     83 AYD--EYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASP 130
PRK10643 PRK10643
two-component system response regulator PmrA;
1222-1339 9.52e-16

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 78.15  E-value: 9.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASEFRVVE-AANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTshIPMVLLTA 1300
Cdd:PRK10643     3 ILIVEDDTLLLQGLILALQTEGYACDcASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYT--LPVLILTA 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERR 1339
Cdd:PRK10643    81 RDTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRH 119
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
934-1284 1.07e-15

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 83.03  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  934 LKHRVAMEQ--QLTHMKLRFFTDISHELRTPLTLITGPLEYVLQNTKLPAEaREQLQVVERNSNRMLRLVNQILDFRKIQ 1011
Cdd:PRK11466   428 IEHRQARAEaeKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQ-RDDLRAITDSGESLLTILNDILDYSAIE 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1012 --NKKMKMQVQRLEIVAFVRKIMDNFEAVAEEHHIDFVFETeKEAVYLWVDAD--KFEKIVYNLLSNAFKYTPEGkMITV 1087
Cdd:PRK11466   507 agGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDI-ADDLPTALMGDprRIRQVITNLLSNALRFTDEG-SIVL 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1088 FVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDsslfNQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKVdf 1167
Cdd:PRK11466   585 RSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCL-- 658
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1168 qkgkehydetveflqndveqggakqeqQTAVEDNGASEGNKGEEGTENTDVRstMLLVEDNT-ELRTFLRSIFASEFRVV 1246
Cdd:PRK11466   659 ---------------------------RLPLRVATAPVPKTVNQAVRLDGLR--LLLIEDNPlTQRITAEMLNTSGAQVV 709
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1119624474 1247 EAANGAEGLEK-ALSLVPDIIISDVMMPEKDGLQMMREL 1284
Cdd:PRK11466   710 AVGNAAQALETlQNSEPFAAALVDFDLPDYDGITLARQL 748
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1219-1345 1.46e-15

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 81.05  E-value: 1.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1219 RSTMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTShiPMVL 1297
Cdd:PRK11361     4 INRILIVDDEDNVRRMLSTAFALQgFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRT--PVIL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEM 1345
Cdd:PRK11361    82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEI 129
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1221-1341 2.15e-15

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 76.92  E-value: 2.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLrsIFA--SE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVL 1297
Cdd:PRK11083     5 TILLVEDEQAIADTL--VYAlqSEgFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAF--HPALPVIF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKK 1341
Cdd:PRK11083    81 LTARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTILRRVKK 124
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1223-1340 2.44e-15

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 73.77  E-value: 2.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDG---LQMMRELHDNmttshIPMVLL 1298
Cdd:cd17572      2 LLVEDSPSLAALYQEYLSDEgYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGmeiLKWIQERSLP-----TSVIVI 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRK 1340
Cdd:cd17572     77 TAHGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRK 118
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1055-1165 2.46e-15

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: 74.09  E-value: 2.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1055 VYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSG 1134
Cdd:cd16947     12 IYANANTEALQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNG 91
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1119624474 1135 IGLSLVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:cd16947     92 LGLTITKRLAESMGGSIYVNSKPYEKTVFTV 122
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1070-1163 2.46e-15

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 73.13  E-value: 2.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1070 NLLSNAFKYTPEG--KMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFnqSSSGIGLSLVKELVEMH 1147
Cdd:cd16921      7 NLLGNAIKFRRPRrpPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSREEY--EGTGVGLAIVRKIIERH 84
                           90
                   ....*....|....*.
gi 1119624474 1148 KASITVDSKLGEGSCF 1163
Cdd:cd16921     85 GGRIWLESEPGEGTTF 100
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1223-1336 2.47e-15

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: 73.53  E-value: 2.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASEF--RVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTA 1300
Cdd:cd19923      4 LVVDDFSTMRRIIKNLLKELGfnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVTA 83
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd19923     84 EAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1222-1336 2.82e-15

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 73.21  E-value: 2.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASEFRVVEAAN-GAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnMTTSHIPMVLLTA 1300
Cdd:cd17616      1 VLLIEDDSATAQSIELMLKSEGFNVYTTDlGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLR--LAKVKTPILILSG 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd17616     79 LADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1215-1321 3.45e-15

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 76.22  E-value: 3.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1215 NTDVRSTMLLVEDNTELRTFLRSI--FASEFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTS 1291
Cdd:PRK10651     2 SNQEPATILLIDDHPMLRTGVKQLisMAPDITVVgEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSG 81
                           90       100       110
                   ....*....|....*....|....*....|
gi 1119624474 1292 HIpmVLLTAKTAIESMLEGLEYGADDYITK 1321
Cdd:PRK10651    82 RI--VVFSVSNHEEDVVTALKRGADGYLLK 109
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1216-1333 4.43e-15

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: 74.95  E-value: 4.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1216 TDVRSTMLLVEDNTELRTFLRSIFAS-EFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGL---QMMRELHDNMtts 1291
Cdd:COG4567      1 SAEDRSLLLVDDDEAFARVLARALERrGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLdliEALRERDPDA--- 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1119624474 1292 hiPMVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVR 1333
Cdd:COG4567     78 --RIVVLTGYASIATAVEAIKLGADDYLAKPADADDLLAALE 117
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1224-1348 7.56e-15

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: 74.75  E-value: 7.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1224 LVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmTTSHIPMVLLTAK- 1301
Cdd:COG4566      4 IVDDDEAVRDSLAFLLESAgLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAA--RGSPLPVIFLTGHg 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1302 ---TAIESMLEgleyGADDYITKPFSATYLKARVRNILERRKKLQEMYRE 1348
Cdd:COG4566     82 dvpMAVRAMKA----GAVDFLEKPFDDQALLDAVRRALARDRARRAERAR 127
PRK15479 PRK15479
transcriptional regulator TctD;
1222-1338 8.42e-15

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 75.14  E-value: 8.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANG--AEGLEKALSLVpdIIISDVMMPEKDGLQMMRELHDNMTTshIPMVLL 1298
Cdd:PRK15479     3 LLLAEDNRELAHWLEKALVQNgFAVDCVFDGlaADHLLQSEMYA--LAVLDINMPGMDGLEVLQRLRKRGQT--LPVLLL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK15479    79 TARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRR 118
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1220-1335 9.75e-15

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: 71.87  E-value: 9.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1220 STMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDG---LQMMRELHdnmttSHIPM 1295
Cdd:cd17554      1 KKILVVDDEENIRELYKEELEDEgYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGletLRKIREKK-----PDLPV 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1119624474 1296 VLLTAKTAIESMLEGLeyGADDYITKPFSATYLKARVRNI 1335
Cdd:cd17554     76 IICTAYSEYKSDFSSW--AADAYVVKSSDLTELKETIKRL 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1221-1322 1.52e-14

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 71.46  E-value: 1.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRtflRSIFA----SEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmTTSHIPMV 1296
Cdd:cd17555      2 TILVIDDDEVVR---ESIAAyledSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITK--ESPDTPVI 76
                           90       100
                   ....*....|....*....|....*.
gi 1119624474 1297 LLTAKTAIESMLEGLEYGADDYITKP 1322
Cdd:cd17555     77 VVSGAGVMSDAVEALRLGAWDYLTKP 102
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1223-1337 2.24e-14

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 71.01  E-value: 2.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEkALSLVPDI--IISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:cd17544      4 LVVDDSATSRNHLRALLRRHnFQVLEAANGQEALE-VLEQHPDIklVITDYNMPEMDGFELVREIRKKYSRDQLAIIGIS 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1119624474 1300 A--KTAIESMLegLEYGADDYITKPFSATYLKARVRNILE 1337
Cdd:cd17544     83 AsgDNALSARF--IKAGANDFLTKPFLPEEFYCRVTQNLE 120
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1067-1165 2.26e-14

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: 70.39  E-value: 2.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1067 IVYNLLSNAFKYT----PEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRfenlvDSSLFNQSSSGIGLSLVKE 1142
Cdd:cd16915      4 IVGNLIDNALDALaatgAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLALVRQ 78
                           90       100
                   ....*....|....*....|...
gi 1119624474 1143 LVEMHKASITVDSKLGEGSCFKV 1165
Cdd:cd16915     79 SVERLGGSITVESEPGGGTTFSI 101
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1223-1322 2.32e-14

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: 70.48  E-value: 2.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLR-SIFASEFRVVEAANGAEGLEKALSLVP---------DIIISDVMMPEKDGLQMMRELHDNMTTSH 1292
Cdd:cd19924      2 LVVDDSPTARKQLRdLLKNLGFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDDPRLAN 81
                           90       100       110
                   ....*....|....*....|....*....|
gi 1119624474 1293 IPMVLLTAKTAIESMLEGLEYGADDYITKP 1322
Cdd:cd19924     82 IPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10610 PRK10610
chemotaxis protein CheY;
1223-1338 4.05e-14

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 70.39  E-value: 4.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFaSEF---RVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:PRK10610     9 LVVDDFSTMRRIVRNLL-KELgfnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVT 87
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK10610    88 AEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
921-1152 4.32e-14

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 75.77  E-value: 4.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  921 IVTAVYILFTiyRLKHRVAMEqqlthmklRFFT-DISHELRTPLTLItgpleyvlqntKLPAEAREQLQVVERNS----- 994
Cdd:PRK10755   119 VTSALNQLVS--RLTSTLDQE--------RLFTaDVAHELRTPLAGI-----------RLHLELLEKQHHIDVAPliarl 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  995 NRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAFVRKIM-DNFEAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLS 1073
Cdd:PRK10755   178 DQMMHTVEQLLQLARAGQSFSSGHYQTVKLLEDVILPSqDELSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVE 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1074 NAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSL---FVRFenlvDSSLfnqSSSGIGLSLVKELVEMHKAS 1150
Cdd:PRK10755   258 NAHRYSPEGSTITIKLSQEDGGAVLAVEDEGPGIDESKCGELskaFVRM----DSRY---GGIGLGLSIVSRITQLHHGQ 330

                   ..
gi 1119624474 1151 IT 1152
Cdd:PRK10755   331 FF 332
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1070-1167 5.37e-14

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: 69.54  E-value: 5.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1070 NLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMHKA 1149
Cdd:cd16952      7 NLVSNAVKYTPPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVMSRHDA 86
                           90
                   ....*....|....*...
gi 1119624474 1150 SITVDSKLGEGSCFKVDF 1167
Cdd:cd16952     87 RLLIASELGKGSRFTCLF 104
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1223-1337 8.59e-14

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: 69.37  E-value: 8.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDN---TEL--RTFLRSIFASEFRVVEaaNGAEGL-------EKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTT 1290
Cdd:cd17557      3 LLVEDNpgdAELiqEAFKEAGVPNELHVVR--DGEEALdflrgegEYADAPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1119624474 1291 SHIPMVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILE 1337
Cdd:cd17557     81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGE 127
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1222-1324 9.77e-14

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 68.98  E-value: 9.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELhdnmTTSHI-PMVLL 1298
Cdd:cd19932      3 VLIAEDEALIRMDLREMLEEAgYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKII----TSENIaPIVLL 78
                           90       100
                   ....*....|....*....|....*.
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFS 1324
Cdd:cd19932     79 TAYSQQDLVERAKEAGAMAYLVKPFS 104
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
1222-1337 1.37e-13

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: 68.68  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLL-- 1298
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMIsg 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1119624474 1299 --TAKTAIESMleglEYGADDYITKPFSATYLKARVRNILE 1337
Cdd:cd17550     79 hgTIETAVKAT----KLGAYDFIEKPLSLDRLLLTIERALE 115
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1224-1322 1.50e-13

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 67.86  E-value: 1.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1224 LVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTAKT 1302
Cdd:cd19936      3 LVDDDRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR---QKSTLPVIFLTSKD 79
                           90       100
                   ....*....|....*....|
gi 1119624474 1303 AIESMLEGLEYGADDYITKP 1322
Cdd:cd19936     80 DEIDEVFGLRMGADDYITKP 99
PRK10604 PRK10604
sensor protein RstB; Provisional
955-1163 1.57e-13

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 74.64  E-value: 1.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTlitgPLEYVLQNTKLPAEArEQlQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAFVRKIMDN 1034
Cdd:PRK10604   219 IAHELRTPLV----RLRYRLEMSDNLSAA-ES-QALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLAD 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1035 FEAVAEEHHIDfvFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTpEGKMITVFVHDnGQTVSVGVQDQGIGIAENKKKS 1114
Cdd:PRK10604   293 IQAVTPEKTVR--LDTPHQGDYGALDMRLMERVLDNLLNNALRYA-HSRVRVSLLLD-GNQACLIVEDDGPGIPPEERER 368
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1115 LFVRFENLvDSSLFNQSSS-GIGLSLVKELVEMHKASITVD-SKLGeGSCF 1163
Cdd:PRK10604   369 VFEPFVRL-DPSRDRATGGcGLGLAIVHSIALAMGGSVNCDeSELG-GARF 417
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
1221-1323 1.69e-13

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: 67.91  E-value: 1.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVP-DIIISDVMMPEKDGLQMMRELHDnmTTSHIPMVLL 1298
Cdd:cd18160      1 TILLADDEPSVRKFIVTTLKKAgYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARK--IDPDVKILFI 78
                           90       100
                   ....*....|....*....|....*
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPF 1323
Cdd:cd18160     79 SGGAAAAPELLSDAVGDNATLKKPF 103
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1223-1340 4.34e-13

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: 67.18  E-value: 4.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNT----ELRTFLRSIfaSEFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmtTSHIPMVL 1297
Cdd:cd17532      2 LIVDDEPlareELRYLLEEH--PDIEIVgEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSK---LAKPPLIV 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1119624474 1298 LTakTAIESM-LEGLEYGADDYITKPFSATYLKARVRNILERRK 1340
Cdd:cd17532     77 FV--TAYDEYaVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
PRK10336 PRK10336
two-component system response regulator QseB;
1222-1338 4.47e-13

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 70.31  E-value: 4.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTA 1300
Cdd:PRK10336     3 ILLIEDDMLIGDGIKTGLSKMgFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREK--GQREPVLILTA 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK10336    81 RDALAERVEGLRLGADDYLCKPFALIEVAARLEALMRR 118
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
1222-1322 4.51e-13

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: 66.45  E-value: 4.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTA 1300
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEgFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKP 1322
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1223-1336 4.78e-13

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: 66.92  E-value: 4.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIF-ASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVLLTAK 1301
Cdd:cd18159      2 LIVEDDETIASLLKKHLeKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR---QISNVPIIFISSR 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1119624474 1302 TAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:cd18159     79 DDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1223-1383 5.36e-13

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 72.10  E-value: 5.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFAS--EFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELhdnMTTSHIPMVL-- 1297
Cdd:PRK00742     7 LVVDDSAFMRRLISEILNSdpDIEVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKI---MRLRPTPVVMvs 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1298 -LTAKTAIESmLEGLEYGADDYITKPFSATylkarVRNILERRKKLQEMYRE----KLMNMATSPDEPTVEESKAPEMSP 1372
Cdd:PRK00742    84 sLTERGAEIT-LRALELGAVDFVTKPFLGI-----SLGMDEYKEELAEKVRAaaraRVRALPPRAAAAARAAAAAPAALA 157
                          170
                   ....*....|.
gi 1119624474 1373 NDRKFMDKLMA 1383
Cdd:PRK00742   158 AAPLLSSKLVA 168
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
938-1165 8.48e-13

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 73.24  E-value: 8.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  938 VAMEQQLTHMKLRFFTDISHELRTPLTLITGPLEyvlqNTKLPAEAREQLQVVERNSNRMLRLvNQILDFRKiQNKKMKM 1017
Cdd:TIGR03785  475 VARLRQYTHYLENMSSRLSHELRTPVAVVRSSLE----NLELQALEQEKQKYLERAREGTERL-SMILNNMS-EATRLEQ 548
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1018 QVQRLEIVAF-----VRKIMDNFEAVAEEHhiDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDN 1092
Cdd:TIGR03785  549 AIQSAEVEDFdlsevLSGCMQGYQMTYPPQ--RFELNIPETPLVMRGSPELIAQMLDKLVDNAREFSPEDGLIEVGLSQN 626
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119624474 1093 GQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMHKASITVDSKL-GEGSCFKV 1165
Cdd:TIGR03785  627 KSHALLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRI 700
pleD PRK09581
response regulator PleD; Reviewed
1215-1354 1.19e-12

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 71.86  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1215 NTDVRSTMLLVEDNTELRTFLRSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIP 1294
Cdd:PRK09581   151 NKDEDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVP 230
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119624474 1295 MVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILeRRKKLQEMYREKL---MNMA 1354
Cdd:PRK09581   231 ILLLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQI-RRKRYQDALRNNLeqsIEMA 292
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1060-1167 1.31e-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: 65.56  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1060 DADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKK---SLFVRFENLVDSslfnQSSSGIG 1136
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKkalELFYRDDTSRRS----GGHYGMG 76
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1119624474 1137 LSLVKELVEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:cd16975     77 LYIAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1223-1273 1.81e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 63.36  E-value: 1.81e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1119624474  1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMP 1273
Cdd:smart00448    4 LVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10816 PRK10816
two-component system response regulator PhoP;
1222-1338 2.43e-12

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 68.23  E-value: 2.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASEFRVVEAANGAEGLEKALS-LVPDIIISDVMMPEKDGLQMMRELHDNMTTshIPMVLLTA 1300
Cdd:PRK10816     3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNeHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVLTA 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILER 1338
Cdd:PRK10816    81 RESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRR 118
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1223-1330 2.78e-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: 64.96  E-value: 2.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASEFRVVEAANGAEgleKALSLVP------DIIISDVMMPEKDGLQMMRELHDNMttsHIPMV 1296
Cdd:cd17584      2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAE---EALSMLRenkdefDLVITDVHMPDMDGFEFLELIRLEM---DLPVI 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1119624474 1297 LLTAKTAIESMLEGLEYGADDYITKPFSATYLKA 1330
Cdd:cd17584     76 MMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKN 109
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
1221-1325 2.92e-12

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: 64.77  E-value: 2.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFL-RSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmTTSHIPMVLLT 1299
Cdd:cd17563      2 SLLLVDDDEVFAERLaRALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRA--LQPDARIVVLT 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1119624474 1300 A----KTAIESMleglEYGADDYITKPFSA 1325
Cdd:cd17563     80 GyasiATAVEAI----KLGADDYLAKPADA 105
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1221-1323 3.67e-12

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: 64.60  E-value: 3.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnMTTSHIPMVLLT 1299
Cdd:cd19919      2 TVWIVDDDSSIRWVLERALAGAgLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIK--QRHPDLPVIIMT 79
                           90       100
                   ....*....|....*....|....
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPF 1323
Cdd:cd19919     80 AHSDLDSAVSAYQGGAFEYLPKPF 103
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
947-1158 4.16e-12

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 70.43  E-value: 4.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  947 MKLRFFTDISHELRTPLTLITGPLEyVLQN--TKLPAEAREQLQVverNSNRMLRLVNQI----------LDFRKIQnkk 1014
Cdd:PRK10549   239 MRRDFMADISHELRTPLAVLRGELE-AIQDgvRKFTPESVASLQA---EVGTLTKLVDDLhqlslsdegaLAYRKTP--- 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1015 mkmqvqrLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKEAVyLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQ 1094
Cdd:PRK10549   312 -------VDLVPLLEVAGGAFRERFASRGLTLQLSLPDSAT-VFGDPDRLMQLFNNLLENSLRYTDSGGSLHISAEQRDK 383
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119624474 1095 TVSVGVQDQGIGIAENKKKSLFVRFENlVDSSLfNQSS--SGIGLSLVKELVEMHKASITVD-SKLG 1158
Cdd:PRK10549   384 TLRLTFADSAPGVSDEQLQKLFERFYR-TEGSR-NRASggSGLGLAICLNIVEAHNGRIIAAhSPFG 448
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1222-1321 4.79e-12

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: 64.29  E-value: 4.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE--FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIpmVLL 1298
Cdd:cd19931      1 VLLIDDHPLLRKGIKQLIELDpdFTVVgEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARI--VIL 78
                           90       100
                   ....*....|....*....|...
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITK 1321
Cdd:cd19931     79 TVSDAEDDVVTALRAGADGYLLK 101
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1067-1167 4.91e-12

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: 63.84  E-value: 4.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1067 IVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRF---ENlvdsSLFNQSSSGIGLSLVKEL 1143
Cdd:cd16948      9 IIGQIVSNALKYSKQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGftgEN----GRNFQESTGMGLYLVKKL 84
                           90       100
                   ....*....|....*....|....
gi 1119624474 1144 VEMHKASITVDSKLGEGSCFKVDF 1167
Cdd:cd16948     85 CDKLGHKIDVESEVGEGTTFTITF 108
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1065-1153 5.47e-12

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: 63.63  E-value: 5.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1065 EKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLfNQSSSGIGLSLVKELV 1144
Cdd:cd16945      6 RQAINNLLDNAIDFSPEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHS-GQKSTGLGLAFVQEVA 84

                   ....*....
gi 1119624474 1145 EMHKASITV 1153
Cdd:cd16945     85 QLHGGRITL 93
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1221-1338 2.04e-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: 62.26  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTEL----RTFLRSIfaSEFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPM 1295
Cdd:cd19925      2 NVLIVEDDPMVaeihRAYVEQV--PGFTVIgTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1119624474 1296 VllTAKTAIESMLEGLEYGADDYITKPFSAtylkARVRNILER 1338
Cdd:cd19925     80 V--TAANDVETVREALRLGVVDYLIKPFTF----ERLRQRLER 116
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1223-1284 2.13e-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: 62.60  E-value: 2.13e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE--FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMREL 1284
Cdd:COG2197      5 LIVDDHPLVREGLRALLEAEpdIEVVgEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1221-1337 3.65e-11

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: 61.65  E-value: 3.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTE-LRTFLRSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLT 1299
Cdd:cd17569      2 TILLVDDEPNiLKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRER--YPDTVRILLT 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1119624474 1300 A----KTAIESMLEGLEYGaddYITKPFSATYLKARVRNILE 1337
Cdd:cd17569     80 GyadlDAAIEAINEGEIYR---FLTKPWDDEELKETIRQALE 118
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
1221-1338 3.82e-11

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: 62.04  E-value: 3.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASEFRVV--EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLL 1298
Cdd:cd17575      2 MVLLVDDQAIIGEAVRRALADEEDIDfhYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVR-------NILER 1338
Cdd:cd17575     82 STKEEPEVKSEAFALGANDYLVKLPDKIELVARIRyhsrsyiNLLQR 128
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
291-576 6.16e-11

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 64.66  E-value: 6.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  291 YDLPTGRTEHYAasrlpaekvksIYRDLSDEIWFEQDVVGEVAHFNPYTRKLKcekvyaEPTNTDRSRPAFhIHEDIFGT 370
Cdd:COG4257     10 YPVPAPGSGPRD-----------VAVDPDGAVWFTDQGGGRIGRLDPATGEFT------EYPLGGGSGPHG-IAVDPDGN 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  371 LWvhpygggfsYFDRKNNCLRpFYNSMTGENWRFS-----NKIHSAFSDRQGNLWMC-THSKGLEKVTFRTDRFRL-KVP 443
Cdd:COG4257     72 LW---------FTDNGNNRIG-RIDPKTGEITTFAlpgggSNPHGIAFDPDGNLWFTdQGGNRIGRLDPATGEVTEfPLP 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  444 VNHSYeslsneVRALCEDKDGNMWVGL-KDGMLRVYNRhreEIGYLTEagtvsHSGKPLFGNTYFVMQDSHDNLWIATKG 522
Cdd:COG4257    142 TGGAG------PYGIAVDPDGNLWVTDfGANAIGRIDP---DTGTLTE-----YALPTPGAGPRGLAVDPDGNLWVADTG 207
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1119624474  523 AGvvkaeplpgtlryRLTRYRYSADDV--YSLSDDNV--YCLYEDRRGRIWVATFANG 576
Cdd:COG4257    208 SG-------------RIGRFDPKTGTVteYPLPGGGArpYGVAVDGDGRVWFAESGAN 252
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1223-1330 6.42e-11

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


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 60.88  E-value: 6.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVE-AANGAEGLEKALSLVPDIIISDVMMP-EKDGLQMMRELHDNMttsHIPMVLLT 1299
Cdd:cd17534      4 LIVEDEAIIALDLKEILESLgYEVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKF---DIPVIFLT 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1119624474 1300 A---KTAIESMLEGLEYGaddYITKPFSATYLKA 1330
Cdd:cd17534     81 AysdEETLERAKETNPYG---YLVKPFNERELKA 111
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1043-1167 1.10e-10

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: 60.72  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1043 HIDFVFETEKEAVYLWvDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVgvQDQGIGIAENKKKSLFVRFENL 1122
Cdd:cd16954     18 GVSISLDISPELRFPG-ERNDLMELLGNLLDNACKWCLEFVEVTARQTDGGLHLIV--DDDGPGVPESQRSKIFQRGQRL 94
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1119624474 1123 vDSSLFNQsssGIGLSLVKELVEMHKASITV-DSKLGeGSCFKVDF 1167
Cdd:cd16954     95 -DEQRPGQ---GLGLAIAKEIVEQYGGELSLsDSPLG-GARFEVVF 135
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1070-1165 1.35e-10

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: 59.71  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1070 NLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLvDSSLfNQSSSGIGLSLVKELVEMHKA 1149
Cdd:cd16923      7 NLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRG-DNSR-NTEGAGLGLSIAKAIIELHGG 84
                           90
                   ....*....|....*.
gi 1119624474 1150 SITVDSkLGEGSCFKV 1165
Cdd:cd16923     85 SASAEY-DDNHDLFKV 99
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1222-1336 1.90e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 65.05  E-value: 1.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFAS-EFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELhdNMTTSHIPMVLLTA 1300
Cdd:PRK10365     8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEI--KALNPAIPVLIMTA 85
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNIL 1336
Cdd:PRK10365    86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1060-1158 2.68e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli 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: 59.01  E-value: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1060 DADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENlVDSSLfNQSS--SGIGL 1137
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYR-VESSR-NRASggSGLGL 78
                           90       100
                   ....*....|....*....|..
gi 1119624474 1138 SLVKELVEMHKASITVD-SKLG 1158
Cdd:cd16946     79 AICHNIALAHGGTISAEhSPLG 100
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
1223-1323 3.08e-10

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 58.77  E-value: 3.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFAS--EFRVVEAA-NGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:cd17561      5 LIADDNREFVQLLEEYLNSqpDMEVVGVAhNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIMLT 84
                           90       100
                   ....*....|....*....|....
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKPF 1323
Cdd:cd17561     85 AFGQEDITQRAVELGASYYILKPF 108
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
933-1165 3.75e-10

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 64.70  E-value: 3.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  933 RLKHRVAMEQQLThmklrFFTDISHELRTPLTLITGPLEYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQN 1012
Cdd:PRK13837   440 RLEHARRLEAVGT-----LASGIAHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAGARARLIIDQILAFGRKGE 514
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1013 KKmkmqVQRLEIVAFVRKIMDNFeAVAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFV--- 1089
Cdd:PRK13837   515 RN----TKPFDLSELVTEIAPLL-RVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGRVDISLsra 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1090 ---------HDN---GQTVSVGVQDQGIGIAENKKKSLFVRFenlvdsslFNQSSSGIGLSL--VKELVEMHKASITVDS 1155
Cdd:PRK13837   590 klrapkvlsHGVlppGRYVLLRVSDTGAGIDEAVLPHIFEPF--------FTTRAGGTGLGLatVHGIVSAHAGYIDVQS 661
                          250
                   ....*....|
gi 1119624474 1156 KLGEGSCFKV 1165
Cdd:PRK13837   662 TVGRGTRFDV 671
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
896-1163 3.90e-10

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 63.73  E-value: 3.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  896 DIEVLPSFWetplayFLYVLFFLLIIVTAVYIlftIYRLKHRVAMEQQLTHM-KLRFFTD----ISHELRTPLTLITGPL 970
Cdd:COG5806    153 DISELLDFI------LYFIIIQLLAMLIAVYL---IENLIENILLRKELQRAeKLEVVSElaasIAHEVRNPLTVVRGFI 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  971 EYVLQNTKLPAEAREQLQVVERNSNRMLRLVNQILDFRKIQNKKMkmqvQRLEIVAFVRKIMDNFEAVAEEHHIDFVFET 1050
Cdd:COG5806    224 QLLQEPELSDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKL----EKIDVSEELEHVIDVLSPYANMNNVEIQTEL 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1051 EkEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAE---NKKKSLFvrfenlvdssl 1127
Cdd:COG5806    300 E-PGLYIEGDRQKLQQCLINIIKNGIEAMPNGGTLTIDVSIDKNKVIISIKDTGVGMTKeqlERLGEPY----------- 367
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1119624474 1128 FNQSSSGIGLSL--VKELVEMHKASITVDSKLGEGSCF 1163
Cdd:COG5806    368 FSTKEKGTGLGTmvSYRIIEAMNGTIRVESEVGKGTTF 405
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
1222-1337 3.94e-10

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: 62.12  E-value: 3.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE--FRVVEAA-NGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELhDNMTTSHIPMVLL 1298
Cdd:TIGR02875    5 IVIADDNKEFCNLLKEYLAAQpdMEVVGVAhNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKL-NEIELSARPRVIM 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1119624474 1299 TAKTAIESMLE-GLEYGADDYITKPFSATYLKARVRNILE 1337
Cdd:TIGR02875   84 LSAFGQEKITQrAVALGADYYVLKPFDLEILAARIRQLAW 123
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1223-1335 3.95e-10

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 63.36  E-value: 3.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFAS--EFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELhdnMTTSHIPMVLLT 1299
Cdd:PRK12555     4 GIVNDSPLAVEALRRALARdpDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRI---MAERPCPILIVT 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1119624474 1300 AKTA--IESMLEGLEYGADDYITKPF---------SATYLKARVRNI 1335
Cdd:PRK12555    81 SLTErnASRVFEAMGAGALDAVDTPTlgigagleeYAAELLAKIDQI 127
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1220-1333 6.40e-10

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 57.99  E-value: 6.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1220 STMLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELhdNMTTSHIPMVLL 1298
Cdd:cd17537      1 ATVYVVDDDEAVRDSLAFLLRSVgLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDEL--LARGSNIPIIFI 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVR 1333
Cdd:cd17537     79 TGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIE 113
envZ PRK09467
osmolarity sensor protein; Provisional
955-1153 8.83e-10

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 62.62  E-value: 8.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLEYVLQNTKLPAEAreqlqvVERNSNRMLRLVNQILDFRKiQNKKMKMQVQRL-EIVAfvrkimd 1033
Cdd:PRK09467   236 VSHDLRTPLTRIRLATEMMSEEDGYLAES------INKDIEECNAIIEQFIDYLR-TGQEMPMEMADLnALLG------- 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1034 nfEAVAEEHHIDFVFETE--KEAVYLWVDADKFEKIVYNLLSNAFKYTpeGKMITVFVHDNGQTVSVGVQDQGIGIAENK 1111
Cdd:PRK09467   302 --EVIAAESGYEREIETAlqPGPIEVPMNPIAIKRALANLVVNAARYG--NGWIKVSSGTEGKRAWFQVEDDGPGIPPEQ 377
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1119624474 1112 KKSLFVRFE--NLVDSSlfnqSSSGIGLSLVKELVEMHKASITV 1153
Cdd:PRK09467   378 LKHLFQPFTrgDSARGS----SGTGLGLAIVKRIVDQHNGKVEL 417
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
1222-1333 1.15e-09

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: 57.56  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRelHDNMTTSHIPMVLLTA 1300
Cdd:cd17553      3 ILIVDDQYGIRILLNEVFNKEgYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILK--RMKVIDENIRVIIMTA 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVR 1333
Cdd:cd17553     81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVK 113
PRK10337 PRK10337
sensor protein QseC; Provisional
950-1165 1.29e-09

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 62.36  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  950 RFFTDISHELRTPLTLITGPLEyVLQNTKLPAEAREQ-LQVVERNSNRMLRLVNQILDFRKIQNKKMKMQVQRLEIVAFV 1028
Cdd:PRK10337   239 RFTSDAAHELRSPLAALKVQTE-VAQLSDDDPQARKKaLLQLHAGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1029 RK-IMDNFEAvAEEHHIDFVFETEKEAVYLWVDADKFEKIVYNLLSNAFKYTPEGKMITVFVHDNGQTvsvgVQDQGIGI 1107
Cdd:PRK10337   318 QSaVMDIYHT-AQQAGIDVRLTLNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSVVDVTLNARNFT----VRDNGPGV 392
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1119624474 1108 AENKKKSLFVRFENLVDSSlfnQSSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:PRK10337   393 TPEALARIGERFYRPPGQE---ATGSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKV 447
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
1224-1322 1.36e-09

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 56.90  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1224 LVEDNTELRTFLRSIFASEF--RVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMvllTA 1300
Cdd:cd17565      3 IVDDDKNIIKILSDIIEDDDlgEVVgEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIM---IS 79
                           90       100
                   ....*....|....*....|...
gi 1119624474 1301 KTAIESML-EGLEYGADDYITKP 1322
Cdd:cd17565     80 QVSDKEMIgKAYQAGIEFFINKP 102
PRK13557 PRK13557
histidine kinase; Provisional
955-1337 1.55e-09

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 62.38  E-value: 1.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  955 ISHELRTPLTLITGPLEYVLQNTKLPAEAREQLQV-VER---NSNRMLRLVNQILDF-RKiqnkkmkmqvQRLE-IVAFV 1028
Cdd:PRK13557   170 IAHDFNNLLQVMSGYLDVIQAALSHPDADRGRMARsVENiraAAERAATLTQQLLAFaRK----------QRLEgRVLNL 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1029 RKIMDNFEAVAEE---HHIDFVFETEKEavyLW---VDADKFEKIVYNLLSNAFKYTPEGKMITV-------FVHDN--- 1092
Cdd:PRK13557   240 NGLVSGMGELAERtlgDAVTIETDLAPD---LWncrIDPTQAEVALLNVLINARDAMPEGGRVTIrtrnveiEDEDLamy 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1093 -----GQTVSVGVQDQGIGIAenkkKSLFVRfenlVDSSLFNQSS----SGIGLSLVKELVEMHKASITVDSKLGEGSCF 1163
Cdd:PRK13557   317 hglppGRYVSIAVTDTGSGMP----PEILAR----VMDPFFTTKEegkgTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTV 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1164 KVDFQKgkehydetveflqnDVEQGGAKQEQQTAVEDNGASEgnkgeegtentdvrsTMLLVEDNTEL----RTFLRSIf 1239
Cdd:PRK13557   389 RLYFPA--------------SDQAENPEQEPKARAIDRGGTE---------------TILIVDDRPDVaelaRMILEDF- 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1240 asEFRVVEAANGAEGLEK-ALSLVPDIIISDVMMP-EKDGLQMMRELHDNMTTSHipmVLLTAKTAiESMLE-----GLE 1312
Cdd:PRK13557   439 --GYRTLVASNGREALEIlDSHPEVDLLFTDLIMPgGMNGVMLAREARRRQPKIK---VLLTTGYA-EASIErtdagGSE 512
                          410       420
                   ....*....|....*....|....*
gi 1119624474 1313 YgadDYITKPFSATYLKARVRNILE 1337
Cdd:PRK13557   513 F---DILNKPYRRAELARRVRMVLD 534
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1065-1165 1.65e-09

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: 56.64  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1065 EKIVYNLLSNAFK----YTPEGKMITV-FVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLfnqsssGIGLSL 1139
Cdd:cd16920      2 QQVLINLVRNGIEamseGGCERRELTIrTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSEGL------GMGLSI 75
                           90       100
                   ....*....|....*....|....*.
gi 1119624474 1140 VKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:cd16920     76 CRSIIEAHGGRLSVESPAGGGATFQF 101
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
1223-1344 1.79e-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: 56.94  E-value: 1.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTAKT 1302
Cdd:cd17539      2 LLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVADPG 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1119624474 1303 AIESMLEGLEYGADDYITKPFSATYLKARVRNILeRRKKLQE 1344
Cdd:cd17539     82 DRGRLIRALEIGVNDYLVRPIDPNELLARVRTQI-RRKRYTD 122
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1243-1322 2.25e-09

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: 56.22  E-value: 2.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1243 FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTAKTAIESMLEGLEYGADDYITKP 1322
Cdd:cd17602     23 FRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
fixJ PRK09390
response regulator FixJ; Provisional
1240-1383 2.38e-09

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 58.86  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1240 ASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTAKTAIESMLEGLEYGADDYI 1319
Cdd:PRK09390    25 SAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKAR--GSPLPVIVMTGHGDVPLAVEAMKLGAVDFI 102
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1320 TKPFSATYLKARVRNILERRKklqemyreklmnmATSPDEPTVEE--SKAPEMSPNDRKFMDKLMA 1383
Cdd:PRK09390   103 EKPFEDERLIGAIERALAQAP-------------EAAKSEAVAADirARIASLSERERQVMDGLVA 155
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1220-1333 4.85e-09

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 58.49  E-value: 4.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1220 STMLLVEDNTELRTFLRSIFAS-EFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTshiPMVLL 1298
Cdd:PRK10701     2 NKIVFVEDDAEVGSLIAAYLAKhDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG---PIVLL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVR 1333
Cdd:PRK10701    79 TSLDSDMNHILALEMGACDYILKTTPPAVLLARLR 113
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
1223-1332 5.09e-09

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 55.35  E-value: 5.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFAS--EFRVVEAANGAEGLEKALSLVPDIIISDVMMPE-KDGLQMMREL-HDNMTTSHIPMVLL 1298
Cdd:cd17589      2 LIVDDQPTFRSMLKSMLRSlgVTRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELrHKKLISPSTVFIMV 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARV 1332
Cdd:cd17589     82 TGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
1430-1483 1.32e-08

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 58.06  E-value: 1.32e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1119624474 1430 RINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEYRDRKAGKN 1483
Cdd:PRK10572   236 RISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEKN 289
PRK15115 PRK15115
response regulator GlrR; Provisional
1222-1351 1.36e-08

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 59.08  E-value: 1.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTshIPMVLLTA 1300
Cdd:PRK15115     8 LLLVDDDPGLLKLLGMRLTSEgYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPG--MPVIILTA 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKL-QEMYREKLM 1351
Cdd:PRK15115    86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPAtDERWREAIV 137
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
1020-1167 1.45e-08

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 59.15  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1020 QRLEIVAFVRKIMDNFEAVAEEHHIDFVFETEKeavyLWVDADKFEK---IVYNLLSNAFKY----TPEGKmITVFVHDN 1092
Cdd:COG3920    357 EGVDLRDYLRELLEPLRDSYGGRGIRIELDGPD----VELPADAAVPlglILNELVTNALKHaflsGEGGR-IRVSWRRE 431
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1093 GQTVSVGVQDQGIGIAENKKKslfvrfenlvdsslfnQSSSGIGLSLVKELVEMHKASITVDSklGEGSCFKVDF 1167
Cdd:COG3920    432 DGRLRLTVSDNGVGLPEDVDP----------------PARKGLGLRLIRALVRQLGGTLELDR--PEGTRVRITF 488
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
1221-1347 2.70e-08

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 53.91  E-value: 2.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDG---LQMMRELHDNMTTshipmVL 1297
Cdd:cd17596      2 TILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGvefLKEVRERWPEVVR-----II 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1298 LTAKTAIESMLEGL-EYGADDYITKPFSATYLKARVRNILERRKKLQEMYR 1347
Cdd:cd17596     77 ISGYTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRENER 127
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
1059-1175 2.92e-08

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 58.31  E-value: 2.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1059 VDADKFEKIVYNLLSNAFK---YTPEG-KMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLfvrFENLVDSSLFNQSSSG 1134
Cdd:PRK15053   428 LDSTEFAAIVGNLLDNAFEaslRSDEGnKIVELFLSDEGDDVVIEVADQGCGVPESLRDKI---FEQGVSTRADEPGEHG 504
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1119624474 1135 IGLSLVKELVEMHKASITVDSKLGEGSCFKVDFQKGKEHYD 1175
Cdd:PRK15053   505 IGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIPKVKPNDS 545
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1066-1166 6.18e-08

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 52.19  E-value: 6.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1066 KIVYNLLSNAFKYTPEGKM-ITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRF-ENLVDSSLFNQsSSGIGLSLVKEL 1143
Cdd:cd16953      3 QVLRNLIGNAISFSPPDTGrITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFyTERPANEAFGQ-HSGLGLSISRQI 81
                           90       100
                   ....*....|....*....|....*..
gi 1119624474 1144 VEMHKASITV----DSKLGEGSCFKVD 1166
Cdd:cd16953     82 IEAHGGISVAenhnQPGQVIGARFTVQ 108
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1219-1323 6.91e-08

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 56.80  E-value: 6.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1219 RSTMLLVEDNTELRTFL-RSIFASEFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTshIPMVL 1297
Cdd:PRK10923     3 RGIVWVVDDDSSIRWVLeRALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVII 80
                           90       100
                   ....*....|....*....|....*.
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPF 1323
Cdd:PRK10923    81 MTAHSDLDAAVSAYQQGAFDYLPKPF 106
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
933-1162 7.38e-08

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 57.00  E-value: 7.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  933 RLKHRVAMEQQLTHM-KL----RFFTDISHELRTPLTLITGPL---EYVLQnTKLPAEAREQLQVVERNSNRMLRLVNQI 1004
Cdd:COG4192    413 IEKNLRQTQDELIQAaKMavvgQTMTSLAHELNQPLNAMSMYLfsaKKALE-QENYAQLPTSLDKIEGLIERMDKIIKSL 491
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1005 LDFRKIQNKKMK----MQV--QRLEIVAFVRKIMDNFEAVAEEHhidFVFetekeavylwVDADKFEKIVYNLLSNAFKY 1078
Cdd:COG4192    492 RQFSRKSDTPLQpvdlRQVieQAWELVESRAKPQQITLHIPDDL---MVQ----------GDQVLLEQVLVNLLVNALDA 558
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1079 TPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKksLFVRFENLVDSSLfnqsssGIGLSLVKELVEMHKASITVDSKLG 1158
Cdd:COG4192    559 VATQPQISVDLLSNAENLRVAISDNGNGWPLVDK--LFTPFTTTKEVGL------GLGLSICRSIMQQFGGDLYLASTLE 630

                   ....
gi 1119624474 1159 EGSC 1162
Cdd:COG4192    631 RGAM 634
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
1064-1169 7.85e-08

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 56.56  E-value: 7.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1064 FEKIVYNLLSNAFKYTPEGKMITVFVHDNgqTVSVGVQDQGIGIAENKKKSLFVRFENlVDSSlfnQSSSGIGLSLVKEL 1143
Cdd:PRK10815   379 FMEVMGNVLDNACKYCLEFVEISARQTDE--HLHIVVEDDGPGIPESKRELIFDRGQR-ADTL---RPGQGLGLSVAREI 452
                           90       100
                   ....*....|....*....|....*..
gi 1119624474 1144 VEMHKASITV-DSKLGeGSCFKVDFQK 1169
Cdd:PRK10815   453 TEQYEGKISAgDSPLG-GARMEVIFGR 478
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
1439-1476 8.73e-08

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: 49.46  E-value: 8.73e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1119624474 1439 ETGEYSMTQIAYMVGInDPRYFSKCFKQKMGMTPTEYR 1476
Cdd:pfam00165    5 LSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
7-211 8.85e-08

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 55.41  E-value: 8.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474    7 LWMLAVLTAAVLKAQPE-GSFTHYSSDDGlseNTVMDMLQDSRGNMWFSTW--NGINKFDGYT--FKTF----KARQDNQ 77
Cdd:COG4257     30 VWFTDQGGGRIGRLDPAtGEFTEYPLGGG---SGPHGIAVDPDGNLWFTDNgnNRIGRIDPKTgeITTFalpgGGSNPHG 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474   78 IALTSNrvdnmkldryGFIWL-QTYDDRAFRFDPRTEVFESVPAegePGSQTAISSIKVLPDGTVWLLTRREGAV-RITT 155
Cdd:COG4257    107 IAFDPD----------GNLWFtDQGGNRIGRLDPATGEVTEFPL---PTGGAGPYGIAVDPDGNLWVTDFGANAIgRIDP 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  156 DS---TDY----------RLTS-----VWYSpASERLRVSRvFDVcqADGA--EWVLSDNGL----VCFTPDGAepvIYF 211
Cdd:COG4257    174 DTgtlTEYalptpgagprGLAVdpdgnLWVA-DTGSGRIGR-FDP--KTGTvtEYPLPGGGArpygVAVDGDGR---VWF 246
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1223-1337 1.07e-07

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 51.89  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIF--ASEFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHipmVLLT 1299
Cdd:cd19930      2 LIAEDQEMVRGALAALLelEDDLEVVaQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTK---VLIV 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1300 AKTAIESMLE-GLEYGADDYITKPFSATYLKARVRNILE 1337
Cdd:cd19930     79 TTFGRPGYFRrALAAGVDGYVLKDRPIEELADAIRTVHA 117
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
409-679 1.15e-07

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 55.03  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  409 HSAFSDRQGNLWMC-THSKGLEKVTFRTDRFrlkvpVNHSYESLSnEVRALCEDKDGNMWVGLkdgmlrvYNRHReeIGY 487
Cdd:COG4257     20 RDVAVDPDGAVWFTdQGGGRIGRLDPATGEF-----TEYPLGGGS-GPHGIAVDPDGNLWFTD-------NGNNR--IGR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  488 LTEA-GTVS-HSGKPLFGNTYFVMQDSHDNLWIATKGAGVVkaeplpgtLRYRLTRYRYSADDVYSlSDDNVYCLYEDRR 565
Cdd:COG4257     85 IDPKtGEITtFALPGGGSNPHGIAFDPDGNLWFTDQGGNRI--------GRLDPATGEVTEFPLPT-GGAGPYGIAVDPD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  566 GRIWVATF-ANGISYLTrNADGKEVFISHRNNLKGFpikycskvRCITGDADGHIWIGTTVG--LLMVDdgfdrPEDARF 642
Cdd:COG4257    156 GNLWVTDFgANAIGRID-PDTGTLTEYALPTPGAGP--------RGLAVDPDGNLWVADTGSgrIGRFD-----PKTGTV 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1119624474  643 YHYlrapekANALSNNDIHWVKPTREGELYVATFGGG 679
Cdd:COG4257    222 TEY------PLPGGGARPYGVAVDGDGRVWFAESGAN 252
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1066-1165 1.26e-07

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: 51.30  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1066 KIVYNLLSNAFKYTpeGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSL---FVRFENLVDSslfnqSSSGIGLSLVKE 1142
Cdd:cd16950      3 RVLSNLVDNALRYG--GGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELfqpFYRGDNARGT-----SGTGLGLAIVQR 75
                           90       100
                   ....*....|....*....|...
gi 1119624474 1143 LVEMHKASITVDSKLGEGSCFKV 1165
Cdd:cd16950     76 ISDAHGGSLTLANRAGGGLCARI 98
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1222-1339 1.29e-07

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 54.43  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE-FRVVEAANGAEgLEKALSLVP-DIIISDVMMPEKDGLQMMRELhdnMTTSHIPMVLLT 1299
Cdd:PRK13856     4 VLVIDDDVAMRHLIVEYLTIHaFKVTAVADSQQ-FNRVLASETvDVVVVDLNLGREDGLEIVRSL---ATKSDVPIIIIS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1119624474 1300 AKTAIES-MLEGLEYGADDYITKPFSATYLKARVRNILERR 1339
Cdd:PRK13856    80 GDRLEEAdKVVALELGATDFIAKPFGTREFLARIRVALRVR 120
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1235-1338 1.45e-07

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: 51.38  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1235 LRSIFASE-FRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVLLTAKTAIESMLEGLEY 1313
Cdd:cd17593     17 ARALPADWdVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVE--QLETKVIVVSGDVQPEAKERVLEL 94
                           90       100
                   ....*....|....*....|....*
gi 1119624474 1314 GADDYITKPFSatylKARVRNILER 1338
Cdd:cd17593     95 GALAFLKKPFD----PEKLAQLLEE 115
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
1399-1480 2.51e-07

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 53.78  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1399 LVKDMAVSRSVFFKKLKSlTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEYRDR 1478
Cdd:PRK09978   164 IASELLMSPSLLKKKLRE-EETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQER 242

                   ..
gi 1119624474 1479 KA 1480
Cdd:PRK09978   243 SA 244
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
1377-1482 3.22e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 53.52  E-value: 3.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1377 FMDKLMALMEKNLDNgDLIVDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGIND 1456
Cdd:PRK13502   177 LLDKLITALANSLEC-PFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFED 255
                           90       100
                   ....*....|....*....|....*.
gi 1119624474 1457 PRYFSKCFKQKMGMTPTEYRDRKAGK 1482
Cdd:PRK13502   256 SNYFSVVFTRETGMTPSQWRHLSNQS 281
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
1412-1478 3.34e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 53.75  E-value: 3.34e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1412 KKLKSL----TGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEYRDR 1478
Cdd:PRK13501   207 RSLKQLfrqqTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQR 277
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1065-1163 3.69e-07

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 49.74  E-value: 3.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1065 EKIVYNLLSNAFKYTpeGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSGIGLSLVKELV 1144
Cdd:cd16939      2 ARALDNLLRNALRYA--HRTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVA 79
                           90       100
                   ....*....|....*....|
gi 1119624474 1145 EMHKASITV-DSKLGeGSCF 1163
Cdd:cd16939     80 LWHGGHVECdDSELG-GACF 98
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
1222-1332 3.84e-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: 50.12  E-value: 3.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLrSIFASEFRVveAANGAEGLEKALSLVP----DIIISDVMMPEKDGLQMMRELHDNmtTSHIPMVL 1297
Cdd:cd17573      1 ILLIEDDSTLGKEI-SKGLNEKGY--QADVAESLKDGEYYIDirnyDLVLVSDKLPDGNGLSIVSRIKEK--HPSIVVIV 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFSATYLKARV 1332
Cdd:cd17573     76 LSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
ftrA PRK09393
transcriptional activator FtrA; Provisional
1370-1478 4.12e-07

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 53.81  E-value: 4.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1370 MSPNDRKFMDKLMALMEKNLDNgDLIVDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIA 1449
Cdd:PRK09393   212 VASRESDRLGPLIDWMRAHLAE-PHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIA 290
                           90       100
                   ....*....|....*....|....*....
gi 1119624474 1450 YMVGINDPRYFSKCFKQKMGMTPTEYRDR 1478
Cdd:PRK09393   291 ERAGFGSEESLRHHFRRRAATSPAAYRKR 319
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
1422-1483 5.30e-07

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 52.84  E-value: 5.30e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119624474 1422 PVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEYRDRKAGKN 1483
Cdd:PRK10296   217 PMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRKKLTEFN 278
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
1067-1166 5.50e-07

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 54.15  E-value: 5.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1067 IVYNLLSNAF---KYTPEGKMITVFVHDNGQtVSVGVQDQGIGIAENKKKSLFVR-FenlvdSSlfNQSSSGIGLSLVKE 1142
Cdd:PRK11086   437 ILGNLIENALeavGGEEGGEISVSLHYRNGW-LHCEVSDDGPGIAPDEIDAIFDKgY-----ST--KGSNRGVGLYLVKQ 508
                           90       100
                   ....*....|....*....|....
gi 1119624474 1143 LVEMHKASITVDSKLGEGSCFKVD 1166
Cdd:PRK11086   509 SVENLGGSIAVESEPGVGTQFFVQ 532
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1066-1165 1.02e-06

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 48.57  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1066 KIVYNLLSNAFKYTPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFEnlvdSSLFNQSSSGIGLSLVKELVE 1145
Cdd:cd16943      6 QVLLNLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFF----TTKPVGEGTGLGLSLSYRIIQ 81
                           90       100
                   ....*....|....*....|
gi 1119624474 1146 MHKASITVDSKLGEGSCFKV 1165
Cdd:cd16943     82 KHGGTIRVASVPGGGTRFTI 101
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
1412-1476 1.24e-06

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 51.99  E-value: 1.24e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119624474 1412 KKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEYR 1476
Cdd:PRK13503   206 RQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
1223-1322 1.50e-06

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: 47.92  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFAS-EFRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRelHDNMTTSHIPMVLLTAK 1301
Cdd:cd19926      2 LVVDDEPDIRELLEITLGRmGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQ--HIQQRLPQTPVAVITAY 79
                           90       100
                   ....*....|....*....|.
gi 1119624474 1302 TAIESMLEGLEYGADDYITKP 1322
Cdd:cd19926     80 GSLDTAIEALKAGAFDFLTKP 100
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1222-1350 1.71e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 50.62  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASE--FRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIpmVLL 1298
Cdd:PRK10403     9 VLIVDDHPLMRRGVRQLLELDpgFEVVaEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQI--IIL 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEMYREKL 1350
Cdd:PRK10403    87 TVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAKGSKVFSERVNQYL 138
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
1377-1483 3.48e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 50.87  E-value: 3.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1377 FMDKLMALMEKNLDNgDLIVDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGIND 1456
Cdd:PRK13500   207 LLDKLITRLAASLKS-PFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFED 285
                           90       100
                   ....*....|....*....|....*..
gi 1119624474 1457 PRYFSKCFKQKMGMTPTEYRDRKAGKN 1483
Cdd:PRK13500   286 SNYFSVVFTRETGMTPSQWRHLNSQKD 312
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
1373-1478 4.98e-06

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 50.03  E-value: 4.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1373 NDRKFMdKLMALMEKNLDNGDLIVDDLVKDMAVS-RSVFfkKLKSLTGLAPVEFIKEMRINRAVQLIET---GEySMTQI 1448
Cdd:PRK09685   195 RERQFQ-KVVALIDQSIQEEILRPEWIAGELGISvRSLY--RLFAEQGLVVAQYIRNRRLDRCADDLRPaadDE-KITSI 270
                           90       100       110
                   ....*....|....*....|....*....|
gi 1119624474 1449 AYMVGINDPRYFSKCFKQKMGMTPTEYRDR 1478
Cdd:PRK09685   271 AYKWGFSDSSHFSTAFKQRFGVSPGEYRRK 300
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
1280-1475 5.07e-06

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 50.06  E-value: 5.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1280 MMRELHDNMTTSHIPMVLLTAKTAIESML-EGLEYGADdyITKPFSATYLK------ARVRNILERRKKLQEMYREK--- 1349
Cdd:PRK15186    78 TMEETHEQLNYNLIELDSASIKNAYNFFLyEHADFSAP--LTKPTTKHLLApietgvARVFNLLHSSNKSQKLSQDKkey 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1350 LMNMATSpdeptvEESKAPEMSPNDRKFMDKLMALMEKNLDNGDL----IVDDLVKDMAVSRSVFFKKLKSlTGLAPVEF 1425
Cdd:PRK15186   156 LIRFLLS------EFIYEPEAFALFRELSQNTLAENIYNIIISDIsrkwALKDISDSLYMSCSTLKRKLKQ-ENTSFSEV 228
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1426 IKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEY 1475
Cdd:PRK15186   229 YLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
PRK10693 PRK10693
two-component system response regulator RssB;
1247-1322 6.21e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 49.99  E-value: 6.21e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119624474 1247 EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnMTTSHIPMVLLTAKTAIESMLEGLEYGADDYITKP 1322
Cdd:PRK10693     2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLR--NRGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
908-1165 7.37e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 49.23  E-value: 7.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  908 LAYFLYVLFFLLIIVTAVYILFTIYRLKHRVAMEQQLTHM------------KLRfftdISHEL------RtpLTLIT-- 967
Cdd:COG4585      2 LALALLGALALLVGALLGLLLALVLLRARRAERAAELERElaaraeeareeeRRR----IARELhdgvgqS--LSAIKlq 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  968 -GPLEYVLQntKLPAEAREQLQVVERNSNRMLRLVNQILdfRKIQNkkmkMQVQRLEIVAFVRKIMDNFEavaEEHHIDF 1046
Cdd:COG4585     76 lEAARRLLD--ADPEAAREELEEIRELAREALAELRRLV--RGLRP----PALDDLGLAAALEELAERLL---RAAGIRV 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1047 VFETEKEAVYLwvdADKFEKIVY----NLLSNAFKYTPeGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSlfvrfenl 1122
Cdd:COG4585    145 ELDVDGDPDRL---PPEVELALYrivqEALTNALKHAG-ATRVTVTLEVDDGELTLTVRDDGVGFDPEAAPG-------- 212
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1119624474 1123 vdsslfnqssSGIGLSLVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:COG4585    213 ----------GGLGLRGMRERAEALGGTLTIGSAPGGGTRVRA 245
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
1223-1322 7.92e-06

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 46.24  E-value: 7.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVE-DNTELRTFLRSIFASEFRVVEAANGAEGLE--KALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLT 1299
Cdd:cd17582      2 LLVEnDDSTRQIVTALLRKCSYEVTAASDGLQAWDvlEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMMS 81
                           90       100
                   ....*....|....*....|...
gi 1119624474 1300 AKTAIESMLEGLEYGADDYITKP 1322
Cdd:cd17582     82 SQDSVGVVFKCLSKGAADYLVKP 104
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
1071-1172 8.51e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 50.02  E-value: 8.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1071 LLSNAFKY----TPEGKMITVFVHDNGQTVSVGVQDQGIGIAENKKKSLFVRFENlvdsslfNQSSSGIGLSLVKELVEM 1146
Cdd:COG2972    344 LVENAIEHgiepKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSS-------KGEGRGIGLRNVRERLKL 416
                           90       100
                   ....*....|....*....|....*....
gi 1119624474 1147 H---KASITVDSKLGEGSCFKVDFQKGKE 1172
Cdd:COG2972    417 YygeEYGLEIESEPGEGTTVTIRIPLEEE 445
dpiA PRK10046
two-component response regulator DpiA; Provisional
1221-1343 1.43e-05

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 48.09  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRT----FLRSIFASEfRVVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDnmttSHIP-- 1294
Cdd:PRK10046     6 TLLIVEDETPLAEmhaeYIRHIPGFS-QILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQ----AHYPgd 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1119624474 1295 MVLLTAKTAIESMLEGLEYGADDYITKPFSATYLKARVRNILERRKKLQ 1343
Cdd:PRK10046    81 VVFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLE 129
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1070-1151 2.73e-05

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: 44.62  E-value: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1070 NLLSNAFKYTPEGKMITVFVHDNGQTVSvgVQDQGIGIAENKKKSLFVRFENLVDSSLFNQSSSGIGLSLVKELVEMHKA 1149
Cdd:cd16949      7 NVLRNALRYSPSKILLDISQDGDQWTIT--ITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIEQHGG 84

                   ..
gi 1119624474 1150 SI 1151
Cdd:cd16949     85 KI 86
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
1221-1330 3.10e-05

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: 44.74  E-value: 3.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNTELRTFLRSIFASEFR--VVEAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMREL---HDNMTTSHI-- 1293
Cdd:cd17530      2 RVLVLDDDPFQCMMAATILEDLGPgnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLaesHSNAAVILMsg 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1119624474 1294 --PMVLLTAKTAIESMleGLEYGADdyITKPFSATYLKA 1330
Cdd:cd17530     82 ldGGILESAETLAGAN--GLNLLGT--LSKPFSPEELTE 116
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
91-340 4.03e-05

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 46.94  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474   91 DRYGFIWL-QTYDDRAFRFDPRTEVFESVPaegePGSQTAISSIKVLPDGTVWLLTRREGAV-RITTDSTDYRLTSVwys 168
Cdd:COG4257     25 DPDGAVWFtDQGGGRIGRLDPATGEFTEYP----LGGGSGPHGIAVDPDGNLWFTDNGNNRIgRIDPKTGEITTFAL--- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  169 PASERLRVSRVFDvcqADGAEWVLSDNG--------------------------LVCFTPDGAepvIYFenAEEGKDSFK 222
Cdd:COG4257     98 PGGGSNPHGIAFD---PDGNLWFTDQGGnrigrldpatgevtefplptggagpyGIAVDPDGN---LWV--TDFGANAIG 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  223 KrqsfyvmedcgdcllFGSGNGTVWVYRKKDRTFRPVQLDAAS--RIsgikhlkklsqVVVATVSDGFFVYDLPTGRTEH 300
Cdd:COG4257    170 R---------------IDPDTGTLTEYALPTPGAGPRGLAVDPdgNL-----------WVADTGSGRIGRFDPKTGTVTE 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1119624474  301 YAASRLPAEKVkSIYRDLSDEIWFEQDVVGEVAHFNPYTR 340
Cdd:COG4257    224 YPLPGGGARPY-GVAVDGDGRVWFAESGANRIVRFDPDTE 262
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
1223-1323 4.06e-05

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 43.87  E-value: 4.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFASE-FRVVEAANGAEGLEK-ALSLVPDIIISDVMMP-EKDGLQMMRELHdnMTTSHIPMVLLT 1299
Cdd:cd18161      2 LVVEDDPDVRRLTAEVLEDLgYTVLEAASGDEALDLlESGPDIDLLVTDVIMPgGMNGSQLAEEAR--RRRPDLKVLLTS 79
                           90       100
                   ....*....|....*....|....
gi 1119624474 1300 AKTAIESMLEGLEYGAdDYITKPF 1323
Cdd:cd18161     80 GYAENAIEGGDLAPGV-DVLSKPF 102
PRK15369 PRK15369
two component system response regulator;
1222-1321 4.19e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 46.23  E-value: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFAS--EFRVVEAA-NGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHDNMTTSHIpmVLL 1298
Cdd:PRK15369     6 ILLVDDHELIINGIKNMLAPypRYKIVGQVdNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNI--LVL 83
                           90       100
                   ....*....|....*....|...
gi 1119624474 1299 TAKTAIESMLEGLEYGADDYITK 1321
Cdd:PRK15369    84 TARQEEHMASRTLAAGALGYVLK 106
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
1396-1475 6.78e-05

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 46.53  E-value: 6.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1396 VDDLVKDMAVSRSVFFKKLKSlTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCFKQKMGMTPTEY 1475
Cdd:PRK15185   225 LTDVADHIFMSTSTLKRKLAE-EGTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPSTF 303
PLN03029 PLN03029
type-a response regulator protein; Provisional
1264-1380 8.20e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 45.79  E-value: 8.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1264 DIIISDVMMPEKDGLQMMRELHDNMTTSHIPMVLLTAKTAIESMLEGLEYGADDYITKPFSAT--------YLKARVRNI 1335
Cdd:PLN03029    74 NLIITDYCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSdlnrlkphMMKTKSKNQ 153
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1119624474 1336 LERRKKLQEMYREKLMNMATSPDEPTVEESK-APEMSP-----NDRKFMDK 1380
Cdd:PLN03029   154 KQENQEKQEKLEESEIQSEKQEQPSQQPQSQpQPQQQPqqpnnNKRKAMEE 204
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
551-573 1.93e-04

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: 39.99  E-value: 1.93e-04
                           10        20
                   ....*....|....*....|...
gi 1119624474  551 SLSDDNVYCLYEDRRGRIWVATF 573
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTN 23
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
1222-1322 2.19e-04

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: 41.72  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTELRTFLRSIFASEFRVVEAANGAEGLEKALSLVP-DIIISDVMMPEKDGLQMMRELHDnmTTSHIPMVLLTA 1300
Cdd:cd19928      1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEgDLVITDVVMPDENGLDLIPRIKK--ARPDLPIIVMSA 78
                           90       100
                   ....*....|....*....|..
gi 1119624474 1301 KTAIESMLEGLEYGADDYITKP 1322
Cdd:cd19928     79 QNTLMTAVKAAERGAFEYLPKP 100
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1223-1322 2.95e-04

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: 41.97  E-value: 2.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFL-RSIFASEFRVVEAANGAEGLE---------KALSLVPDI--IISDVMMPEKDGLQMMRELHDNMTT 1290
Cdd:cd17581      2 LAVDDSLVDRKVIeRLLRISSCRVTAVDSGKRALEflgledeedSSNFNEPKVnmIITDYCMPGMTGYDLLKKVKESSAL 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1119624474 1291 SHIPMVLLTAKTAIESMLEGLEYGADDYITKP 1322
Cdd:cd17581     82 KEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
1223-1324 4.05e-04

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: 41.62  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDNTELRTFLRSIFAS-EFRVVEAANGAEGLeKALSLVP---DIIISDVMMPEKDGLQMMRELHDNMTTSHIPM-VL 1297
Cdd:cd19933      4 LLVDDNAVNRMVTKGLLEKlGCEVTTVSSGEECL-NLLASAEhsfQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLiVA 82
                           90       100
                   ....*....|....*....|....*..
gi 1119624474 1298 LTAKTAIESMLEGLEYGADDYITKPFS 1324
Cdd:cd19933     83 LTANTDDSTREKCLSLGMNGVITKPVS 109
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
605-788 9.61e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 42.70  E-value: 9.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  605 CSKVRCITGDADGHIWI----GTTVGLLMVDDG-FDRPEDARFYHylrapekanalsnndIHWVKPTREGELYVATFGGG 679
Cdd:COG4257     16 GSGPRDVAVDPDGAVWFtdqgGGRIGRLDPATGeFTEYPLGGGSG---------------PHGIAVDPDGNLWFTDNGNN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474  680 LNQLVDLnAEGQARFKAYTVRDGLPSDILLsiqeDKKGQLWIS--TENGLSKFTPGLGRFENFQNKYSNSSIRfseaASA 757
Cdd:COG4257     81 RIGRIDP-KTGEITTFALPGGGSNPHGIAF----DPDGNLWFTdqGGNRIGRLDPATGEVTEFPLPTGGAGPY----GIA 151
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1119624474  758 YASDGNILFGTN--HGIFYFNPDSIQKSVYVPP 788
Cdd:COG4257    152 VDPDGNLWVTDFgaNAIGRIDPDTGTLTEYALP 184
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
1381-1478 1.08e-03

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 40.29  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1381 LMALMEKNLDNGdLIVDDLVKDMAVSRSVFFKKLKSLTGLAPVEFIKEMRINRAVQLIETGEYSMTQIAYMVGINDPRYF 1460
Cdd:PRK10219    10 LIAWIDEHIDQP-LNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTF 88
                           90
                   ....*....|....*...
gi 1119624474 1461 SKCFKQKMGMTPTEYRDR 1478
Cdd:PRK10219    89 SRVFRRQFDRTPSDYRHR 106
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
1222-1322 1.16e-03

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 40.78  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1222 MLLVEDNTE-LRTF---LRSIFASEFRVVEAANGAEGLE--KALSLVPDII---ISDVMMPEKDG---LQMMRELHdnmt 1289
Cdd:cd17595      3 ILTVDDDPQvLRAVardLRRQYGKDYRVLRADSGAEALDalKELKLRGEAValfLVDQRMPEMDGvefLEKAMELF---- 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1119624474 1290 tSHIPMVLLTAKTAIESMLEGL-EYGADDYITKP 1322
Cdd:cd17595     79 -PEAKRVLLTAYADTDAAIRAInDVQLDYYLLKP 111
PRK11697 PRK11697
two-component system response regulator BtsR;
1221-1343 1.96e-03

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 41.76  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1221 TMLLVEDNT----ELRTFLRSifASEFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMREL-HDNMttSHIp 1294
Cdd:PRK11697     3 KVLIVDDEPlareELRELLQE--EGDIEIVgECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLdPEHM--PYI- 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1295 mVLLTAKTaiESMLEGLEYGADDYITKPFSAtylkARVRNILER-RKKLQ 1343
Cdd:PRK11697    78 -VFVTAFD--EYAIKAFEEHAFDYLLKPIDP----ARLAKTLARlRQERS 120
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
34-57 2.38e-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: 36.91  E-value: 2.38e-03
                           10        20
                   ....*....|....*....|....
gi 1119624474   34 GLSENTVMDMLQDSRGNMWFSTWN 57
Cdd:pfam07494    1 GLPSNSVTSLLEDSDGRLWIGTNG 24
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
7-116 3.34e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 41.16  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474    7 LWMLAVLTAAVLKAQPE-GSFTHYSSDDGLSenTVMDMLQDSRGNMWFSTWNG--INKFDGYT--FKTFKarqdnqIALT 81
Cdd:COG4257    158 LWVTDFGANAIGRIDPDtGTLTEYALPTPGA--GPRGLAVDPDGNLWVADTGSgrIGRFDPKTgtVTEYP------LPGG 229
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1119624474   82 SNRVDNMKLDRYGFIWL-QTYDDRAFRFDPRTEVFE 116
Cdd:COG4257    230 GARPYGVAVDGDGRVWFaESGANRIVRFDPDTELTE 265
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
1064-1165 3.40e-03

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


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 38.90  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1064 FEKIVYNLLSNAFKYTPEGKMITV-------------FVHD--NGQTVSVGVQDQGIGIAENKKKSLFVRFenlvdsslF 1128
Cdd:cd16919      1 LELAILNLAVNARDAMPEGGRLTIetsnqrvdadyalNYRDliPGNYVCLEVSDTGSGMPAEVLRRAFEPF--------F 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1119624474 1129 NQ----SSSGIGLSLVKELVEMHKASITVDSKLGEGSCFKV 1165
Cdd:cd16919     73 TTkevgKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRI 113
Reg_prop pfam07494
Two component regulator propeller; A large group of two component regulator proteins appear to ...
452-469 4.64e-03

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


Pssm-ID: 400050 [Multi-domain]  Cd Length: 24  Bit Score: 35.75  E-value: 4.64e-03
                           10
                   ....*....|....*...
gi 1119624474  452 SNEVRALCEDKDGNMWVG 469
Cdd:pfam07494    4 SNSVTSLLEDSDGRLWIG 21
7tmD_STE3 cd14966
fungal a-factor pheromone receptor STE3, member of the class D family of seven-transmembrane G ...
900-937 8.22e-03

fungal a-factor pheromone receptor STE3, member of the class D family of seven-transmembrane G protein-coupled receptors; This subfamily represents the a-factor pheromone receptor encoded by the STE3 gene, which is required for pheromone sensing and mating in haploid cells of the yeast Saccharomyces cerevisiae. The STE3-encoded seven-transmembrane domain receptor is a member of the class D GPCRs. Class D receptors are composed of two major subfamilies: Ste2 and Ste3. These two GPCRs (Ste2 and Ste3) sense the polypeptide mating pheromones, alpha-factor and a-factor, which activate a G protein-coupled receptors on the surface of the opposite yeast-mating haploid-types (MATa and MAT-alpha), respectively. Activation of these receptors by pheromones leads to activation of the mitogen-activated protein kinase (MAPK) signal transduction cascades, G1 cell cycle arrest, and polarized cell growth in the direction of the partner cell (a process called shmooing), which ultimately induces cell-cell fusion and the formation of a diploid zygote. Like all GPCRs, these pheromone mating factor receptors possess the same basic architecture of seven-transmembrane (7TM) domains and share common signaling mechanisms; however, there is no significant sequence similarity either between Ste2 and Ste3, or between these two receptors and the other 7TM GPCRs. Thus, STE2 and STE3 represent phylogenetically distinct groups.


Pssm-ID: 320097  Cd Length: 259  Bit Score: 39.79  E-value: 8.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1119624474  900 LPSFWETPLAYFLYVLFFLLI-IVTAVYILFTIYRLKHR 937
Cdd:cd14966    144 YPAIYNSWPALVLVYIWPLIIsLIAAVYAVLTLRRFFRR 182
PRK14084 PRK14084
DNA-binding response regulator;
1223-1470 9.55e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 39.73  E-value: 9.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1223 LLVEDN----TELRTFLRSIfaSEFRVV-EAANGAEGLEKALSLVPDIIISDVMMPEKDGLQMMRELHdnmTTSHIPMVL 1297
Cdd:PRK14084     4 LIVDDEplarNELTYLLNEI--GGFEEInEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQ---KMKEPPAII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1298 LTakTAIESM-LEGLEYGADDYITKPFSATYLKARVRNILERRKKLQEmyreklmNMATSPDEPTVEESKAPEMSPNDRK 1376
Cdd:PRK14084    79 FA--TAHDQFaVKAFELNATDYILKPFEQKRIEQAVNKVRATKAKDDN-------NASAIANDMSANFDQSLPIEIDDKI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1377 FMDKLMALMEKNLDNGDLIVDDLVKDMAVSR--SVFFKKLKsltglaPVEFIKEMR---INRA-VQLIE-----TGEYSM 1445
Cdd:PRK14084   150 HMLNQQDIIAIGVHNGITTIHTTNHKYETTEplNRYEKRLN------PTYFIRIHRsyiINKKhIKEVEqwfnyTYQVIL 223
                          250       260
                   ....*....|....*....|....*.
gi 1119624474 1446 T-QIAYMVGindpRYFSKCFKQKMGM 1470
Cdd:PRK14084   224 TnGVKMQVS----RSFMKDFKASIGL 245
PRK15044 PRK15044
transcriptional regulator SirC; Provisional
1393-1475 9.63e-03

transcriptional regulator SirC; Provisional


Pssm-ID: 185004 [Multi-domain]  Cd Length: 295  Bit Score: 40.02  E-value: 9.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119624474 1393 DLIVDDLVKDMA---VSRSVFFK--KLKSLTGLAPVEFIK---EMRINRAVQLIETGEYSMTQIAYMVGINDPRYFSKCF 1464
Cdd:PRK15044   199 NIIISDLTRKWSqaeVAGKLFMSvsSLKRKLAAEEVSFSKiylDARMNQAIKLLRMGAGNISQVATMCGYDTPSYFIAIF 278
                           90
                   ....*....|.
gi 1119624474 1465 KQKMGMTPTEY 1475
Cdd:PRK15044   279 KRHFKITPLSF 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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