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Conserved domains on  [gi|2594348833|ref|WP_316931800|]
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MULTISPECIES: substrate-binding domain-containing protein [Bacteroides]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
27-295 5.20e-135

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


:

Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 405.39  E-value: 5.20e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCS-DDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQK 105
Cdd:cd06308     1 VIGFSQCSlNDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 106 GIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKA 185
Cdd:cd06308    81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPGIKIVASQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 186 DAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGKGNglELVLDNVLDATFIYP 265
Cdd:cd06308   161 DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDGLPEAGE--KAVKDGILAATFLYP 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 2594348833 266 TNGDKVMQLAMNILEKKSYPRETVMNTAVV 295
Cdd:cd06308   239 TGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
387-641 1.58e-63

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 217.85  E-value: 1.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 387 RDILEEQRDKLEEQRDQLIQLSHQLEEATHAKLVFFTNISHDFRTPLTLVADPVEHLLADssLSEDQRRMLLLVQRNVNI 466
Cdd:COG0642    79 LLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADR 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 467 LLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYmPDTDYRTLADVEKLERIYFNLLSNA 546
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDL-PDDLPTVRGDPDRLRQVLLNLLSNA 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 547 FKFTPENGKVTVRLSSltkdDHCWIRFTVANTGSMISAEHIRNIFDRFYKID--MHHAGSGIGLALVKAFVELHKGTITV 624
Cdd:COG0642   236 IKYTPEGGTVTVSVRR----EGDRVRISVEDTGPGIPPEDLERIFEPFFRTDpsRRGGGTGLGLAIVKRIVELHGGTIEV 311
                         250
                  ....*....|....*..
gi 2594348833 625 ESDEKQGTIFTVDLPVQ 641
Cdd:COG0642   312 ESEPGKGTTFTVTLPLA 328
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
708-909 1.51e-41

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: 151.26  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 708 KPCVLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVIL 786
Cdd:COG0745     1 MPRILVVEDDPDIReLLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRA--RPSDIPIIM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 787 LTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQFFGDGQTLAKEDVCDMDK--DFVEKFKALIEAK 864
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDLLDLAAREVTRDGEpvELTPKEFRLLELL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 865 MGDSNLNVedlgkdmglSRVQLYRKIKSLTNYSPNEL-LRIARLKK 909
Cdd:COG0745   159 MRNPGRVV---------SREQLLEEVWGYDYGDDRTVdVHISRLRK 195
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
870-954 3.45e-25

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 106.02  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 870 LNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPT 949
Cdd:COG2207   169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                  ....*
gi 2594348833 950 DLLKR 954
Cdd:COG2207   249 EYRKR 253
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
357-415 1.59e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 357 KSLRSKNRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEAT 415
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
 
Name Accession Description Interval E-value
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
27-295 5.20e-135

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 405.39  E-value: 5.20e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCS-DDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQK 105
Cdd:cd06308     1 VIGFSQCSlNDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 106 GIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKA 185
Cdd:cd06308    81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPGIKIVASQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 186 DAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGKGNglELVLDNVLDATFIYP 265
Cdd:cd06308   161 DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDGLPEAGE--KAVKDGILAATFLYP 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 2594348833 266 TNGDKVMQLAMNILEKKSYPRETVMNTAVV 295
Cdd:cd06308   239 TGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
2-300 4.12e-81

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 265.25  E-value: 4.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833   2 KYTKWITVLFCLLGLAAC--------RQDAPRFRIGVAQCS-DDSWRHKMNDEILREAMfYDGVSVEIRSAADDNRKQAE 72
Cdd:COG1879     2 RLALLAAVLALALALAACgsaaaeaaAAAAKGKTIGFVVKTlGNPFFVAVRKGAEAAAK-ELGVELIVVDAEGDAAKQIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  73 DVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVE 152
Cdd:COG1879    81 QIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 153 LTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE 232
Cdd:COG1879   161 LTGSPGAPAANERTDGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 233 KEMIFVGIDALPGkgnGLELVLDNVLDATFIYPTN--GDKVMQLAMNILEKKSYPRETVMNTAVVDRTNA 300
Cdd:COG1879   241 GDVKVVGFDGSPE---ALQAIKDGTIDATVAQDPYlqGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
387-641 1.58e-63

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 217.85  E-value: 1.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 387 RDILEEQRDKLEEQRDQLIQLSHQLEEATHAKLVFFTNISHDFRTPLTLVADPVEHLLADssLSEDQRRMLLLVQRNVNI 466
Cdd:COG0642    79 LLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADR 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 467 LLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYmPDTDYRTLADVEKLERIYFNLLSNA 546
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDL-PDDLPTVRGDPDRLRQVLLNLLSNA 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 547 FKFTPENGKVTVRLSSltkdDHCWIRFTVANTGSMISAEHIRNIFDRFYKID--MHHAGSGIGLALVKAFVELHKGTITV 624
Cdd:COG0642   236 IKYTPEGGTVTVSVRR----EGDRVRISVEDTGPGIPPEDLERIFEPFFRTDpsRRGGGTGLGLAIVKRIVELHGGTIEV 311
                         250
                  ....*....|....*..
gi 2594348833 625 ESDEKQGTIFTVDLPVQ 641
Cdd:COG0642   312 ESEPGKGTTFTVTLPLA 328
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
34-283 3.67e-48

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 172.11  E-value: 3.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  34 SDDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVD 113
Cdd:pfam13407   8 TGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAGIPVVTFD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 114 RKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAI-SNYPDIKLIDKADAA-WER 191
Cdd:pfam13407  88 SDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLkEKYPGIKVVAEVEGTnWDP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 192 EPAEVEMDSMLRRHP-KIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGkgnGLELVLDNVLDATFIY--PTNG 268
Cdd:pfam13407 168 EKAQQQMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPE---ALEAIKDGTIDATVLQdpYGQG 244
                         250
                  ....*....|....*
gi 2594348833 269 DKVMQLAMNILEKKS 283
Cdd:pfam13407 245 YAAVELAAALLKGKK 259
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
708-909 1.51e-41

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: 151.26  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 708 KPCVLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVIL 786
Cdd:COG0745     1 MPRILVVEDDPDIReLLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRA--RPSDIPIIM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 787 LTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQFFGDGQTLAKEDVCDMDK--DFVEKFKALIEAK 864
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDLLDLAAREVTRDGEpvELTPKEFRLLELL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 865 MGDSNLNVedlgkdmglSRVQLYRKIKSLTNYSPNEL-LRIARLKK 909
Cdd:COG0745   159 MRNPGRVV---------SREQLLEEVWGYDYGDDRTVdVHISRLRK 195
PRK15347 PRK15347
two component system sensor kinase;
388-813 5.63e-40

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 160.19  E-value: 5.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 388 DILEEQRDKLEEQrdqLIQLSHQLEEATHA-------KLVFFTNISHDFRTPLTLVADPVEhLLADSSLSEDQRRMLLLV 460
Cdd:PRK15347  364 DTLNEQYDTLENK---VAERTQALAEAKQRaeqankrKSEHLTTISHEIRTPLNGVLGALE-LLQNTPLTAEQMDLADTA 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 461 QRNVNILLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYMPDTDYRTLADVEKLERIYF 540
Cdd:PRK15347  440 RQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILV 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 541 NLLSNAFKFTPENGkvtVRLSSLTKDDHcwIRFTVANTGSMISAEHIRNIFDRFYKIDMHHAGSGIGLALVKAFVELHKG 620
Cdd:PRK15347  520 NLLGNAVKFTETGG---IRLRVKRHEQQ--LCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGG 594
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 621 TITVESDEKQGTIFTVDLPVQtcETVVSENSPAfSVSATSvtSTDATTSAVAGVPATPATSGYSGSSSLN---------- 690
Cdd:PRK15347  595 ELTLFSTPGVGSCFSLVLPLN--EYAPPEPLKG-ELSAPL--ALHRQLSAWGITCQPGHQNPALLDPELAylpgrlydll 669
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 691 DALTYEEEELEksyDSSKPC------VLIIDDnADIRLYVHG--LLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMP 762
Cdd:PRK15347  670 QQIIQGAPNEP---VINLPLqpwqlqILLVDD-VETNRDIIGmmLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMP 745
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 763 GMDGIECCRRLKSEL--QTCHIPVILLTACSLDEQRIQGYDGGADSYISKPFS 813
Cdd:PRK15347  746 GLDGLETTQLWRDDPnnLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVT 798
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
711-812 2.36e-35

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: 129.54  E-value: 2.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMITA 81
                          90       100
                  ....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPF 812
Cdd:cd17538    82 LDDREDRIRGLEAGADDFLSKPI 104
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
530-641 1.25e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 121.99  E-value: 1.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  530 ADVEKLERIYFNLLSNAFKFTPENGKVTVRLssltKDDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMH---HAGSGI 606
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTL----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRsrkIGGTGL 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2594348833  607 GLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:smart00387  77 GLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
535-640 2.36e-30

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: 115.67  E-value: 2.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTPEnGKVTVRLSSLTKD-DHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMH----HAGSGIGLA 609
Cdd:cd16922     1 LRQILLNLLGNAIKFTEE-GEVTLRVSLEEEEeDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSttrkYGGTGLGLA 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2594348833 610 LVKAFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:cd16922    80 ISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
530-642 4.52e-28

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: 108.99  E-value: 4.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 530 ADVEKLERIYFNLLSNAFKFTPENGKVTVRLssltkDDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMH-HAGSGIGL 608
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITVTL-----SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRgGGGTGLGL 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2594348833 609 ALVKAFVELHKGTITVESDEKQGTIFTVDLPVQT 642
Cdd:pfam02518  76 SIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
711-822 5.91e-28

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 108.78  E-value: 5.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqTCHIPVILLTA 789
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRR--DPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
pleD PRK09581
response regulator PleD; Reviewed
711-832 2.65e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 116.54  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDD-NADIRLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:PRK09581    5 ILVVDDiPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshrRLK 832
Cdd:PRK09581   85 LDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLT----RLK 123
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
870-954 3.45e-25

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 106.02  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 870 LNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPT 949
Cdd:COG2207   169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                  ....*
gi 2594348833 950 DLLKR 954
Cdd:COG2207   249 EYRKR 253
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
869-952 5.73e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 96.47  E-value: 5.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  869 NLNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESP 948
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 2594348833  949 TDLL 952
Cdd:smart00342  81 SEYR 84
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
367-639 9.27e-24

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: 105.55  E-value: 9.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 367 KELSEQKKQVEQQRdklEEQRdiLEEQRdKLEEQRDQLIQLSH---QLEEATHAKLVFFTNISHDFRTPLTLVADPVEHL 443
Cdd:TIGR01386 193 RRLSAVAARISPES---LDQR--LDPSR-APAELRELAQSFNAmlgRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVA 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 444 LADSSLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYMPd 523
Cdd:TIGR01386 267 LSQPRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEG- 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 524 tdyRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLssLTKDDHCWIRftVANTGSMISAEHIRNIFDRFYKIDM---- 599
Cdd:TIGR01386 346 ---LVRGDPQMFRRAISNLLSNALRHTPDGGTITVRI--ERRSDEVRVS--VSNPGPGIPPEHLSRLFDRFYRVDParsn 418
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2594348833 600 HHAGSGIGLALVKAFVELHKGTITVESDEkQGTIFTVDLP 639
Cdd:TIGR01386 419 SGEGTGLGLAIVRSIMEAHGGRASAESPD-GKTRFILRFP 457
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
65-261 9.86e-24

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 102.48  E-value: 9.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  65 DDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSL 144
Cdd:PRK10653   66 NNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 145 KGKGNVVELTGLGGSTPAMERHQGFMAAISNYpDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQ 224
Cdd:PRK10653  146 GEGAKVIQLEGIAGTSAARERGEGFKQAVAAH-KFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALR 224
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2594348833 225 AAKKAGREKEMIfVGIDalpGKGNGLELVLDNVLDAT 261
Cdd:PRK10653  225 ALQTAGKSDVMV-VGFD---GTPDGIKAVNRGKLAAT 257
HTH_18 pfam12833
Helix-turn-helix domain;
875-954 5.52e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 90.73  E-value: 5.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 875 LGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLA-SSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPTDLLK 953
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80

                  .
gi 2594348833 954 R 954
Cdd:pfam12833  81 R 81
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
391-639 2.75e-18

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 88.73  E-value: 2.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 391 EEQRDKLEEQRDQLIQLSHQLEEATHAklvFFTNISHDFRTPLTLVADPVEHLlaDSSLSEDQRRMLLLVQRNVNILLRL 470
Cdd:NF012163  216 NDELGKLAQDFNQLASTLEKNEQMRRD---FMADISHELRTPLAVLRAELEAI--QDGIRKFTPESLDSLQAEVGTLTKL 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 471 VNQILDFRKYENGKMEYTPISLD----ILSSFEGWNESFmaVARKKHIHFSfdyMPDTDYrTLADVEKLERIYFNLLSNA 546
Cdd:NF012163  291 VDDLHDLSMSDEGALAYQKASVDlvplLEVEGGAFRERF--ASAGLELEVS---LPDSSL-VFGDRDRLMQLFNNLLENS 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 547 FKFTPENGKVTVRLSSLTKDdhcwIRFTVANTGSMISAEHIRNIFDRFYKIDMHH----AGSGIGLALVKAFVELHKGTI 622
Cdd:NF012163  365 LRYTDSGGSLHISASQRPKE----VTLTVADSAPGVSDEQLARLFERFYRVEVSRnrasGGSGLGLAISLNIVQAHGGTL 440
                         250
                  ....*....|....*..
gi 2594348833 623 TVESDEKQGTIFTVDLP 639
Cdd:NF012163  441 HAAHSPLGGLRIVVTLP 457
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
711-762 7.44e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.05  E-value: 7.44e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833  711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMP 762
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
711-824 1.36e-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: 62.89  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNAD----IRLYVHglLHTDYTVIEAA-DGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVI 785
Cdd:TIGR02875   5 IVIADDNKEfcnlLKEYLA--AQPDMEVVGVAhNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARPRVI 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2594348833 786 LLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNL 824
Cdd:TIGR02875  83 MLSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQL 121
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
873-951 4.83e-10

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 61.62  E-value: 4.83e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 873 EDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPTDL 951
Cdd:PRK13503  191 EALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDI 269
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
357-415 1.59e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 357 KSLRSKNRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEAT 415
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
357-415 7.29e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.29  E-value: 7.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 357 KSLRSKNRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLI----QLSHQLEEAT 415
Cdd:pfam20492  27 EELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAeekeQLEAELAEAQ 89
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
356-406 5.31e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.16  E-value: 5.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2594348833 356 YKSLRSKNR-LNKELSEQKKQVEQQRDK---LEEQRDILEEQRDKLEEQRDQLIQ 406
Cdd:cd22887    20 LASLEEEIKdLEEELKEKNKANEILNDEliaLQIENNLLEEKLRKLQEENDELVE 74
 
Name Accession Description Interval E-value
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
27-295 5.20e-135

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 405.39  E-value: 5.20e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCS-DDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQK 105
Cdd:cd06308     1 VIGFSQCSlNDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 106 GIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKA 185
Cdd:cd06308    81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPGIKIVASQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 186 DAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGKGNglELVLDNVLDATFIYP 265
Cdd:cd06308   161 DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDGLPEAGE--KAVKDGILAATFLYP 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 2594348833 266 TNGDKVMQLAMNILEKKSYPRETVMNTAVV 295
Cdd:cd06308   239 TGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
2-300 4.12e-81

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 265.25  E-value: 4.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833   2 KYTKWITVLFCLLGLAAC--------RQDAPRFRIGVAQCS-DDSWRHKMNDEILREAMfYDGVSVEIRSAADDNRKQAE 72
Cdd:COG1879     2 RLALLAAVLALALALAACgsaaaeaaAAAAKGKTIGFVVKTlGNPFFVAVRKGAEAAAK-ELGVELIVVDAEGDAAKQIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  73 DVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVE 152
Cdd:COG1879    81 QIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 153 LTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE 232
Cdd:COG1879   161 LTGSPGAPAANERTDGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 233 KEMIFVGIDALPGkgnGLELVLDNVLDATFIYPTN--GDKVMQLAMNILEKKSYPRETVMNTAVVDRTNA 300
Cdd:COG1879   241 GDVKVVGFDGSPE---ALQAIKDGTIDATVAQDPYlqGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
27-294 1.78e-74

periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 245.55  E-value: 1.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCS-DDSWRHKMNDEILREAMFYdGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQK 105
Cdd:cd01536     1 KIGVVVKDlTNPFWVAVKKGAEAAAKEL-GVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 106 GIPVILVDRKI-LSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDK 184
Cdd:cd01536    80 GIPVVAVDTDIdGGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYPDIEIVAE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 185 ADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPgkgNGLELVLDNVLDAT-FI 263
Cdd:cd01536   160 QPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDGTP---EALKAIKDGELDATvAQ 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2594348833 264 YPTN-GDKVMQLAMNILEKKSYPRETVMNTAV 294
Cdd:cd01536   237 DPYLqGYLAVEAAVKLLNGEKVPKEILTPVTL 268
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
27-300 7.09e-64

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 217.09  E-value: 7.09e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCSDDS-WRHKMNDEILREAMFYdGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQK 105
Cdd:cd06309     1 TVGFSQAGSESpWRVANTKSIKEAAKKR-GYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 106 GIPVILVDRKIL---SDKYTAYIGADNYEIGRAVGNYIASSLK-GKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKL 181
Cdd:cd06309    80 GIPVILVDRTIDgedGSLYVTFIGSDFVEEGRRAAEWLVKNYKgGKGNVVELQGTAGSSVAIDRSKGFREVIKKHPNIKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 182 IDKADAAWEREPAEVEMDSMLRRHP-KIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALPgkgNGLELVLDNVL 258
Cdd:cd06309   160 VASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLKpgKDVLVVGIDGQK---DALEAIKAGEL 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2594348833 259 DATFIY-PTNGDKVMQLAMNILEKKSYPRETVMNTAVVDRTNA 300
Cdd:cd06309   237 NATVECnPLFGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNA 279
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
387-641 1.58e-63

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 217.85  E-value: 1.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 387 RDILEEQRDKLEEQRDQLIQLSHQLEEATHAKLVFFTNISHDFRTPLTLVADPVEHLLADssLSEDQRRMLLLVQRNVNI 466
Cdd:COG0642    79 LLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADR 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 467 LLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYmPDTDYRTLADVEKLERIYFNLLSNA 546
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDL-PDDLPTVRGDPDRLRQVLLNLLSNA 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 547 FKFTPENGKVTVRLSSltkdDHCWIRFTVANTGSMISAEHIRNIFDRFYKID--MHHAGSGIGLALVKAFVELHKGTITV 624
Cdd:COG0642   236 IKYTPEGGTVTVSVRR----EGDRVRISVEDTGPGIPPEDLERIFEPFFRTDpsRRGGGTGLGLAIVKRIVELHGGTIEV 311
                         250
                  ....*....|....*..
gi 2594348833 625 ESDEKQGTIFTVDLPVQ 641
Cdd:COG0642   312 ESEPGKGTTFTVTLPLA 328
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
403-642 2.37e-61

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 208.61  E-value: 2.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 403 QLIQLSHQLEEATHAKLVFFTNISHDFRTPLTLVADPVEHLLADSSLS-EDQRRMLLLVQRNVNILLRLVNQILDFRKYE 481
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSpEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 482 NGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYmPDTDYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLS 561
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDL-PPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 562 SltkdDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDM--HHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:COG2205   160 R----EGDGVRISVSDNGPGIPEEELERIFERFYRGDNsrGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLP 235

                  ...
gi 2594348833 640 VQT 642
Cdd:COG2205   236 LAE 238
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
385-640 1.85e-58

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 205.94  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 385 EQRDILEEQRdkLEEQRDQliqlshqleeathaklvFFTNISHDFRTPLTLVADPVEHLL-ADSSLSEDQRRMLLLVQRN 463
Cdd:COG5002   151 VERDITELER--LEQMRRE-----------------FVANVSHELRTPLTSIRGYLELLLdGAADDPEERREYLEIILEE 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 464 VNILLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDyMPDTDYRTLADVEKLERIYFNLL 543
Cdd:COG5002   212 AERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELD-LPEDPLLVLGDPDRLEQVLTNLL 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 544 SNAFKFTPENGKVTVRLSSltkdDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMHHA----GSGIGLALVKAFVELHK 619
Cdd:COG5002   291 DNAIKYTPEGGTITVSLRE----EDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSretgGTGLGLAIVKHIVEAHG 366
                         250       260
                  ....*....|....*....|.
gi 2594348833 620 GTITVESDEKQGTIFTVDLPV 640
Cdd:COG5002   367 GRIWVESEPGKGTTFTITLPL 387
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
55-261 7.51e-53

periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380546 [Multi-domain]  Cd Length: 268  Bit Score: 185.96  E-value: 7.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGR 134
Cdd:cd06323    29 GVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSVTGGKVVSHIASDNVAGGE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 AVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAH 214
Cdd:cd06323   109 MAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYPKINVVASQTADFDRTKGLNVMENLLQAHPDIDAVFAH 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2594348833 215 NDRIAPGAYQAAKKAGReKEMIFVGIDALPgkgNGLELVLDNVLDAT 261
Cdd:cd06323   189 NDEMALGAIQALKAAGR-KDVIVVGFDGTP---DAVKAVKDGKLAAT 231
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
36-299 3.59e-52

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 185.14  E-value: 3.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  36 DSWRHKMNDEILREA--MFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVD 113
Cdd:cd19996    11 NSWRVQMIAEFEAEAakLKKLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 114 RKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREP 193
Cdd:cd19996    91 SGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPGIKIVGEVYADWDYAK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 194 AEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKeMIFVGiDALPG------KGNGLELVldnvldaTFIYPT- 266
Cdd:cd19996   171 AKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPL-VPMTG-EDNNGflkawkELPGFKSI-------APSYPPw 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2594348833 267 NGDKVMQLAMNILEKKSYPRETVMNTAVVDRTN 299
Cdd:cd19996   242 LGATALDAALAALEGEPVPKYVYIPLPVITDEN 274
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
34-283 3.67e-48

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 172.11  E-value: 3.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  34 SDDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVD 113
Cdd:pfam13407   8 TGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAGIPVVTFD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 114 RKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAI-SNYPDIKLIDKADAA-WER 191
Cdd:pfam13407  88 SDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLkEKYPGIKVVAEVEGTnWDP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 192 EPAEVEMDSMLRRHP-KIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGkgnGLELVLDNVLDATFIY--PTNG 268
Cdd:pfam13407 168 EKAQQQMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPE---ALEAIKDGTIDATVLQdpYGQG 244
                         250
                  ....*....|....*
gi 2594348833 269 DKVMQLAMNILEKKS 283
Cdd:pfam13407 245 YAAVELAAALLKGKK 259
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
42-290 3.41e-47

periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 169.87  E-value: 3.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  42 MNDEILREAMFYdGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKY 121
Cdd:cd19968    17 MHEQAVDEAAKL-GVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVDRRAEGAAP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 122 TAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSM 201
Cdd:cd19968    96 VPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGPKIKVVFEQTGNFERDEGLTVMENI 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 202 LRRHP-KIDAVYAHNDRIAPGAYQAAKKAG-REKEMIFVGIDALPgkgNGLELVLDNVLDATFIYPTNGD--KVMQLAMN 277
Cdd:cd19968   176 LTSLPgPPDAIICANDDMALGAIEAMRAAGlDLKKVKVIGFDAVP---DALQAIKDGELYATVEQPPGGQarTALRILVD 252
                         250
                  ....*....|...
gi 2594348833 278 ILEKKSYPRETVM 290
Cdd:cd19968   253 YLKDKKAPKKVNL 265
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
27-300 2.36e-46

periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 167.45  E-value: 2.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQcsdDSWRHKMNDEILREAMFY---DGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAY 103
Cdd:cd06313     1 KIGFTV---YGLSSEFITNLVEAMKAVakeLNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 104 QKGIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLID 183
Cdd:cd06313    78 EAGIPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYPDIKVLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 184 KADAAWEREPAEVEMDSMLRRHP-KIDAVYAHNDRIAPGAYQAAKKAGReKEMIFVGIDALPgkgNGLELVLDNVLDATF 262
Cdd:cd06313   158 EQTANWSRDEAMSLMENWLQAYGdEIDGIIAQNDDMALGALQAVKAAGR-DDIPVVGIDGIE---DALQAVKSGELIATV 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2594348833 263 IY--PTNGDKVMQLAMNILEKKSYPRETVMNTAVVDRTNA 300
Cdd:cd06313   234 LQdaEAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDNV 273
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
28-261 1.36e-44

periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.


Pssm-ID: 380524 [Multi-domain]  Cd Length: 272  Bit Score: 162.40  E-value: 1.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  28 IGVA-QCSDDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKG 106
Cdd:cd06301     3 IGVSmQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 107 IPVILVDRKILS-DKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKA 185
Cdd:cd06301    83 IPLVYVNREPDSkPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYPGMKIVAEQ 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833 186 DAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPgkgNGLELVLDNVLDAT 261
Cdd:cd06301   163 TANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDDILVAGIDATP---DALKAMKAGRLDAT 235
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
54-295 4.26e-44

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 160.68  E-value: 4.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  54 DGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLI-ISANEAAPMTPiVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEI 132
Cdd:cd19972    28 KGYKVITVDAKGDSATQVNQIQDLITQNIDALIyIPAGATAAAVP-VKAARAAGIPVIAVDRNPEDAPGDTFIATDSVAA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 133 GRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAW-EREPAEVEMDsMLRRHPKIDAV 211
Cdd:cd19972   107 AKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEAPGIKVVAEQTADWdQDEGFKVAQD-MLQANPNITVF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 212 YAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGkgnGLELVLDNVLDATFIYPTN--GDKVMQLAMNILEKKSYPRETV 289
Cdd:cd19972   186 FGQSDAMALGAAQAVKVAGLDHKIWVVGFDGDVA---GLKAVKDGVLDATMTQQTQkmGRLAVDSAIDLLNGKAVPKEQL 262

                  ....*.
gi 2594348833 290 MNTAVV 295
Cdd:cd19972   263 QDAVLT 268
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
42-292 3.16e-43

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 158.13  E-value: 3.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  42 MNDEIlREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKY 121
Cdd:cd19971    17 INDGI-KKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPVKDTDL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 122 -TAYIGADNYEIGRAVGNYIASSLKGKGNVVELTgLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDS 200
Cdd:cd19971    96 vDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLD-HPTAESCVDRIDGFLDAIKKNPKFEVVAQQDGKGQLEVAMPIMED 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 201 MLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALP-GKgnglELVLDNVLDATFI-YPTN-GDKVMQLAMN 277
Cdd:cd19971   175 ILQAHPDLDAVFALNDPSALGALAALKAAGKLGDILVYGVDGSPdAK----AAIKDGKMTATAAqSPIEiGKKAVETAYK 250
                         250
                  ....*....|....*
gi 2594348833 278 ILEKKSYPRETVMNT 292
Cdd:cd19971   251 ILNGEKVEKEIVVPT 265
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
62-239 8.25e-43

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 157.14  E-value: 8.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  62 SAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIA 141
Cdd:cd06311    36 VTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEYIG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 142 SSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPG 221
Cdd:cd06311   116 KKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNPGIKILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIG 195
                         170
                  ....*....|....*...
gi 2594348833 222 AYQAAKKAGREKEMIFVG 239
Cdd:cd06311   196 VLQAIKEAGRTDIKVMTG 213
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
708-909 1.51e-41

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: 151.26  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 708 KPCVLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVIL 786
Cdd:COG0745     1 MPRILVVEDDPDIReLLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRA--RPSDIPIIM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 787 LTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQFFGDGQTLAKEDVCDMDK--DFVEKFKALIEAK 864
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDLLDLAAREVTRDGEpvELTPKEFRLLELL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 865 MGDSNLNVedlgkdmglSRVQLYRKIKSLTNYSPNEL-LRIARLKK 909
Cdd:COG0745   159 MRNPGRVV---------SREQLLEEVWGYDYGDDRTVdVHISRLRK 195
PRK15347 PRK15347
two component system sensor kinase;
388-813 5.63e-40

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 160.19  E-value: 5.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 388 DILEEQRDKLEEQrdqLIQLSHQLEEATHA-------KLVFFTNISHDFRTPLTLVADPVEhLLADSSLSEDQRRMLLLV 460
Cdd:PRK15347  364 DTLNEQYDTLENK---VAERTQALAEAKQRaeqankrKSEHLTTISHEIRTPLNGVLGALE-LLQNTPLTAEQMDLADTA 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 461 QRNVNILLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYMPDTDYRTLADVEKLERIYF 540
Cdd:PRK15347  440 RQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILV 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 541 NLLSNAFKFTPENGkvtVRLSSLTKDDHcwIRFTVANTGSMISAEHIRNIFDRFYKIDMHHAGSGIGLALVKAFVELHKG 620
Cdd:PRK15347  520 NLLGNAVKFTETGG---IRLRVKRHEQQ--LCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGG 594
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 621 TITVESDEKQGTIFTVDLPVQtcETVVSENSPAfSVSATSvtSTDATTSAVAGVPATPATSGYSGSSSLN---------- 690
Cdd:PRK15347  595 ELTLFSTPGVGSCFSLVLPLN--EYAPPEPLKG-ELSAPL--ALHRQLSAWGITCQPGHQNPALLDPELAylpgrlydll 669
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 691 DALTYEEEELEksyDSSKPC------VLIIDDnADIRLYVHG--LLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMP 762
Cdd:PRK15347  670 QQIIQGAPNEP---VINLPLqpwqlqILLVDD-VETNRDIIGmmLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMP 745
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 763 GMDGIECCRRLKSEL--QTCHIPVILLTACSLDEQRIQGYDGGADSYISKPFS 813
Cdd:PRK15347  746 GLDGLETTQLWRDDPnnLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVT 798
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
28-299 6.29e-40

periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380541 [Multi-domain]  Cd Length: 282  Bit Score: 149.10  E-value: 6.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  28 IGVAQCSDDS-WRHKMNDEILREAMfYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKG 106
Cdd:cd06318     2 IGFSQRTLASpYYAALVAAAKAEAK-KLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 107 IPVILVDRKILSD-KYTAYIGADNYEIGRAVGNYIASSLKGK-GNVVELTGLGGSTPAMERHQGFMAAISNYP------- 177
Cdd:cd06318    81 IPVITVDSALDPSaNVATQVGRDNKQNGVLVGKEAAKALGGDpGKIIELSGDKGNEVSRDRRDGFLAGVNEYQlrkygks 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 178 DIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPgkgNGLELVLDNV 257
Cdd:cd06318   161 NIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAGADGQK---EALKLIKDGK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2594348833 258 LDATFIY-PTN-GDKVMQLAMNILE-KKSYPRETVMNTAVVDRTN 299
Cdd:cd06318   238 YVATGLNdPDLlGKTAVDTAAKVVKgEESFPEFTYTPTALITKDN 282
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
708-821 8.28e-40

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 145.44  E-value: 8.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 708 KPCVLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVIL 786
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAaGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2594348833 787 LTACSLDEQRIQGYDGGADSYISKPFSSQLLLARV 821
Cdd:COG3706    81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
705-833 9.73e-40

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: 146.85  E-value: 9.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 705 DSSKPCVLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIP 783
Cdd:COG3437     3 TGQAPTVLIVDDDPENLELLRQLLRTlGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIP 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2594348833 784 VILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQ 833
Cdd:COG3437    83 VIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRE 132
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
383-831 3.00e-38

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 155.28  E-value: 3.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  383 LEEQRDILEeqrdKLEEQRDQLIQlshqleeATHAKLVFFTNISHDFRTPLTLVADPVEhLLADSSLSEDQR-RMLLLVQ 461
Cdd:PRK09959   688 ITETRDLIH----ALEVERNKAIN-------ATVAKSQFLATMSHEIRTPISSIMGFLE-LLSGSGLSKEQRvEAISLAY 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  462 RNVNILLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYMPDTDYRTLADVEKLERIYFN 541
Cdd:PRK09959   756 ATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSN 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  542 LLSNAFKFTPENG-KVTVRLSSLtKDDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDM--HHAGSGIGLALVKAFVELH 618
Cdd:PRK09959   836 LLSNALKFTTEGAvKITTSLGHI-DDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAgrQQTGSGLGLMICKELIKNM 914
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  619 KGTITVESDEKQGTIFTVDLPVQTCETVvsenspafsvsatsvtstdATTSAVAGVPATpatsgysgsssLNDALTyeee 698
Cdd:PRK09959   915 QGDLSLESHPGIGTTFTITIPVEISQQV-------------------ATVEAKAEQPIT-----------LPEKLS---- 960
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  699 eleksydsskpcVLIIDDNADIRLYVHGLLH-TDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSel 777
Cdd:PRK09959   961 ------------ILIADDHPTNRLLLKRQLNlLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLRE-- 1026
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  778 QTCHIPVILLTACSLDEQRIQGYDGGADSYISKPFSSQLL------LARVRNLIDSHRRL 831
Cdd:PRK09959  1027 QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLkthlsqLHQVAHIAPQYRHL 1086
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
55-281 7.14e-38

D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 142.85  E-value: 7.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLII-SANEAAPMTPiVEEAYQKGIPVILVDRKI-LSDKYTAYIGADNYEI 132
Cdd:cd19967    29 GYEVTVFDHQNDTAKEAELFDTAIASGAKAIILdPADADASIAA-VKKAKDAGIPVFLIDREInAEGVAVAQIVSDNYQG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 133 GRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVY 212
Cdd:cd19967   108 AVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQYPELKMVAQQSADWDRTEAFEKMESILQANPDIKGVI 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 213 AHNDRIAPGAYQAAKKAGREKEMIFVGIDalpGKGNGLELVLDNVLDATFIYPTngDKVMQLAMNILEK 281
Cdd:cd19967   188 CGNDEMALGAIAALKAAGRAGDVIIVGFD---GSNDVRDAIKEGKISATVLQPA--KLIARLAVEQADQ 251
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
27-232 1.02e-36

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380654 [Multi-domain]  Cd Length: 313  Bit Score: 140.91  E-value: 1.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCS-DDSWRHKMNDEILREAMFY--DGVSVE--IRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEE 101
Cdd:cd19999     1 VIGVSNGYvGNEWRAQMIADFEEVAAEYkeEGVISDliVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 102 AYQKGIPVILVDRKIlSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKL 181
Cdd:cd19999    81 AQAAGILVVSFDQPV-SSPDAINVVIDQYKWAAIQAQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKYPGIKV 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 182 IDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHnDRIAPGAYQAAKKAGRE 232
Cdd:cd19999   160 LASVPGGWDQATAQQVMATLLATYPDIDGVLTQ-DGMAEGVLRAFQAAGKD 209
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
54-244 1.05e-36

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 139.72  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  54 DGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIG 133
Cdd:cd06322    28 LGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDVKADGAKVVTHVGTDNYAGG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 134 RAVGNYIA-SSLKGKGNVVELTGLgGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVY 212
Cdd:cd06322   108 KLAGEYALkALLGGGGKIAIIDYP-EVESVVLRVNGFKEAIKKYPNIEIVAEQPGDGRREEALAATEDMLQANPDLDGIF 186
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2594348833 213 AHNDRIAPGAYQAAKKAGREKEMIFVGIDALP 244
Cdd:cd06322   187 AIGDPAALGALTAIESAGKEDKIKVIGFDGNP 218
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
705-830 1.82e-36

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: 133.82  E-value: 1.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 705 DSSKPCVLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIP 783
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERlGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIP 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2594348833 784 VILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRR 830
Cdd:COG0784    82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
55-296 1.87e-36

periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).


Pssm-ID: 380537 [Multi-domain]  Cd Length: 271  Bit Score: 138.87  E-value: 1.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVE-IRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIG 133
Cdd:cd06314    29 GVNVEfVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDAPDSKRLAYIGTDNYEAG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 134 RAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLI----DKADAAwerePAEVEMDSMLRRHPKID 209
Cdd:cd06314   109 REAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSPGIEIVdplsDNDDIA----KAVQNVEDILKANPDLD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 210 A---VYAHNdriAPGAYQAAKKAGREKEMIFVGIDALPgkgNGLELVLDNVLDATFI-YPTN-GDKVMQLAMNILE-KKS 283
Cdd:cd06314   185 AifgVGAYN---GPAIAAALKDAGKVGKVKIVGFDTLP---ETLQGIKDGVIAATVGqRPYEmGYLSVKLLYKLLKgGKP 258
                         250
                  ....*....|...
gi 2594348833 284 YPRETVMNTAVVD 296
Cdd:cd06314   259 VPDVIDTGVDVVT 271
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
55-300 4.02e-36

periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 138.16  E-value: 4.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQ-----AEDVhyfIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSD-------KYT 122
Cdd:cd06320    29 GVKVDVQAAPSETDTQgqlnlLETM---LNKGYDAILVSPISDTNLIPPIEKANKKGIPVINLDDAVDADalkkaggKVT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 123 AYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSML 202
Cdd:cd06320   106 SFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKAPGLKLVASQPADWDRTKALDAATAIL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 203 RRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDalpGKGNGLELVLDNVLDATFIY--PTNGDKVMQLAMNILE 280
Cdd:cd06320   186 QAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVGTD---GIPEAKKSIKAGELTATVAQypYLEGAMAVEAALRLLQ 262
                         250       260
                  ....*....|....*....|
gi 2594348833 281 KKSYPRETVMNTAVVDRTNA 300
Cdd:cd06320   263 GQKVPAVVATPQALITKDNV 282
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
55-244 9.22e-36

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 136.65  E-value: 9.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDrkILSDKYTAYIGADNYEIGR 134
Cdd:cd06321    31 GAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAVD--VAAEGADATVTTDNVQAGY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 AVGNYIASSLKGKGNVVELTGLGgSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAH 214
Cdd:cd06321   109 LACEYLVEQLGGKGKVAIIDGPP-VSAVIDRVNGCKEALAEYPGIKLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAI 187
                         170       180       190
                  ....*....|....*....|....*....|
gi 2594348833 215 NDRIAPGAYQAAKKAGReKEMIFVGIDALP 244
Cdd:cd06321   188 NDPGAIGALLAAQQAGR-DDIVITSVDGSP 216
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
27-242 1.36e-35

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 136.95  E-value: 1.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCSDDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKG 106
Cdd:cd19992     1 KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 107 IPVILVDRKILSDKYTAYIGADNYEIGRAVGNYiASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPD---IKLI- 182
Cdd:cd19992    81 VPVISYDRLILNADVDLYVGRDNYKVGQLQAEY-ALEAVPKGNYVILSGDPGDNNAQLITAGAMDVLQPAIDsgdIKIVl 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 183 DKADAAWEREPAEVEMDSML-RRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDA 242
Cdd:cd19992   160 DQYVKGWSPDEAMKLVENALtANNNNIDAVLAPNDGMAGGAIQALKAQGLAGKVFVTGQDA 220
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
711-812 2.36e-35

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: 129.54  E-value: 2.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMITA 81
                          90       100
                  ....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPF 812
Cdd:cd17538    82 LDDREDRIRGLEAGADDFLSKPI 104
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
387-889 2.83e-34

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 141.23  E-value: 2.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 387 RDILEEQRdkleeqrdqliqlsHQ--LEEATHAKLVFFTNISHDFRTPLT-LVAdpVEHLLADSSLSEDQRRMLLLVQRN 463
Cdd:PRK11091  264 RDITERKR--------------YQdaLEKASRDKTTFISTISHELRTPLNgIVG--LSRILLDTELTAEQRKYLKTIHVS 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 464 VNILLRLVNQILDFRKYENGKMEYTPISLDiLSSFEGWNESFMAV-ARKKHIHFSFDYMPDTDYRTLADVEKLERIYFNL 542
Cdd:PRK11091  328 AITLGNIFNDIIDMDKMERRKLQLDNQPID-FTDFLADLENLSGLqAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNL 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 543 LSNAFKFTPEnGKVTVRLSSLTKDDhcwIRFTVANTGSMISAEHIRNIFDRFYKI-DMH---HA-GSGIGLALVKAFVEL 617
Cdd:PRK11091  407 ISNAVKFTQQ-GGVTVRVRYEEGDM---LTFEVEDSGIGIPEDELDKIFAMYYQVkDSHggkPAtGTGIGLAVSKRLAQA 482
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 618 HKGTITVESDEKQGTIFTVDLPVQTCETVVsenspafsvsatsvtstdattsavagvpatpatsgysgssslndaltyEE 697
Cdd:PRK11091  483 MGGDITVTSEEGKGSCFTLTIHAPAVAEEV------------------------------------------------ED 514
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 698 EELEKSYDSSKPCVLIIDdnaDIRLYV---HGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRL 773
Cdd:PRK11091  515 AFDEDDMPLPALNILLVE---DIELNVivaRSVLEKlGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIAREL 591
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 774 KSELQTCHI-PVILLTACSLDEQriQGY-DGGADSYISKPFSsqlllarVRNLIDShrrLKQFFGDGQTlakEDVCDMDK 851
Cdd:PRK11091  592 RERYPREDLpPLVALTANVLKDK--KEYlDAGMDDVLSKPLS-------VPALTAM---IKKFWDTQDD---EESTVTTE 656
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 2594348833 852 DFVEKFKALIEAKMgdsnLN--VEDLGKDMGLSRVQLYRK 889
Cdd:PRK11091  657 ESSKANEALLDIPM----LEqyVELVGPKLITDSLAVFEK 692
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
376-641 3.59e-34

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 137.99  E-value: 3.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 376 VEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEathaklvfFTNI-SHDFRTPLTLVADPVEHLLAD--SSLSED 452
Cdd:COG4251   247 LLILVLELLELRLELEELEEELEERTAELERSNEELEQ--------FAYVaSHDLREPLRKISGFSQLLEEDygDKLDEE 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 453 QRRMLLLVQRNVNILLRLVNQILDFRKYENGKMEYTPISL-----DILSSFEgwnesfmAVARKKHIHFSFDYMPdtdyR 527
Cdd:COG4251   319 GREYLERIRDAAERMQALIDDLLAYSRVGRQELEFEPVDLnelleEVLEDLE-------PRIEERGAEIEVGPLP----T 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 528 TLADVEKLERIYFNLLSNAFKFTPENGKVTVRLSSLTKDDHCwiRFTVANTGSMISAEHIRNIFDRFYKidMHHA----G 603
Cdd:COG4251   388 VRGDPTLLRQVFQNLISNAIKYSRPGEPPRIEIGAEREGGEW--VFSVRDNGIGIDPEYAEKIFEIFQR--LHSRdeyeG 463
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2594348833 604 SGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:COG4251   464 TGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKA 501
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
55-261 1.22e-33

monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380624 [Multi-domain]  Cd Length: 278  Bit Score: 130.92  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAA--DDNRKQA--EDVhyfIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNY 130
Cdd:cd19969    29 GVKTEYTGPAtaDVNEQITaiEQA---IAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGTDNY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 131 EIGRAVGNYIASSLKGKGNVVELTGLGgsTPAM-ERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKID 209
Cdd:cd19969   106 EAGYAAAEKLAELLGGKGKVAVLTGPG--QPNHeERVEGFKEAFAEYPGIEVVAVGDDNDDPEKAAQNTSALLQAHPDLV 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 210 AVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGKgngLELVLDNVLDAT 261
Cdd:cd19969   184 GIFGVDASGGVGAAQAVREAGKTGKVKIVAFDDDPET---LDLIKDGVIDAS 232
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
711-812 1.64e-33

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: 124.55  E-value: 1.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLrAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                          90       100
                  ....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPF 812
Cdd:cd19920    81 LTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
712-811 5.40e-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: 122.90  E-value: 5.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 712 LIIDDNADIRLYV-HGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTAC 790
Cdd:cd17574     1 LVVEDDEEIAELLsDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAK 78
                          90       100
                  ....*....|....*....|.
gi 2594348833 791 SLDEQRIQGYDGGADSYISKP 811
Cdd:cd17574    79 DEEEDKVLGLELGADDYITKP 99
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
27-300 8.87e-33

periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380523 [Multi-domain]  Cd Length: 302  Bit Score: 128.98  E-value: 8.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQC-SDDSWRHKMNDEILREAM--FYDGV--SVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEE 101
Cdd:cd06300     1 TIGLSNTyAGNSWREQMIASLKADAAqsGQKGLvkELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 102 AYQKGIPVILVDrKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKL 181
Cdd:cd06300    81 AADAGIPVVAFD-GAVTSPDAYNVSNDQVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYPGIKV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 182 IDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRiAPGAYQAAKKAGRekEMIFVGIDALPGKGNGLELVLDNVL--D 259
Cdd:cd06300   160 VGEVFGGWDEATAQTAMLDFLATHPQVDGVWTQGGE-DTGVLQAFQQAGR--PPVPIVGGDENGFAKQWWKHPKKGLtgA 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2594348833 260 ATFIYPTNGDKVMQLAMNILE-KKSYPRETVMNTAVVDRTNA 300
Cdd:cd06300   237 AVWPPPAIGAAGLEVALRLLEgQGPKPQSVLLPPPLITNDDA 278
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
55-242 9.60e-33

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 128.12  E-value: 9.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNR--KQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEI 132
Cdd:cd20004    29 GVEIYWRGPSREDDveAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSDLGGDAVISFVATDNYAA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 133 GRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFM-AAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAV 211
Cdd:cd20004   109 GRLAAKRMAKLLNGKGKVALLRLAKGSASTTDRERGFLeALKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGI 188
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2594348833 212 YAHNDRIAPGAYQAAKKAGREKEMIFVGIDA 242
Cdd:cd20004   189 FTPNESTTIGALRALRRLGLAGKVKFIGFDA 219
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
65-297 1.08e-32

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 128.10  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  65 DDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSL 144
Cdd:cd20006    43 EDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 145 KGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQ 224
Cdd:cd20006   123 GEKGKVAIVSFVKGSSTAIEREEGFKQALAEYPNIKIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAAR 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2594348833 225 AAKKAGREKEMIFVGIDALPGKGNGLElvlDNVLDATFIY-PTN-GDKVMQLAMNILEKKSYPRETVMNTAVVDR 297
Cdd:cd20006   203 ALKELGLGGKVKVVGFDSSVEEIQLLE---EGIIDALVVQnPFNmGYLSVQAAVDLLNGKKIPKRIDTGSVVITK 274
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
530-641 1.25e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 121.99  E-value: 1.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  530 ADVEKLERIYFNLLSNAFKFTPENGKVTVRLssltKDDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMH---HAGSGI 606
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTL----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRsrkIGGTGL 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2594348833  607 GLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:smart00387  77 GLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
45-296 3.28e-32

ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 127.56  E-value: 3.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  45 EILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAY 124
Cdd:COG4213    22 DNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYDRLILNSDVDYY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 125 IGADNYEIGRAVGNYIASSL--KGKGNVVELTGLGGSTPAMERHQGFMAAISNYPD---IKLI-DKADAAWEREPAEVEM 198
Cdd:COG4213   102 VSFDNVKVGELQGQYLVDGLplKGKGNIELFGGSPTDNNATLFFEGAMSVLQPYIDsgkLVVVsGQWTLGWDPETAQKRM 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 199 DSMLRRHP-KIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDA-LPgkgnGLELVLDNVLDATfIY-PTN--GDKVMQ 273
Cdd:COG4213   182 ENLLTANGnKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVTGQDAeLA----AVQRILAGTQYMT-VYkDTRelAEAAAE 256
                         250       260
                  ....*....|....*....|...
gi 2594348833 274 LAMNILEKKSYPRETVMNTAVVD 296
Cdd:COG4213   257 LAVALAKGEKPEVNGTYDNGKKD 279
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
55-242 1.98e-31

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 124.38  E-value: 1.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAAD--DNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEI 132
Cdd:cd06310    29 GVKIIFVGPESeeDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVIDSGIKGDAYLSYIATDNYAA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 133 GRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAIS-NYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAV 211
Cdd:cd06310   109 GRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKkHPGGIKVLASQYAGSDYAKAANETEDLLGKYPDIDGI 188
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2594348833 212 YAHNDRIAPGAYQAAKKAGREKEMIFVGIDA 242
Cdd:cd06310   189 FATNEITALGAAVAIKSRKLSGQIKIVGFDS 219
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
375-641 5.95e-31

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 125.30  E-value: 5.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 375 QVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQlSHQLeeATHAKLVffTNISHDFRTPLTLV---ADPVEHLLADSSLSE 451
Cdd:COG4191   104 EENAELEELERDITELERAEEELRELQEQLVQ-SEKL--AALGELA--AGIAHEINNPLAAIlgnAELLRRRLEDEPDPE 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 452 DQRRMLLLVQRNVNILLRLVNQILDF-RKyenGKMEYTPISL-----DILSSFEgwnesfmAVARKKHIHFSFDYmPDTD 525
Cdd:COG4191   179 ELREALERILEGAERAAEIVRSLRAFsRR---DEEEREPVDLnelidEALELLR-------PRLKARGIEVELDL-PPDL 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 526 YRTLADVEKLERIYFNLLSNAFKFTPE--NGKVTVRlsslTKDDHCWIRFTVANTGSMISAEHIRNIFDRFY--KIDMHh 601
Cdd:COG4191   248 PPVLGDPGQLEQVLLNLLINAIDAMEEgeGGRITIS----TRREGDYVVISVRDNGPGIPPEVLERIFEPFFttKPVGK- 322
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2594348833 602 aGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:COG4191   323 -GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
70-244 8.62e-31

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 122.74  E-value: 8.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  70 QAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTA------YIGADNYEIGRAVGNYIASS 143
Cdd:cd19970    47 QIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNRLDADALKEgginvpFVGPDNRQGAYLAGDYLAKK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 144 LKGKGNVVELTGLGGSTPAMERHQGFMAAISNYpDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAY 223
Cdd:cd19970   127 LGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEA-GMKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAI 205
                         170       180
                  ....*....|....*....|.
gi 2594348833 224 QAAKKAGREKEMIFVGIDALP 244
Cdd:cd19970   206 KAVDAAGKAGKVLVVGFDNIP 226
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
712-825 1.16e-30

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: 116.60  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 712 LIIDDNADI-RLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTAC 790
Cdd:cd19937     1 LVVDDEEDIvELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2594348833 791 SLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
535-640 2.36e-30

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: 115.67  E-value: 2.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTPEnGKVTVRLSSLTKD-DHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMH----HAGSGIGLA 609
Cdd:cd16922     1 LRQILLNLLGNAIKFTEE-GEVTLRVSLEEEEeDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSttrkYGGTGLGLA 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2594348833 610 LVKAFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:cd16922    80 ISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
711-811 2.57e-30

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: 115.17  E-value: 2.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDqGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKP 811
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
711-822 3.34e-30

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: 115.42  E-value: 3.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd17618     3 ILIVEDEPAIREMIAFNLeRAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLTA 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:cd17618    83 RGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
55-261 9.85e-30

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 119.77  E-value: 9.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGR 134
Cdd:cd06319    29 GYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVIADIGTGGGDYVSYIISDNYDGGY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 AVGNYIASSLKGKG----NVVELTGLGGSTPAMERHQGFMAAI--SNYPDIKLIDKADAAWERepAEVEMDSMLRRHPKI 208
Cdd:cd06319   109 QAGEYLAEALKENGwgggSVGIIAIPQSRVNGQARTAGFEDALeeAGVEEVALRQTPNSTVEE--TYSAAQDLLAANPDI 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 209 DAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPgkgNGLELVLDNVLDAT 261
Cdd:cd06319   187 KGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDP---EALDLIKDGKLDGT 236
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
387-640 1.27e-29

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 121.49  E-value: 1.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 387 RDIleEQRDKLEEQRDQLIQLshqleeATHAKLVffTNISHDFRTPLTLV---ADpvehLLADSSLSEDQRRMLLLVQRN 463
Cdd:COG3852   114 RDI--TERKRLERELRRAEKL------AAVGELA--AGLAHEIRNPLTGIrgaAQ----LLERELPDDELREYTQLIIEE 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 464 VNILLRLVNQILDFRKyeNGKMEYTPISL-DILSSFEgwneSFMAVARKKHIHFSFDYMPDtDYRTLADVEKLERIYFNL 542
Cdd:COG3852   180 ADRLNNLVDRLLSFSR--PRPPEREPVNLhEVLERVL----ELLRAEAPKNIRIVRDYDPS-LPEVLGDPDQLIQVLLNL 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 543 LSNAFKFTPENGKVTVRLSSLTKDDHC------WIRFTVANTGSMISAEHIRNIFDRFY--KIDmhhaGSGIGLALVKAF 614
Cdd:COG3852   253 VRNAAEAMPEGGTITIRTRVERQVTLGglrprlYVRIEVIDNGPGIPEEILDRIFEPFFttKEK----GTGLGLAIVQKI 328
                         250       260
                  ....*....|....*....|....*.
gi 2594348833 615 VELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:COG3852   329 VEQHGGTIEVESEPGKGTTFRIYLPL 354
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
425-641 1.46e-29

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 122.76  E-value: 1.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 425 ISHDFRTPLT---LVADPVEHLLAD--SSLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENGKMEytPISL-DILSSF 498
Cdd:COG5000   208 IAHEIKNPLTpiqLSAERLRRKLADklEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLE--PVDLnELLREV 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 499 EgwnESFMAVARKKHIHFSFDYmPDTDYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLSslTKDDhcWIRFTVANT 578
Cdd:COG5000   286 L---ALYEPALKEKDIRLELDL-DPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTR--REDG--RVRIEVSDN 357
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2594348833 579 GSMISAEHIRNIFDRFY--KidmhHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:COG5000   358 GPGIPEEVLERIFEPFFttK----PKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
55-317 3.47e-29

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 119.25  E-value: 3.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFI--DKGVDLLIISaNEAAPMTPIVEEAYQKGIPVILVDRKILSD----------KYT 122
Cdd:cd06324    30 GIELEVLYANRNRFKMLELAEELLarPPKPDYLILV-NEKGVAPELLELAEQAKIPVFLINNDLTDEerallgkpreKFK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 123 AYIGA---DNYEIGRAVGNYIASSLK-----GKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPA 194
Cdd:cd06324   109 YWLGSivpDNEQAGYLLAKALIKAARkksddGKIRVLAISGDKSTPASILREQGLRDALAEHPDVTLLQIVYANWSEDEA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 195 EVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALPgkgNGLELVLDNVLDATFiyptnGDKVM 272
Cdd:cd06324   189 YQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpgKDVLVGGIDWSP---EALQAVKDGELTASV-----GGHFL 260
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2594348833 273 QLAM------NILEKKSYPRETVMNT---AVVDRTNAHvmQLQTTHISELDQKI 317
Cdd:cd06324   261 EGAWalvllyDYHHGIDFAAGTSVQLkpmLAITRDNVA--QYLKLFGDDNWPKI 312
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
55-242 1.31e-28

D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380646 [Multi-domain]  Cd Length: 284  Bit Score: 116.57  E-value: 1.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGR 134
Cdd:cd19991    29 GAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADVDLYVSFDNEKVGE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 AVGNYIaSSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPD---IKLIDKADA-AWEREPAEVEMDSMLRRH-PKID 209
Cdd:cd19991   109 LQAEAL-VKAKPKGNYVLLGGSPTDNNAKLFREGQMKVLQPLIDsgdIKVVGDQWVdDWDPEEALKIMENALTANnNKID 187
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2594348833 210 AVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDA 242
Cdd:cd19991   188 AVIASNDGTAGGAIQALAEQGLAGKVAVSGQDA 220
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
421-639 2.80e-28

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 119.88  E-value: 2.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 421 FFTNISHDFRTPLT---------LVADPVEHLLAD---SSLSEDQRR------MLLLVQRNVNiLLRLVNQILDFRKyEN 482
Cdd:PRK09835  265 FSADIAHEIRTPITnlitqteiaLSQSRSQKELEDvlySNLEELTRMakmvsdMLFLAQADNN-QLIPEKKMLDLAD-EV 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 483 GKmeytpisldILSSFEGWnesfmavARKKHIHFSFDYMPdtdYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLSs 562
Cdd:PRK09835  343 GK---------VFDFFEAW-------AEERGVELRFVGDP---CQVAGDPLMLRRAISNLLSNALRYTPAGEAITVRCQ- 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 563 lTKDDHCwiRFTVANTGSMISAEHIRNIFDRFYKID----MHHAGSGIGLALVKAFVELHKGTITVESDEKqGTIFTVDL 638
Cdd:PRK09835  403 -EVDHQV--QLVVENPGTPIAPEHLPRLFDRFYRVDpsrqRKGEGSGIGLAIVKSIVVAHKGTVAVTSDAR-GTRFVISL 478

                  .
gi 2594348833 639 P 639
Cdd:PRK09835  479 P 479
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
711-822 4.25e-28

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: 109.55  E-value: 4.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALTA 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2594348833 790 CSL--DEQRIqgYDGGADSYISKPFSSQLLLARVR 822
Cdd:cd17548    82 YAMkgDREKI--LEAGCDGYISKPIDTREFLETVA 114
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
530-642 4.52e-28

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: 108.99  E-value: 4.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 530 ADVEKLERIYFNLLSNAFKFTPENGKVTVRLssltkDDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMH-HAGSGIGL 608
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITVTL-----SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRgGGGTGLGL 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2594348833 609 ALVKAFVELHKGTITVESDEKQGTIFTVDLPVQT 642
Cdd:pfam02518  76 SIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
712-811 5.50e-28

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 108.47  E-value: 5.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 712 LIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLTAC 790
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEReGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE--LPPDIPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 2594348833 791 SLDEQRIQGYDGGADSYISKP 811
Cdd:cd00156    79 ADEEDAVRALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
711-822 5.91e-28

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 108.78  E-value: 5.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqTCHIPVILLTA 789
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRR--DPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
413-811 6.27e-28

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 121.49  E-value: 6.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 413 EATHAKLVFFTNISHDFRTPLTLVADPVEHLLaDSSLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENGKM--EYTPI 490
Cdd:PRK11107  288 EAARIKSEFLANMSHELRTPLNGVIGFTRQTL-KTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLvlENIPF 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 491 SL-DILssfegwNESFMAV---ARKKHIHFSFDYMPDTDYRTLADVEKLERIYFNLLSNAFKFTpENGKVTVRLSSLT-K 565
Cdd:PRK11107  367 SLrETL------DEVVTLLahsAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFT-ESGNIDILVELRAlS 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 566 DDHCWIRFTVANTGSMISAEHIRNIFDRFYK----IDMHHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:PRK11107  440 NTKVQLEVQIRDTGIGISERQQSQLFQAFRQadasISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLD 519
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 642 TCETVVSENSP---------------AFSVSAT----SVTSTDATTS-------------AVAGVPATPATSGYSGSSSL 689
Cdd:PRK11107  520 LNPNPIIDGLPtdclagkrllyvepnSAAAQATldilSETPLEVTYSptlsqlpeahydiLLLGLPVTFREPLTMLHERL 599
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 690 NDALT---------------YEEEELEKSYDS--SKP--------------------------------CVLIIDDN-AD 719
Cdd:PRK11107  600 AKAKSmtdflilalpcheqvLAEQLKQDGADAclSKPlshtrllpallepchhkqppllpptdesrlplTVMAVDDNpAN 679
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 720 IRLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTACSLDEQRIQG 799
Cdd:PRK11107  680 LKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERL 759
                         490
                  ....*....|..
gi 2594348833 800 YDGGADSYISKP 811
Cdd:PRK11107  760 LSAGMDDYLAKP 771
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
531-639 6.81e-28

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: 108.73  E-value: 6.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 531 DVEKLERIYFNLLSNAFKFTPENGKVTVRLSsLTKDDHCWIrfTVANTGSMISAEHIRNIFDRFYKID----MHHAGSGI 606
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILE-KFRLNRFLL--TVSDSGPGIPPNLREEIFERFRQGDgsstRAHGGTGL 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 607 GLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16925    78 GLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
711-830 8.79e-28

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: 108.62  E-value: 8.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVH-GLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTA 789
Cdd:cd17627     1 ILVVDDDRAVRESLRrSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGND--LPILVLTA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshRR 830
Cdd:cd17627    79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL---RR 116
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
27-244 9.61e-28

similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380528 [Multi-domain]  Cd Length: 273  Bit Score: 113.54  E-value: 9.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVA-QCSDDSWRHKMNDEILREAMFYdGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQK 105
Cdd:cd06305     1 TIAVVrNGTSGDWDQQALQGAVAEAEKL-GGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 106 GIPVILVDRKILSDKYTaYIGADNYEIGRAVGNYIASSLKGKGNVVELTGlGGSTPAMERHQGFMAAISNYPDIKLI--- 182
Cdd:cd06305    80 GIPVVTFDTDSQVPGVN-NITQDDYALGTLSLGQLVKDLNGEGNIAVFNV-FGVPPLDKRYDIYKAVLKANPGIKKIvae 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833 183 --DKADAAWEREPAEVEmdSMLRRHPK--IDAVYAHNDRIAPGAYQAAKKAGREKEMIFvGIDALP 244
Cdd:cd06305   158 lgDVTPNTAADAQTQVE--ALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTDIKVY-GVDISN 220
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
28-242 1.23e-27

periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380480 [Multi-domain]  Cd Length: 283  Bit Score: 113.67  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  28 IGVAQCSDDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGI 107
Cdd:cd01538     2 IGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 108 PVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSlKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPD---IKLIDK 184
Cdd:cd01538    82 KVIAYDRLILNADVDYYISFDNEKVGELQAQALLDA-KPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAIDsgkIKVVGD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 185 ADA-AWEREPAEVEMDSMLRRH-PKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDA 242
Cdd:cd01538   161 QWVdDWLPANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKAQGLSGGVPVSGQDA 220
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
710-824 2.43e-27

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: 107.25  E-value: 2.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 710 CVLIIDDNADIRLYVHGLLHTD--YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILL 787
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLagWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILL 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNL 824
Cdd:cd17552    83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKL 119
pleD PRK09581
response regulator PleD; Reviewed
711-832 2.65e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 116.54  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDD-NADIRLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:PRK09581    5 ILVVDDiPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshrRLK 832
Cdd:PRK09581   85 LDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLT----RLK 123
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
49-295 4.38e-27

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 111.94  E-value: 4.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  49 EAMFYDGVSVEIRSAAD--DNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYqKGIPVILVDRKILSDKYTAYIG 126
Cdd:cd20008    23 KAAKELGVEVTFLGPATeaDIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD-AGIPVVLVDSGANTDDYDAFLA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 127 ADNYEIGRAVGNYIASSLK----GKGNVVELTGLGGSTPAMERHQGFMAAIS-NYPDIKLIDKADAAWEREPAEVEMDSM 201
Cdd:cd20008   102 TDNVAAGALAADELAELLKasggGKGKVAIISFQAGSQTLVDREEGFRDYIKeKYPDIEIVDVQYSDGDIAKALNQTTDL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 202 LRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGKGNGLElvlDNVLDATFIY-PTN-GDKVMQLAMNIL 279
Cdd:cd20008   182 LTANPDLVGIFGANNPSAVGVAQALAEAGKAGKIVLVGFDSSPDEVALLK---SGVIKALVVQdPYQmGYEGVKTAVKAL 258
                         250
                  ....*....|....*.
gi 2594348833 280 EKKSYPrETVMNTAVV 295
Cdd:cd20008   259 KGEEIV-EKNVDTGVT 273
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
711-825 9.05e-27

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: 105.87  E-value: 9.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd17598    81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
707-833 1.70e-26

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: 113.52  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 707 SKPCVLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVI 785
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERaGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2594348833 786 LLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQ 833
Cdd:COG2204    79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRE 126
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
54-299 1.87e-26

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 110.16  E-value: 1.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  54 DGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIG 133
Cdd:cd06317    28 LGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVIPSDFQAAQVGVDNLEGG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 134 RAVGN----YIASSLKGKGNvVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKID 209
Cdd:cd06317   108 KEIGKyaadYIKAELGGQAK-IGVVGALSSLIQNQRQKGFEEALKANPGVEIVATVDGQNVQEKALSAAENLLTANPDLD 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 210 AVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGKgnGLELVLDNVLDATF-IYP-TNGDKVMQLAMNILEKKSYPRE 287
Cdd:cd06317   187 AIYATGEPALLGAVAAVRSQGRQGKIKVFGWDLTKQA--IFLGIDEGVLQAVVqQDPeKMGYEAVKAAVKAIKGEDVEKT 264
                         250
                  ....*....|..
gi 2594348833 288 TVMNTAVVDRTN 299
Cdd:cd06317   265 IDVPPTIVTKEN 276
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
394-813 2.56e-26

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 116.23  E-value: 2.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 394 RDKLEEQrdqLIQLSHQLEEATHAKLVFFTNISHDFRTPLTLVADPVEhLLADSSLSEDQRRMLLLVQRNVNILLRLVNQ 473
Cdd:PRK10841  426 RVKMEES---LQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLD-LLQTKELPKGVDRLVTAMNNSSSLLLKIISD 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 474 ILDFRKYENGKM-----EYTP---ISlDILSSFegwnesFMAVARKKHIHFSFdYMPDTDYRTLADVEKLERIYFNLLSN 545
Cdd:PRK10841  502 ILDFSKIESEQLkieprEFSPrevIN-HITANY------LPLVVKKRLGLYCF-IEPDVPVALNGDPMRLQQVISNLLSN 573
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 546 AFKFTpENGKVTVRLSSltkdDHCWIRFTVANTGSMISAEHIRNIFDRFYKI----DMHHAGSGIGLALVKAFVELHKGT 621
Cdd:PRK10841  574 AIKFT-DTGCIVLHVRV----DGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVgtgvQRNFQGTGLGLAICEKLINMMDGD 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 622 ITVESDEKQGTIFTVDLPV----------------QTC-------------ETVVSENS------PAFSVSATSVTSTD- 665
Cdd:PRK10841  649 ISVDSEPGMGSQFTIRIPLygaqypqkkgveglqgKRCwlavrnasleqflETLLQRSGiqvqryEGQEPTPEDVLITDd 728
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 666 --ATTSAVAGV---------PATPATSGY--SGSSSLNDALT-----YE-EEELEKSYDSSKPCVLIIDDNADIRLYV-- 724
Cdd:PRK10841  729 pvQKKWQGRAVitfcrrhigIPLEIAPGEwvHSTATPHELPAllariYRiELESDDSANALPSTDKAVSDNDDMMILVvd 808
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 725 -HGL---LHTD------YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLTACSLDE 794
Cdd:PRK10841  809 dHPInrrLLADqlgslgYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQ--LGLTLPVIGVTANALAE 886
                         490
                  ....*....|....*....
gi 2594348833 795 QRIQGYDGGADSYISKPFS 813
Cdd:PRK10841  887 EKQRCLEAGMDSCLSKPVT 905
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
37-299 3.50e-26

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380652 [Multi-domain]  Cd Length: 305  Bit Score: 110.07  E-value: 3.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  37 SWRHKMND--EILREAMFYDGVSVE--IRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILV 112
Cdd:cd19997    12 TWRQQMVDafEEAAKKAKADGLIADyiVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 113 DRKILSDKytAYIGADNYE-IGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWER 191
Cdd:cd19997    92 DSGVTEPC--AYILNNDFEdYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKYPDLKVVAEVYGNWTQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 192 EPAEVEMDSMLRRHPKIDAVYAHNDRiAPGAYQAAKKAGREKEMIFVGID-------ALPGKGNGLELVldnvldATFIY 264
Cdd:cd19997   170 SVAQKAVTGILPSLPEVDAVITQGGD-GYGAAQAFEAAGRPLPIIIGGNRgeflkwwQEEYAKNGYETV------SVSTD 242
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2594348833 265 PTNGDKVMQLAMNILEKKSYPRETVMNTAVVDRTN 299
Cdd:cd19997   243 PGQGSAAFWVALDILNGKDVPKEMILPVVTITEDD 277
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
712-830 1.30e-25

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: 102.30  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 712 LIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRL-KSELQTchiPVILLTA 789
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLrEEGIET---PVLLLTA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshRR 830
Cdd:cd17625    78 LDAVEDRVKGLDLGADDYLPKPFSLAELLARIRALL---RR 115
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
425-649 1.47e-25

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: 111.60  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 425 ISHDFRTPLTLVADPVEhLLADSsLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENGKMEYTPISlDILSSFEgwnES 504
Cdd:COG5809   277 IAHEIRNPLTSLKGFIQ-LLKDT-IDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYEPKDLN-TLIEEVI---PL 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 505 FMAVARKKHIHFSFDYMPDTDYrTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLsslTKDDHCWIRFTVANTGSMISA 584
Cdd:COG5809   351 LQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMPEGGNITIET---KAEDDDKVVISVTDEGCGIPE 426
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2594348833 585 EHIRNIFDRFY--KidmhHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQTCETVVSE 649
Cdd:COG5809   427 ERLKKLGEPFYttK----EKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSMN 489
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
78-296 2.19e-25

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 106.55  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  78 IDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDrKILSDKY--TAYIGADNYEIGRAVGNYIASSLKGKGNVVELTG 155
Cdd:cd20007    53 IAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVD-TTLGDPSfvLSQIASDNVAGGALAAEALAELIGGKGKVLVINS 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 156 LGGSTPAMERHQGFMAAISNYPDIKLI----DKADAAwerePAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGR 231
Cdd:cd20007   132 TPGVSTTDARVKGFAEEMKKYPGIKVLgvqySENDPA----KAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGK 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2594348833 232 EKEMIFVGIDALPGKGNGLElvlDNVLDATFIY-P-TNGDKVMQLAMNILEKKSYPRETVMNTAVVD 296
Cdd:cd20007   208 TGKVKVVGFDASPAQVEQLK---AGTIDALIAQkPaEIGYLAVEQAVAALTGKPVPKDILTPFVVIT 271
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
711-822 2.95e-25

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: 101.43  E-value: 2.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELqtCHIPVILL 787
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLesEPDIEVVgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRY--PDLKVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:cd17535    79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIR 113
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
870-954 3.45e-25

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 106.02  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 870 LNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPT 949
Cdd:COG2207   169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                  ....*
gi 2594348833 950 DLLKR 954
Cdd:COG2207   249 EYRKR 253
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
711-830 1.07e-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: 99.73  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqTCHIPVILLTA 789
Cdd:cd17615     2 VLVVDDEPNITeLLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLTA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshRR 830
Cdd:cd17615    80 KDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL---RR 117
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
41-261 1.27e-24

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380628 [Multi-domain]  Cd Length: 285  Bit Score: 104.86  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  41 KMNDEILREAmfyDGVSVEIRSAA----DDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKI 116
Cdd:cd19973    16 KMKEGAQKAA---KALGIKLMTAAgkidGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDTPT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 117 -LSDKYTAYIGADNYEIGRAVGNYIASSLKGK-GNVVELTGLGGSTPAMERHQGFMA----------AISNYPDIKLIDK 184
Cdd:cd19973    93 dPIDAADATFATDNFKAGVLIGEWAKAALGAKdAKIATLDLTPGHTVGVLRHQGFLKgfgidekdpeSNEDEDDSQVVGS 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2594348833 185 ADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDalpGKGNGLELVLDNVLDAT 261
Cdd:cd19973   173 ADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEKGVLIVSVD---GGCPGVKDVKDGIIGAT 246
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
56-304 2.64e-24

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 104.29  E-value: 2.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  56 VSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKytAY-IGADNYEIGR 134
Cdd:cd19998    34 VELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVDEPC--AYnVNTDQAKAGE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 AVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYA- 213
Cdd:cd19998   112 QTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEVFKKYPDIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVWTq 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 214 HNDRiapGAYQAAKKAGRekEMIFVGIDAlpgkGNGLELVLDNVLdatfiypTNGDKV-------------MQLAMNILE 280
Cdd:cd19998   192 GGET---GVIKALQAAGH--PLVPVGGEA----ENGFRKAMLEPL-------ANGLPGisagsppalsavaLKLAVAVLE 255
                         250       260
                  ....*....|....*....|....
gi 2594348833 281 KKSYPRETVMNTAVVDRTNAHVMQ 304
Cdd:cd19998   256 GEKEPKTIELPLPWVTTDDVKLCQ 279
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
387-640 3.38e-24

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 108.52  E-value: 3.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 387 RDILEeqRDKLEEQRDQLIQLshqleeATHAKLVffTNISHDFRTPLTLVADPVEHLLADSSLSEDQRrMLLLVQRNVNI 466
Cdd:PRK11360  369 SDLTE--RKRLQRRVARQERL------AALGELV--AGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQE-YLSVVLREVDR 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 467 LLRLVNQILDFRKyeNGKMEYTPISLDIL---SSFegwnesFMAVARKK-HIHFSFDYMPDTDyRTLADVEKLERIYFNL 542
Cdd:PRK11360  438 LNKVIDQLLEFSR--PRESQWQPVSLNALveeVLQ------LFQTAGVQaRVDFETELDNELP-PIWADPELLKQVLLNI 508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 543 LSNAFKFTPENGKVTVRlSSLTKDDHCWIrfTVANTGSMISAEHIRNIFDRFYKidMHHAGSGIGLALVKAFVELHKGTI 622
Cdd:PRK11360  509 LINAVQAISARGKIRIR-TWQYSDGQVAV--SIEDNGCGIDPELLKKIFDPFFT--TKAKGTGLGLALSQRIINAHGGDI 583
                         250
                  ....*....|....*...
gi 2594348833 623 TVESDEKQGTIFTVDLPV 640
Cdd:PRK11360  584 EVESEPGVGTTFTLYLPI 601
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
869-952 5.73e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 96.47  E-value: 5.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  869 NLNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESP 948
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 2594348833  949 TDLL 952
Cdd:smart00342  81 SEYR 84
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
711-825 6.08e-24

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 97.76  E-value: 6.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLH-TDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd17562     3 ILAVDDSASIRQMVSFTLRgAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLTT 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd17562    83 ESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
367-639 9.27e-24

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: 105.55  E-value: 9.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 367 KELSEQKKQVEQQRdklEEQRdiLEEQRdKLEEQRDQLIQLSH---QLEEATHAKLVFFTNISHDFRTPLTLVADPVEHL 443
Cdd:TIGR01386 193 RRLSAVAARISPES---LDQR--LDPSR-APAELRELAQSFNAmlgRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVA 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 444 LADSSLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYMPd 523
Cdd:TIGR01386 267 LSQPRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEG- 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 524 tdyRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLssLTKDDHCWIRftVANTGSMISAEHIRNIFDRFYKIDM---- 599
Cdd:TIGR01386 346 ---LVRGDPQMFRRAISNLLSNALRHTPDGGTITVRI--ERRSDEVRVS--VSNPGPGIPPEHLSRLFDRFYRVDParsn 418
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2594348833 600 HHAGSGIGLALVKAFVELHKGTITVESDEkQGTIFTVDLP 639
Cdd:TIGR01386 419 SGEGTGLGLAIVRSIMEAHGGRASAESPD-GKTRFILRFP 457
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
65-261 9.86e-24

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 102.48  E-value: 9.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  65 DDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSL 144
Cdd:PRK10653   66 NNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 145 KGKGNVVELTGLGGSTPAMERHQGFMAAISNYpDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQ 224
Cdd:PRK10653  146 GEGAKVIQLEGIAGTSAARERGEGFKQAVAAH-KFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALR 224
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2594348833 225 AAKKAGREKEMIfVGIDalpGKGNGLELVLDNVLDAT 261
Cdd:PRK10653  225 ALQTAGKSDVMV-VGFD---GTPDGIKAVNRGKLAAT 257
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
711-819 1.08e-23

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 96.77  E-value: 1.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRL-KSELQTCHIPVILLT 788
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLeKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIrELEGGGRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLLLA 819
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKE 111
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
44-289 1.42e-23

periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 102.28  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  44 DEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISA-NEAAPMTpIVEEAYQKGIPVILVDRKILSD--- 119
Cdd:cd01539    20 KALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLvDRTAAQT-IIDKAKAANIPVIFFNREPSREdlk 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 120 KY--TAYIGADNYEIGRAVGNYIASSLK----------GKGNVVELTGLGGSTPAMERHQGFMAAI--SNYPdIKLIDKA 185
Cdd:cd01539    99 SYdkAYYVGTDAEESGIMQGEIIADYWKanpeidkngdGKIQYVMLKGEPGHQDAIARTKYSVKTLndAGIK-TEQLAED 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 186 DAAWEREPAEVEMDSMLRRHP-KIDAVYAHNDRIAPGAYQAAKKAGR-----EKEMIFVGIDALPGkgnGLELVLDNVLD 259
Cdd:cd01539   178 TANWDRAQAKDKMDAWLSKYGdKIELVIANNDDMALGAIEALKAAGYntgdgDKYIPVFGVDATPE---ALEAIKEGKML 254
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2594348833 260 ATFI--YPTNGDKVMQLAMNILEKKSYPRETV 289
Cdd:cd01539   255 GTVLndAKAQAKAIYELAKNLANGKEPLETGY 286
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
55-296 1.89e-23

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380650 [Multi-domain]  Cd Length: 294  Bit Score: 101.60  E-value: 1.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGR 134
Cdd:cd19995    32 DCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNVAVGE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 AVGNYIASSLKGKG----NVVELTGLGGSTPAMERHQGFMAAIS---NYPDIKLIDKADAA-WEREPAEVEMDSMLRRHP 206
Cdd:cd19995   112 AQAQSLVDHLKAIGkkgvNIVMINGSPTDNNAGLFKKGAHEVLDplgDSGELKLVCEYDTPdWDPANAQTAMEQALTKLG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 207 -KIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGkgnGLELVLDNVLDATFI--YPTNGDKVMQLAMNILEKKS 283
Cdd:cd19995   192 nNIDGVLSANDGLAGGAIAALKAQGLAGKVPVTGQDATVA---GLQRILAGDQYMTVYkpIKKEAAAAAKVAVALLKGET 268
                         250
                  ....*....|...
gi 2594348833 284 YPREtvMNTAVVD 296
Cdd:cd19995   269 PPSD--LVTGTVT 279
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
409-639 2.05e-23

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 104.32  E-value: 2.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 409 HQLEeatHAKLVFFTNISHDFRTPLTLVADPVEhLLADSSLSEDQR-RMLLLVQRNVNILLRLVNQILDFRKYENGKMEY 487
Cdd:PRK11006  198 HQLE---GARRNFFANVSHELRTPLTVLQGYLE-MMQDQPLEGALReKALHTMREQTQRMEGLVKQLLTLSKIEAAPTID 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 488 TPISLDILSSFEGWNESFMAVARKKHiHFSFDYmpDTDYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVrlssltkdd 567
Cdd:PRK11006  274 LNEKVDVPMMLRVLEREAQTLSQGKH-TITFEV--DNSLKVFGNEDQLRSAISNLVYNAVNHTPEGTHITV--------- 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 568 hCWIR------FTVANTGSMISAEHIRNIFDRFYKIDM----HHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVD 637
Cdd:PRK11006  342 -RWQRvpqgaeFSVEDNGPGIAPEHIPRLTERFYRVDKarsrQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFV 420

                  ..
gi 2594348833 638 LP 639
Cdd:PRK11006  421 LP 422
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
711-811 2.40e-23

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 95.20  E-value: 2.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVH-GLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTA 789
Cdd:cd19935     1 ILVVEDEKKLAEYLKkGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQ--TPVLMLTA 78
                          90       100
                  ....*....|....*....|..
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKP 811
Cdd:cd19935    79 RDSVEDRVKGLDLGADDYLVKP 100
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
711-811 3.12e-23

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: 94.84  E-value: 3.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQtcHIPVILL 787
Cdd:COG4753     2 VLIVDDEPLIREGLKRILewEAGFEVVgEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDP--DTKIIIL 79
                          90       100
                  ....*....|....*....|....
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKP 811
Cdd:COG4753    80 SGYSDFEYAQEAIKLGADDYLLKP 103
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
45-241 3.20e-23

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 101.81  E-value: 3.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  45 EILREAmfydGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPmtPIVEEAYQKGIPVILVDRKILSDKYtAY 124
Cdd:COG1609    85 EAARER----GYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDD--ARLERLAEAGIPVVLIDRPLPDPGV-PS 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 125 IGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISNY---PDIKLIdkADAAWEREPAEVEMDSM 201
Cdd:COG1609   158 VGVDNRAGARLATEHLIE--LGHRRIAFIGGPADSSSARERLAGYREALAEAglpPDPELV--VEGDFSAESGYEAARRL 233
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2594348833 202 LRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGID 241
Cdd:COG1609   234 LARGPRPTAIFCANDLMALGALRALREAGLRvpEDVSVVGFD 275
orf27 CHL00148
Ycf27; Reviewed
706-825 9.95e-23

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 98.25  E-value: 9.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 706 SSKPCVLIIDDNADIRLYVHGLLH-TDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqtCHIPV 784
Cdd:CHL00148    4 NSKEKILVVDDEAYIRKILETRLSiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE---SDVPI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2594348833 785 ILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:CHL00148   81 IMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
711-822 2.24e-22

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 93.14  E-value: 2.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQtchIPVILLTA 789
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEgFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQ---VPVLMLTA 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:cd17623    78 RGDDIDRILGLELGADDYLPKPFNPRELVARIR 110
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
55-295 2.30e-22

TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.


Pssm-ID: 380529 [Multi-domain]  Cd Length: 269  Bit Score: 98.04  E-value: 2.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSA-ADDN----RKQAEDvhyFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADN 129
Cdd:cd06306    29 GVKLTVYEAgGYTNlskqISQLED---CVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAARVLVDF 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 130 YEIGRAVGNYIASSLKGK-GNVVELTGLGGSTPAMERHQGFMAAISNyPDIKLIDKADAAWEREPAEVEMDSMLRRHPKI 208
Cdd:cd06306   106 YDMGYLAGEYLVEHHPGKpVKVAWFPGPAGAGWAEDREKGFKEALAG-SNVEIVATKYGDTGKAVQLNLVEDALQAHPDI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 209 DaVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPGkgnglelVLDNVLDATfIYPTNGDK-VMQ------LAMNILEK 281
Cdd:cd06306   185 D-YIVGNAVAAEAAVGALREAGLTGKVKVVSTYLTPG-------VYRGIKRGK-ILAAPSDQpVLQgriavdQAVRALEG 255
                         250
                  ....*....|....
gi 2594348833 282 KSYPRETVMNTAVV 295
Cdd:cd06306   256 KPVPKHVGPPILVV 269
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
2-244 2.45e-22

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 98.79  E-value: 2.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833   2 KYTKWITVLFCLLGLAACRQDAPRFRIGVAQCSDDSWRhKMNDEILREAMfYDGVSVEI--RSAADDNRKQAEDVHYFID 79
Cdd:PRK09701    3 KYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWV-DMKKGIEDEAK-TLGVSVDIfaSPSEGDFQSQLQLFEDLSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  80 KGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYT-------AYIGADNYEIGRAVGNYIASSLKGK-GNVV 151
Cdd:PRK09701   81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKkaggnveAFVTTDNVAVGAKGASFIIDKLGAEgGEVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 152 ELTGLGGSTPAMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGR 231
Cdd:PRK09701  161 IIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK 240
                         250
                  ....*....|...
gi 2594348833 232 EKEMIFVGIDALP 244
Cdd:PRK09701  241 TGKVLVVGTDGIP 253
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
711-825 4.04e-22

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: 92.16  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADI-RLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTA 789
Cdd:cd17624     1 ILLVEDDALLgDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQS--LPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd17624    79 RDGVDDRVAGLDAGADDYLVKPFALEELLARLRALL 114
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
504-639 5.23e-22

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 99.54  E-value: 5.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 504 SFMAVARKKHIHFSFDYMPDTDYRTLADVEkLERIYFNLLSNAF----KFTPENGKVTVRLSsltkDDHCWIRFTVANTG 579
Cdd:COG3290   252 GKAARARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIeaveKLPEEERRVELSIR----DDGDELVIEVEDSG 326
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 580 SMISAEHIRNIFDRFY--KIDMHHagsGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:COG3290   327 PGIPEELLEKIFERGFstKLGEGR---GLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLP 385
HTH_18 pfam12833
Helix-turn-helix domain;
875-954 5.52e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 90.73  E-value: 5.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 875 LGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLA-SSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPTDLLK 953
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80

                  .
gi 2594348833 954 R 954
Cdd:pfam12833  81 R 81
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
711-830 6.38e-22

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: 91.96  E-value: 6.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADI--RLYVHgLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLT 788
Cdd:cd19934     1 LLLVEDDALLaaQLKEQ-LSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--TPVLILT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshRR 830
Cdd:cd19934    78 ARDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALI---RR 116
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
37-242 7.28e-22

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380648 [Multi-domain]  Cd Length: 287  Bit Score: 96.78  E-value: 7.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  37 SW------RHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVI 110
Cdd:cd19993     5 SWsnfqeeRWKTDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 111 LVDRKIlSDKYTAYIGADNYEIGR--AVGNYIAsslKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPD---IKLI-DK 184
Cdd:cd19993    85 AYDRLI-ENPIAFYISFDNVEVGRmqARGVLKA---KPEGNYVFIKGSPTDPNADFLRAGQMEVLQPAIDsgkIKIVgEQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 185 ADAAWEREPAEVEMDSML-RRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDA 242
Cdd:cd19993   161 YTDGWKPANAQKNMEQILtANNNKVDAVVASNDGTAGGAVAALAAQGLAGKVPVSGQDA 219
PRK11517 PRK11517
DNA-binding response regulator HprR;
711-828 7.40e-22

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 95.35  E-value: 7.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYV-HGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchiPVILLTA 789
Cdd:PRK11517    3 ILLIEDNQRTQEWVtQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT---PVICLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSH 828
Cdd:PRK11517   80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQH 118
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
45-244 9.08e-22

ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 96.05  E-value: 9.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  45 EILREAmfydGVSVEIRSAADDNRKQAEDVHYFIDKGVD-LLIISANEAapmTPIVEEAYQKGIPVILVDRKILSDKYTa 123
Cdd:cd06267    23 DAARER----GYSLLLCNTDEDPEREREYLRLLLSRRVDgIILAPSSLD---DELLEELLAAGIPVVLIDRRLDGLGVD- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 124 YIGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISNY---PDIKLIdkADAAWEREPAEVEMDS 200
Cdd:cd06267    95 SVVVDNYAGAYLATEHLIE--LGHRRIAFIGGPLDLSTSRERLEGYRDALAEAglpVDPELV--VEGDFSEESGYEAARE 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 201 MLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd06267   171 LLALPPRPTAIFAANDLMAIGALRALRELGLRvpEDISVVGFDDIP 216
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
27-242 9.77e-22

periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380649 [Multi-domain]  Cd Length: 304  Bit Score: 96.93  E-value: 9.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCSDDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKG 106
Cdd:cd19994     1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 107 IPVILVDRKIL-SDKYTAYIGADNYEIGRAVGNYIASSLK----GKGNVVELtgLGGS----------TPAMERHQGFMA 171
Cdd:cd19994    81 IPVIAYDRLIMnTDAVDYYVTFDNEKVGELQGQYLVDKLGlkdgKGPFNIEL--FAGSpddnnaqlffKGAMEVLQPYID 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 172 A---ISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHP----KIDAVYAHNDRIAPGAYQAAKKAGR-EKEMIFV-GIDA 242
Cdd:cd19994   159 DgtlVVRSGQTTFEQVATPDWDTETAQARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAGYdTGPWPVVtGQDA 238
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
711-824 3.02e-21

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: 89.81  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDN-ADIRLYVHGLLHTDYTVIEA-ADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLT 788
Cdd:cd17551     3 ILIVDDNpTNLLLLEALLRSAGYLEVVSfTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMIT 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNL 824
Cdd:cd17551    83 ADTDREVRLRALEAGATDFLTKPFDPVELLARVRNL 118
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
707-833 3.52e-21

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 90.41  E-value: 3.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 707 SKPCVLIIDDNADIRLYVHGLLHTDY---TVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIP 783
Cdd:COG4565     2 KMIRVLIVEDDPMVAELLRRYLERLPgfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDVD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2594348833 784 VILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQ 833
Cdd:COG4565    80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
711-825 4.07e-21

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 89.47  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTA 789
Cdd:COG5803     5 ILIVDDQAGIRMLLKEVLKKEgYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPD--IPVIMMTA 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:COG5803    83 YGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-639 4.32e-21

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: 88.98  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTPENgkVTVRLSSLTKDDHcwIRFTVANTGSMISAEHIRNIFDRFYKIDM--HHAGSGIGLALVK 612
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPEN--TRIYITSFLTDDV--VNIMFKNPSSHPLDFKLEKLFERFYRGDNsrNTEGAGLGLSIAK 76
                          90       100
                  ....*....|....*....|....*..
gi 2594348833 613 AFVELHKGTITVESDEKqGTIFTVDLP 639
Cdd:cd16923    77 AIIELHGGSASAEYDDN-HDLFKVRLP 102
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
711-811 4.44e-21

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: 88.76  E-value: 4.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQtchIPVILLTA 789
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAhGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA---VPVIVLSA 77
                          90       100
                  ....*....|....*....|..
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKP 811
Cdd:cd17620    78 RDEESDKIAALDAGADDYLTKP 99
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
54-242 7.14e-21

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 93.46  E-value: 7.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  54 DGVSVEIRSAADDN--RKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYE 131
Cdd:cd20005    28 LGVKITFEGPDTESdvDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSDLPLATVATDNYA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 132 IGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAI-SNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDA 210
Cdd:cd20005   108 AGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIkEKYPDIKVVNVQYGVGDHAKAADIAKAILQANPDLKG 187
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2594348833 211 VYAHNDRIAPGAYQAAKKAGREKEMIFVGIDA 242
Cdd:cd20005   188 IYATNEGAAIGVANALKEMGKLGKIKVVGFDS 219
ompR PRK09468
osmolarity response regulator; Provisional
711-822 9.11e-21

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 92.34  E-value: 9.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLTA 789
Cdd:PRK09468    8 ILVVDDDMRLRaLLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRS--QNNPTPIIMLTA 85
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:PRK09468   86 KGEEVDRIVGLEIGADDYLPKPFNPRELLARIR 118
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
711-825 1.37e-20

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: 87.81  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADI-RLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELqtcHIPVILLTA 789
Cdd:cd19939     2 ILIVEDELELaRLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS---HVPILMLTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd19939    79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
711-825 1.41e-20

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: 87.86  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIPVILLTA 789
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEgYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR---KTSNVPIIMLTA 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd17614    78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
PRK09303 PRK09303
histidine kinase;
368-640 1.89e-20

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 94.63  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 368 ELSEQKKQVEQQRDKLEEQRdiLEEQRDKLEEQRDQLIQlshQLE--EATHAKLVfftnisHDFRTPLTLVADPVEHLLA 445
Cdd:PRK09303  110 GENLQPSEIDSGRYSQELLQ--LSDELFVLRQENETLLE---QLKfkDRVLAMLA------HDLRTPLTAASLALETLEL 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 446 DSSLSEDQRRMLLLVQ------RNVNILLRLVNQILDFRKYENG-------KMEYTPISLDILSSFEgwnESFmavaRKK 512
Cdd:PRK09303  179 GQIDEDTELKPALIEQlqdqarRQLEEIERLITDLLEVGRTRWEalrfnpqKLDLGSLCQEVILELE---KRW----LAK 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 513 HIHFSFDYMPD--TDYrtlADVEKLERIYFNLLSNAFKFTPENGkvTVRLSSLTKDDHcWIRFTVANTGSMISAEHIRNI 590
Cdd:PRK09303  252 SLEIQTDIPSDlpSVY---ADQERIRQVLLNLLDNAIKYTPEGG--TITLSMLHRTTQ-KVQVSICDTGPGIPEEEQERI 325
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 591 F-DRF-YKIDMHHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:PRK09303  326 FeDRVrLPRDEGTEGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLPV 377
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
711-825 2.32e-20

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: 87.43  E-value: 2.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADI-RLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIPVILLTA 789
Cdd:cd19938     2 ILIVEDEPKLaQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR---RFSDVPIIMVTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd19938    79 RVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
711-826 3.16e-20

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: 87.47  E-value: 3.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDN-ADIRLYVHGL--LHTDYTVIEAADGSEGI---RKAMKYV----PDLIISDVMMPGMDGIECCRRLKSELQTC 780
Cdd:cd17557     2 ILLVEDNpGDAELIQEAFkeAGVPNELHVVRDGEEALdflRGEGEYAdaprPDLILLDLNMPRMDGFEVLREIKADPDLR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 781 HIPVILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLID 826
Cdd:cd17557    82 RIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGE 127
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
711-822 3.98e-20

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: 86.75  E-value: 3.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqtCHIPVILLTA 789
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE---SGVPIVMLTA 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:cd17626    80 KSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
711-826 7.52e-20

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 85.85  E-value: 7.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRlyvHGLLHT------DYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQtcHIP 783
Cdd:cd17536     1 VLIVDDEPLIR---EGLKKLidweelGFEVVgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYP--DIK 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 784 VILLTacsldeqriqGYD----------GGADSYISKPFSSQLLLARVRNLID 826
Cdd:cd17536    76 IIILS----------GYDdfeyaqkairLGVVDYLLKPVDEEELEEALEKAKE 118
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
54-245 1.38e-19

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 89.98  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  54 DGVSVEIRSAADDNR-KQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDK----YTAYIGAD 128
Cdd:cd06312    29 LGVTVQYLGPQNNDIaDQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINSGDDRSKerlgALTYVGQD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 129 NYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAI--SNYPDIKLIDKADaawerePAEVE--MDSMLRR 204
Cdd:cd06312   109 EYLAGQAAGERALE--AGPKNALCVNHEPGNPGLEARCKGFADAFkgAGILVELLDVGGD------PTEAQeaIKAYLQA 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2594348833 205 HPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALPG 245
Cdd:cd06312   181 DPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTFDLSPE 221
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
78-279 1.83e-19

monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 89.25  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  78 IDKGVDLLIISANEAAPMTPIVEEAYQKGIPVIL--VDRKILSDKYTAYIGADNYEIGRAVGNYIASSLK-GKGNVVelt 154
Cdd:cd19965    53 IASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAfnVDAPGGENARLAFVGQDLYPAGYVLGKRIAEKFKpGGGHVL--- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 155 gLGGSTP----AMERHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd19965   130 -LGISTPgqsaLEQRLDGIKQALKEYGRGITYDVIDTGTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLG 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2594348833 231 REKEMIFVGIDALPGKgngLELVLDNVLDAT---------FiYPtngdkVMQLAMNIL 279
Cdd:cd19965   209 LKGKVLVGGFDLVPEV---LQGIKAGYIDFTidqqpylqgF-YP-----VMQLFLYKK 257
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
44-244 3.38e-19

ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 88.39  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  44 DEILREAmfydGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISAneaAPMTP--IVEEAYQKGIPVILVDRKIlSDKY 121
Cdd:cd06289    22 EEALEEA----GYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSP---AAGTTaeLLRRLKAWGIPVVLALRDV-PGSD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 122 TAYIGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISNY---PDIKLIdkADAAWEREPAEVEM 198
Cdd:cd06289    94 LDYVGIDNRLGAQLATEHLIA--LGHRRIAFLGGLSDSSTRRERLAGFRAALAEAglpLDESLI--VPGPATREAGAEAA 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2594348833 199 DSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd06289   170 RELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEpgRDIAVVGFDDVP 217
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
711-819 3.46e-19

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: 83.66  E-value: 3.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLA 819
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDELIE 110
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
711-825 4.23e-19

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: 83.58  E-value: 4.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchiPVILLTAC 790
Cdd:cd17622     4 LLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG---PILLLTAL 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2594348833 791 SLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd17622    81 DSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
65-241 5.44e-19

ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 87.96  E-value: 5.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  65 DDNRKQAEDVHYFIDKGVDLLIIsaneaAPMTPIVEEAYQKGIPVILVDRKIlsDKYTAYIGADNYEIGRAVGNYIASsl 144
Cdd:cd06291    39 EDEEKEKEYLEMLKRNKVDGIIL-----GSHSLDIEEYKKLNIPIVSIDRYL--SEGIPSVSSDNYQGGRLAAEHLIE-- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 145 KGKGNVVELTGLGGSTPAMERHQGFMAAISNY---PDIKLIDkaDAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPG 221
Cdd:cd06291   110 KGCKKILHIGGPSNNSPANERYRGFEDALKEAgieYEIIEID--ENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIG 187
                         170       180
                  ....*....|....*....|..
gi 2594348833 222 AYQAAKKAGRE--KEMIFVGID 241
Cdd:cd06291   188 VLKALQKLGIRvpEDVQIIGFD 209
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
66-244 7.87e-19

periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380525 [Multi-domain]  Cd Length: 296  Bit Score: 88.07  E-value: 7.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  66 DNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYI-GADNYEIGRAVGNYIASSL 144
Cdd:cd06302    41 DAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSARDYFVnQADDEGLGEALVDSLAKEI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 145 KGKGNVVELTGlGGSTPAMERHQGFM--AAISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGA 222
Cdd:cd06302   121 GGKGKVAILSG-SLTATNLNAWIKAMkeYLKSKYPDIELVDTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAA 199
                         170       180
                  ....*....|....*....|..
gi 2594348833 223 YQAAKKAGREKEMIFVGIdALP 244
Cdd:cd06302   200 AQAVEEAGKTGKVAVTGI-GLP 220
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
711-849 8.08e-19

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 86.70  E-value: 8.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNgFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshRRLkqffgdgQTLAKEDVCDM 849
Cdd:PRK10161   85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM---RRI-------SPMAVEEVIEM 134
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
358-641 1.92e-18

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 91.12  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 358 SLRSKNRLNKELSEQkkqVEQQRDKLEEqrdILEEQRdkleeqrdqliQLSHQLEEATHAKLVFFTNISHDFRTPLTLVA 437
Cdd:PRK11466  401 NVHALNRHREQLAAQ---VKARTAELQE---LVIEHR-----------QARAEAEKASQAKSAFLAAMSHEIRTPLYGIL 463
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 438 DPVEhLLADSSLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENGKmeyTPISLD--------ILSSFEGWNESFMava 509
Cdd:PRK11466  464 GTAQ-LLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGG---KNVSVSdepfeprpLLESTLQLMSGRV--- 536
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 510 RKKHIHFSFDYMPDTDYRTLADVEKLERIYFNLLSNAFKFTPENgkvTVRLSSLTKDDHCWIrfTVANTGSMISAEHIRN 589
Cdd:PRK11466  537 KGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEG---SIVLRSRTDGEQWLV--EVEDSGCGIDPAKLAE 611
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 590 IFDRFYKIDMHHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:PRK11466  612 IFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLR 663
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
391-639 2.75e-18

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 88.73  E-value: 2.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 391 EEQRDKLEEQRDQLIQLSHQLEEATHAklvFFTNISHDFRTPLTLVADPVEHLlaDSSLSEDQRRMLLLVQRNVNILLRL 470
Cdd:NF012163  216 NDELGKLAQDFNQLASTLEKNEQMRRD---FMADISHELRTPLAVLRAELEAI--QDGIRKFTPESLDSLQAEVGTLTKL 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 471 VNQILDFRKYENGKMEYTPISLD----ILSSFEGWNESFmaVARKKHIHFSfdyMPDTDYrTLADVEKLERIYFNLLSNA 546
Cdd:NF012163  291 VDDLHDLSMSDEGALAYQKASVDlvplLEVEGGAFRERF--ASAGLELEVS---LPDSSL-VFGDRDRLMQLFNNLLENS 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 547 FKFTPENGKVTVRLSSLTKDdhcwIRFTVANTGSMISAEHIRNIFDRFYKIDMHH----AGSGIGLALVKAFVELHKGTI 622
Cdd:NF012163  365 LRYTDSGGSLHISASQRPKE----VTLTVADSAPGVSDEQLARLFERFYRVEVSRnrasGGSGLGLAISLNIVQAHGGTL 440
                         250
                  ....*....|....*..
gi 2594348833 623 TVESDEKQGTIFTVDLP 639
Cdd:NF012163  441 HAAHSPLGGLRIVVTLP 457
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
711-833 3.37e-18

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 84.47  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIPVILLTA 789
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDgMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR---QWSAIPVIVLSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQ 833
Cdd:PRK10529   81 RSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATPA 124
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
427-640 3.55e-18

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 88.75  E-value: 3.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 427 HDFRTPLTLVADPVEhLLADSSLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENGK--MEYTPISLDILssFEGWNES 504
Cdd:PRK11100  265 HELKSPLAAIRGAAE-LLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQelEVLEPVALAAL--LEELVEA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 505 FMAVARKKHIHFSFDymPDtDYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLSslTKDDHcwIRFTVANTGSMISA 584
Cdd:PRK11100  342 REAQAAAKGITLRLR--PD-DARVLGDPFLLRQALGNLLDNAIDFSPEGGTITLSAE--VDGEQ--VALSVEDQGPGIPD 414
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 585 EHIRNIFDRFY---KIDMHHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:PRK11100  415 YALPRIFERFYslpRPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
859-950 9.00e-18

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: 85.21  E-value: 9.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 859 ALIEAKMGDsNLNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTK 938
Cdd:COG4977   217 AWMEANLEE-PLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRR 295
                          90
                  ....*....|..
gi 2594348833 939 CYREQFGESPTD 950
Cdd:COG4977   296 AFRRRFGVSPSA 307
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
711-824 1.28e-17

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 79.63  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD--YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHipVILLT 788
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAgyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK--VIMCS 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNL 824
Cdd:cd17542    81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
707-834 2.22e-17

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 82.32  E-value: 2.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 707 SKPCVLIIDDN---ADIRLYVhglLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHI 782
Cdd:PRK11083    2 QQPTILLVEDEqaiADTLVYA---LQSEgFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLA--FHPAL 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 783 PVILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshRRLKQF 834
Cdd:PRK11083   77 PVIFLTARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTIL---RRVKKF 125
PRK10490 PRK10490
sensor protein KdpD; Provisional
377-642 2.23e-17

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 87.40  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 377 EQQR----------DKLEEQRDILEEQRDKLEEQRDQLiqlshqlEEATHAKLvfftniSHDFRTPLTLVADPVEHLLAD 446
Cdd:PRK10490  626 EQQRlletftlliaNALERLTLTASEEQARLASEREQL-------RNALLAAL------SHDLRTPLTVLFGQAEILTLD 692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 447 SSlSEDQRRMLLLVQRNVNIL--LRLVNQILDFRKYENG----KMEYTPISLDILSSFEGWNESFmavaRKKHIHFSfdy 520
Cdd:PRK10490  693 LA-SEGSPHARQASEIRQQVLntTRLVNNLLDMARIQSGgfnlRKEWLTLEEVVGSALQMLEPGL----SGHPINLS--- 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 521 MPDTDYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLSslTKDDhcWIRFTVANTGSMISAEHIRNIFDRFYKIDMH 600
Cdd:PRK10490  765 LPEPLTLIHVDGPLFERVLINLLENAVKYAGAQAEIGIDAH--VEGE--RLQLDVWDNGPGIPPGQEQLIFDKFARGNKE 840
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2594348833 601 HA--GSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQT 642
Cdd:PRK10490  841 SAipGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLET 884
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
49-244 2.92e-17

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 83.04  E-value: 2.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  49 EAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISAneAAPMTPIVEEAYQKGIPVILVDRKILSDKYtAYIGAD 128
Cdd:cd06285    23 DAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITP--ARDDAPDLQELAARGVPVVLVDRRIGDTAL-PSVTVD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 129 NYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISNYP-DIKLIDKADAAWEREPAEVEMDSMLRRHPK 207
Cdd:cd06285   100 NELGGRLATRHLLE--LGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGlPVPDERIVPGGFTIEAGREAAYRLLSRPER 177
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2594348833 208 IDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd06285   178 PTAVFAANDLMAIGVLRAARDLGLRvpEDLSVVGFDDIP 216
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
711-833 2.98e-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: 80.77  E-value: 2.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLY-VHGLLHTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQtchIPVILLT 788
Cdd:COG3707     6 VLVVDDEPLRRADlREGLREAGYEVVaEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APVILLT 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 789 ACSlDEQRIQ-GYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQ 833
Cdd:COG3707    83 AYS-DPELIErALEAGVSAYLVKPLDPEDLLPALELALARFRELRA 127
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
711-817 3.05e-17

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 78.53  E-value: 3.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYT-VIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLT 788
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLkELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVT 82
                          90       100
                  ....*....|....*....|....*....
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLL 817
Cdd:cd19923    83 AEAKKENVIAAAQAGVNNYIVKPFTAATL 111
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
541-639 5.17e-17

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: 77.33  E-value: 5.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 541 NLLSNAFKFT----PENGKVTVRLSsltkDDHCWIRFTVANTGSMISAEHIRNIFDRFY--KIDMHHagsGIGLALVKAF 614
Cdd:cd16915     7 NLIDNALDALaatgAPNKQVEVFLR----DEGDDLVIEVRDTGPGIAPELRDKVFERGVstKGQGER---GIGLALVRQS 79
                          90       100
                  ....*....|....*....|....*
gi 2594348833 615 VELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16915    80 VERLGGSITVESEPGGGTTFSIRIP 104
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
711-819 6.36e-17

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: 77.45  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqtcHI-PVILL 787
Cdd:cd19932     3 VLIAEDEALIRMDLREMLEEAgYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE----NIaPIVLL 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLA 819
Cdd:cd19932    79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIP 110
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
533-640 7.51e-17

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: 77.08  E-value: 7.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 533 EKLERIYFNLLSNAFKFTPENGKVTVRLSSltKDDHCWIrfTVANTGSMISAEHIRNIFDRFYKIDMHHAGSGIGLALVK 612
Cdd:cd16943     2 SQLNQVLLNLLVNAAQAMEGRGRITIRTWA--HVDQVLI--EVEDTGSGIDPEILGRIFDPFFTTKPVGEGTGLGLSLSY 77
                          90       100
                  ....*....|....*....|....*...
gi 2594348833 613 AFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:cd16943    78 RIIQKHGGTIRVASVPGGGTRFTIILPI 105
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
711-826 8.93e-17

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: 77.15  E-value: 8.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTChiPVILLTA 789
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDL--PVIMISG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLID 826
Cdd:cd17550    79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
705-833 9.94e-17

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 80.50  E-value: 9.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 705 DSSKPCVLIIDDNADI-RLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIP 783
Cdd:PRK10710    7 DENTPRILIVEDEPKLgQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR---RFSDIP 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2594348833 784 VILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshRRLKQ 833
Cdd:PRK10710   84 IVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTIL---RRCKP 130
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
55-232 1.23e-16

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 81.52  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSV-EIRSAADDNRKQAEDVHYFIDKGVDLLI-ISANEAApMTPIVEEAYQKGIPVILVDRKI----LSDKYTAYIGAD 128
Cdd:cd06316    29 GIEVvAVTDANFDPAKQITDLETLIALKPDIIIsIPVDPVA-TAAAYKKVADAGIKLVFMDNVPdgleAGKDYVSVVSSD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 129 NYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAI-SNYPDIKLIDKADAAWEREPAEVEMDsMLRRHPK 207
Cdd:cd06316   108 NRGNGQIAAELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLkEKYPDIKIVAEQGFADPNDAEEVASA-MLTANPD 186
                         170       180
                  ....*....|....*....|....*
gi 2594348833 208 IDAVYAHNDRIAPGAYQAAKKAGRE 232
Cdd:cd06316   187 IDGIYVSWDTPALGVISALRAAGRS 211
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
541-638 1.25e-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: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 541 NLLSNAFKFTPENGKVTVRLSSltkDDHCWIRftVANTGSMISAEHIRNIFDRFYKID-MHHAGSGIGLALVKAFVELHK 619
Cdd:cd16940    20 NLVDNAVRYSPQGSRVEIKLSA---DDGAVIR--VEDNGPGIDEEELEALFERFYRSDgQNYGGSGLGLSIVKRIVELHG 94
                          90
                  ....*....|....*....
gi 2594348833 620 GTITVESDEKQGTIFTVDL 638
Cdd:cd16940    95 GQIFLGNAQGGGLEAWVRL 113
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
709-823 2.03e-16

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: 75.89  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 709 PCVLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIPVILL 787
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEgYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR---EQSEVGIILV 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRN 823
Cdd:cd17619    78 TGRDDEVDRIVGLEIGADDYVTKPFNPRELLVRAKN 113
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
521-638 2.24e-16

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: 76.40  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 521 MPDTDYRTLADVEKLERIYFNLLSNAFKFTpENGKVtvrLSSLTKDDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMH 600
Cdd:cd16947     7 IPDRPIYANANTEALQRILKNLISNAIKYG-SDGKF---LGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDS 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2594348833 601 HA----GSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDL 638
Cdd:cd16947    83 RNsakqGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
711-833 4.21e-16

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 75.60  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRL-YVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLTA 789
Cdd:cd17549     1 VLLVDDDADVREaLQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRE--LDPDLPVILITG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 790 ---CSLDEQRIQgydGGADSYISKPFSSQLLLARV------RNLIDSHRRLKQ 833
Cdd:cd17549    79 hgdVPMAVEAMR---AGAYDFLEKPFDPERLLDVVrralekRRLVLENRRLRQ 128
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
541-639 4.27e-16

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: 74.93  E-value: 4.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 541 NLLSNAFKFTPENGKVTVRLSsltKDDHCwIRFTVANTGSMISAEHIRNIFDRFYKIDMHHA----GSGIGLALVKAFVE 616
Cdd:cd16952     7 NLVSNAVKYTPPSDTITVRWS---QEESG-ARLSVEDTGPGIPPEHIPRLTERFYRVDIERCrntgGTGLGLAIVKHVMS 82
                          90       100
                  ....*....|....*....|...
gi 2594348833 617 LHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16952    83 RHDARLLIASELGKGSRFTCLFP 105
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
509-640 4.80e-16

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 81.76  E-value: 4.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 509 ARKKHIHFSFDYMPDTDyRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLSSLTKDdhcwIRFTVANTGSMISAEHIR 588
Cdd:PRK10364  324 ANSREIQLRFTANDTLP-EIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAG----VKISVTDSGKGIAADQLE 398
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2594348833 589 NIFDRFY--KIDmhhaGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:PRK10364  399 AIFTPYFttKAE----GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
27-244 5.27e-16

Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 79.21  E-value: 5.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  27 RIGVAQCSDDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKg 106
Cdd:cd01537     1 RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQN- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 107 IPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAIS-NYPDIKLIDKA 185
Cdd:cd01537    80 VPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAK--HGHIQIVLLKGPLGHPDAEARLAGVIKELNdKGIKTEQLQLD 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 186 DAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd01537   158 TGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRvpSDISVFGYDALP 218
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
711-811 5.42e-16

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 74.72  E-value: 5.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVP---------DLIISDVMMPGMDGIECCRRLKSELQTC 780
Cdd:cd19924     1 ILVVDDSPTARkQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2594348833 781 HIPVILLTACSLDEQRIQGYDGGADSYISKP 811
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
711-825 6.42e-16

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 78.04  E-value: 6.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYV-HGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTA 789
Cdd:PRK09836    3 LLIVEDEKKTGEYLtKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKG--MPILLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:PRK09836   81 LGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL 116
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
394-653 6.98e-16

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 82.42  E-value: 6.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 394 RDKLEEQRDQLiqlSHQLEEATHAKLV--FFTNISHDFRTPLTLVADPVEhlLADSSLSEDQ--RRMLLLVQRNVNILLR 469
Cdd:PRK13837  427 RRRLETERDAL---ERRLEHARRLEAVgtLASGIAHNFNNILGAILGYAE--MALNKLARHSraARYIDEIISAGARARL 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 470 LVNQILDF-RKyenGKMEYTPISLDILSsfeGWNESFMAVARKKHIHFSFDYmPDTDYRTLADVEKLERIYFNLLSNAFK 548
Cdd:PRK13837  502 IIDQILAFgRK---GERNTKPFDLSELV---TEIAPLLRVSLPPGVELDFDQ-DQEPAVVEGNPAELQQVLMNLCSNAAQ 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 549 FTPENGKVTVRLS--SLTKDDHC---------WIRFTVANTGSMISAEHIRNIFDRFYKidMHHAGSGIGLALVKAFVEL 617
Cdd:PRK13837  575 AMDGAGRVDISLSraKLRAPKVLshgvlppgrYVLLRVSDTGAGIDEAVLPHIFEPFFT--TRAGGTGLGLATVHGIVSA 652
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2594348833 618 HKGTITVESDEKQGTIFTVDLPVQTCETVVSENSPA 653
Cdd:PRK13837  653 HAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQAFFG 688
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
711-825 7.14e-16

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: 74.37  E-value: 7.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTDYTVIEAAD-GSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLK-SELQTchiPVILLT 788
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDlGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRlAKVKT---PILILS 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd17616    78 GLADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
711-812 1.13e-15

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 73.85  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRlYV--HGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLT 788
Cdd:cd19919     3 VWIVDDDSSIR-WVleRALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ--RHPDLPVIIMT 79
                          90       100
                  ....*....|....*....|....
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPF 812
Cdd:cd19919    80 AHSDLDSAVSAYQGGAFEYLPKPF 103
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
711-819 1.78e-15

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: 73.21  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIE-AADGSEGIRKAMKYVPDLIISDVMMPG-MDGIECCRRLKSElqtCHIPVILL 787
Cdd:cd17534     3 ILIVEDEAIIALDLKEILESlGYEVVGiADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREK---FDIPVIFL 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 788 TACSlDEQRIQ-----GYDGgadsYISKPFSSQLLLA 819
Cdd:cd17534    80 TAYS-DEETLEraketNPYG----YLVKPFNERELKA 111
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
710-830 1.86e-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: 75.91  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 710 CVLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLT 788
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESaGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAA--RGSPLPVIFLT 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 789 AcsldeqriQGyD---------GGADSYISKPFSSQLLLARVRNLIDSHRR 830
Cdd:COG4566    79 G--------HG-DvpmavramkAGAVDFLEKPFDDQALLDAVRRALARDRA 120
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
406-642 2.18e-15

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 80.06  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 406 QLSHQLEEATHAKLVFFTNISHDFRTPLTL-------VADPVEHLLADSSLSedqrrmlllVQRNVNILLRLVNQILDFR 478
Cdd:PRK10549  228 QLASTLEKNEQMRRDFMADISHELRTPLAVlrgeleaIQDGVRKFTPESVAS---------LQAEVGTLTKLVDDLHQLS 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 479 KYENGKMEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDyMPDtDYRTLADVEKLERIYFNLLSNAFKFTPENGKVTV 558
Cdd:PRK10549  299 LSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLS-LPD-SATVFGDPDRLMQLFNNLLENSLRYTDSGGSLHI 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 559 RLSSltKDDHCWIRFtvANTGSMISAEHIRNIFDRFYKIDMHH----AGSGIGLALVKAFVELHKGTITVESDEKQGTIF 634
Cdd:PRK10549  377 SAEQ--RDKTLRLTF--ADSAPGVSDEQLQKLFERFYRTEGSRnrasGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSI 452

                  ....*...
gi 2594348833 635 TVDLPVQT 642
Cdd:PRK10549  453 TVELPLER 460
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
711-825 5.51e-15

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 75.22  E-value: 5.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVpDLIISDVMMPGMDGIECCRRLKSELQTchiPVILLTA 789
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQALDLLDDSI-DLLLLDVMMPKKNGIDTLKELRQTHQT---PVIMLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:PRK10955   80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAIL 115
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
711-833 5.68e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 75.24  E-value: 5.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILL 787
Cdd:COG3279     4 ILIVDDEPLARERLERLLekYPDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRE--LDPPPPIIFT 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2594348833 788 TAcsLDEQRIQGYDGGADSYISKPFSSQLL---LARVRNLIDSHRRLKQ 833
Cdd:COG3279    82 TA--YDEYALEAFEVNAVDYLLKPIDEERLakaLEKAKERLEAKAAAEA 128
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
711-822 6.83e-15

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: 71.71  E-value: 6.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQtchIPVILLTA 789
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERgFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSD---VPIIIISG 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2594348833 790 CSLDEQ-RIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:cd17594    79 DRRDEIdRVVGLELGADDYLAKPFGLRELLARVR 112
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
711-826 1.06e-14

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: 71.27  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD--YTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqtCHIPVILL 787
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDpdIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE---RPTPVVMV 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2594348833 788 TacSLDEQR----IQGYDGGADSYISKPFS--SQLLLARVRNLID 826
Cdd:cd17541    80 S--SLTEEGaeitLEALELGAVDFIAKPSGgiSLDLEEIAEELIE 122
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
711-811 1.38e-14

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: 70.17  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIPVILLTA 789
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR---QKSTLPVIFLTS 77
                          90       100
                  ....*....|....*....|..
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKP 811
Cdd:cd19936    78 KDDEIDEVFGLRMGADDYITKP 99
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
711-824 1.49e-14

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: 70.71  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqTCHIPVILLTA 789
Cdd:cd17554     3 ILVVDDEENIReLYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK--KPDLPVIICTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2594348833 790 CSLDEQRIQGYdgGADSYISKPFSSQLLLARVRNL 824
Cdd:cd17554    81 YSEYKSDFSSW--AADAYVVKSSDLTELKETIKRL 113
PRK10766 PRK10766
two-component system response regulator TorR;
710-825 1.53e-14

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 73.92  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 710 CVLIIDDNADIRLYVHGLL-HTDYTVIEAADGsEGIRKAMKYVP-DLIISDVMMPGMDGIECCRRLKSelqTCHIPVILL 787
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFeQEGYTVSEAASG-AGMREIMQNQHvDLILLDINLPGEDGLMLTRELRS---RSTVGIILV 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:PRK10766   80 TGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
34-261 4.62e-14

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 73.70  E-value: 4.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  34 SDDSWRHKMNDEIlREAMFYDGVSVeIRSAADDNRKQAedVHYF---IDKGVDLLIISAneAAPMTP-IVEEAYQKGIPV 109
Cdd:pfam00532  11 LDEPFFQDLVKGI-TKAAKDHGFDV-FLLAVGDGEDTL--TNAIdllLASGADGIIITT--PAPSGDdITAKAEGYGIPV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 110 ILVDRKILSDKYTAYIGADNYEIGRAVGNYIASSLKGKGNVVeLTGLGGSTPAMERHQGFMAAISNYP-DIKLIDKADAA 188
Cdd:pfam00532  85 IAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRPIAV-MAGPASALTARERVQGFMAALAAAGrEVKIYHVATGD 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 189 WEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKemifvGIDALPGKGNGLeLVLDNVLDAT 261
Cdd:pfam00532 164 NDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRVK-----IPDIVGIGINSV-VGFDGLSKAQ 230
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
711-824 5.21e-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: 69.47  E-value: 5.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYTVIEAADGSEGIRKAMKYvPD--LIISDVMMPGMDGIECCRRLKSELQTCHIPVILL 787
Cdd:cd17544     3 VLVVDDSATSRNHLRALLrRHNFQVLEAANGQEALEVLEQH-PDikLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2594348833 788 TAC---SLDEQRIQgydGGADSYISKPFSSQLLLARV-RNL 824
Cdd:cd17544    82 SASgdnALSARFIK---AGANDFLTKPFLPEEFYCRVtQNL 119
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
852-956 5.32e-14

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: 74.70  E-value: 5.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 852 DFVEKFKALIEAKmGDSNLNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLaSSDMTVAEIGYEVGFS 931
Cdd:COG2169    84 DLVARACRLIEAG-AEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFG 161
                          90       100
                  ....*....|....*....|....*
gi 2594348833 932 SPSYFTKCYREQFGESPTDLlkRKG 956
Cdd:COG2169   162 SLSRFYEAFKKLLGMTPSAY--RRG 184
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
52-239 5.77e-14

periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.


Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 73.36  E-value: 5.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  52 FYDGVSVEIRSAADDNRKQAEDVHYF----------------IDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRK 115
Cdd:cd06307    13 FYELLRRAIEAAAAALRDRRVRLRIHfvdsldpealaaalrrLAAGCDGVALVAPDHPLVRAAIDELAARGIPVVTLVSD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 116 ILSDKYTAYIGADNYEIGRAVGNYIASSLKGK-GNVVELTGLGGSTPAMERHQGFMAAIS-NYPDIKLIDKADAAWEREP 193
Cdd:cd06307    93 LPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRpGKVLVILGSHRFRGHEEREAGFRSVLReRFPDLTVLEVLEGLDDDEL 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2594348833 194 AEVEMDSMLRRHPKIDAVY---AHNDRIApgayQAAKKAGREKEMIFVG 239
Cdd:cd06307   173 AYELLRELLARHPDLVGIYnagGGNEGIA----RALREAGRARRVVFIG 217
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
531-639 9.85e-14

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: 68.26  E-value: 9.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 531 DVEKLERIYFNLLSNAFKFTPENGKVTVRLSSLTKDdhcwIRFTVANTGSMISAEHIRNIFDRFYKIDMHH----AGSGI 606
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQE----VRLDVEDSAPGVSDDQLARLFERFYRVESSRnrasGGSGL 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 607 GLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16946    77 GLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
531-636 1.30e-13

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: 67.87  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 531 DVEKLERIYFNLLSNAFKFTPENGKVTVrlssLTKDDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDM-HHAGS--GIG 607
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVSI----SIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTsRRSGGhyGMG 76
                          90       100
                  ....*....|....*....|....*....
gi 2594348833 608 LALVKAFVELHKGTITVESDEKQGTIFTV 636
Cdd:cd16975    77 LYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-639 1.45e-13

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: 67.74  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTpengkvtvrlsslTKDDHCWI-----------RFTVANTGSMISAEHIRNIFDRFYKIDMHHA- 602
Cdd:cd16921     1 LGQVLTNLLGNAIKFR-------------RPRRPPRIevgaedvgeewTFYVRDNGIGIDPEYAEKVFGIFQRLHSREEy 67
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2594348833 603 -GSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16921    68 eGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
28-244 1.53e-13

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 72.30  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  28 IGVAQCSDDSWRHKMNDEILrEAMFYD----GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLII---SANEAAPMTpive 100
Cdd:cd01391     2 IGVVTSSLHQIREQFGIQRV-EAIFHTadklGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGpgsSSVAIVIQN---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 101 EAYQKGIPVILVDRKILSD------KYTAYIGADNYEIGRAVGNYIAssLKGKGNVVELTG-LGGSTPAmeRHQGFMAAI 173
Cdd:cd01391    77 LAQLFDIPQLALDATSQDLsdktlyKYFLSVVFSDTLGARLGLDIVK--RKNWTYVAAIHGeGLNSGEL--RMAGFKELA 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 174 SNyPDIKLIDKADAAWER-EPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDALP 244
Cdd:cd01391   153 KQ-EGICIVASDKADWNAgEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVIGSDGWA 223
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
65-231 2.47e-13

ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380511 [Multi-domain]  Cd Length: 268  Bit Score: 71.04  E-value: 2.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  65 DDNRKQAED-VHYFIDKGVDLLIISANEAAPMTPIVEEAyqkGIPVILVDRKILSDKYTAYIgADNYEIGRAVGNYIASs 143
Cdd:cd06288    39 GGDPELEAEaIRELLSRRVDGIIYASMHHREVTLPPELT---DIPLVLLNCFDDDPSLPSVV-PDDEQGGYLATRHLIE- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 144 lKGKGNVVELTGLGGSTPAMERHQGFMAAISNY---PDIKLIdkADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAP 220
Cdd:cd06288   114 -AGHRRIAFIGGPEDSLATRLRLAGYRAALAEAgipYDPSLV--VHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAM 190
                         170
                  ....*....|.
gi 2594348833 221 GAYQAAKKAGR 231
Cdd:cd06288   191 GVYQAAAELGL 201
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
82-230 2.73e-13

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 71.03  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  82 VDLLIISAneAAPMTPIVEEAYQKGIPVILVDRKIlSDKYTAYIGADNYEIGRAVGNYIASSlkGKGNVVELTGLGGSTP 161
Cdd:cd06278    55 VDGVIVTS--ATLSSELAEECARRGIPVVLFNRVV-EDPGVDSVSCDNRAGGRLAADLLLAA--GHRRIAFLGGPEGTST 129
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 162 AMERHQGFMAAISNYpDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd06278   130 SRERERGFRAALAEL-GLPPPAVEAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEG 197
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
709-811 2.84e-13

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: 67.23  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 709 PCVLIIDDNADIRL-YVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqTCHIPVILL 787
Cdd:cd17555     1 ATILVIDDDEVVREsIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVIVV 78
                          90       100
                  ....*....|....*....|....
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKP 811
Cdd:cd17555    79 SGAGVMSDAVEALRLGAWDYLTKP 102
PRK10610 PRK10610
chemotaxis protein CheY;
712-817 3.79e-13

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 67.31  E-value: 3.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 712 LIIDDNADIRLYVHGLLHT--DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:PRK10610    9 LVVDDFSTMRRIVRNLLKElgFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTA 88
                          90       100
                  ....*....|....*....|....*...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLL 817
Cdd:PRK10610   89 EAKKENIIAAAQAGASGYVVKPFTAATL 116
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-624 4.03e-13

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 66.33  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTPENGkvTVRLSSLTKDDHcwIRFTVANTGSMISAEHIRNIFDRFYKIDMHHAG---SGIGLALV 611
Cdd:cd16945     5 LRQAINNLLDNAIDFSPEGG--LIALQLEADTEG--IELLVFDEGSGIPDYALNRVFERFYSLPRPHSGqksTGLGLAFV 80
                          90
                  ....*....|...
gi 2594348833 612 KAFVELHKGTITV 624
Cdd:cd16945    81 QEVAQLHGGRITL 93
PRK13557 PRK13557
histidine kinase; Provisional
425-826 4.70e-13

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 72.78  E-value: 4.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 425 ISHDFRTPLTLVADPVEHLLA----DSSLSEDQRRMLLLVQRNVNILLRLVNQILDF-RKYengKMEYTPISLDILSsfe 499
Cdd:PRK13557  170 IAHDFNNLLQVMSGYLDVIQAalshPDADRGRMARSVENIRAAAERAATLTQQLLAFaRKQ---RLEGRVLNLNGLV--- 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 500 gwnESFMAVARK---KHIHFSFDYMPDTdYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLSSLTKDDH-------- 568
Cdd:PRK13557  244 ---SGMGELAERtlgDAVTIETDLAPDL-WNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVEIEDEdlamyhgl 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 569 ---CWIRFTVANTGSMISAEHIRNIFDRFYKIDMHHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVqtcet 645
Cdd:PRK13557  320 ppgRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPA----- 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 646 vvsenspafsvsatsvtstdatTSAVAGVPATPATSGYSGSSSlndaltyeeeelEKsydsskpcVLIIDDNADI----R 721
Cdd:PRK13557  395 ----------------------SDQAENPEQEPKARAIDRGGT------------ET--------ILIVDDRPDVaelaR 432
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 722 LYVHGLlhtDYTVIEAADGsegiRKAMKYV-----PDLIISDVMMPG-MDGIECCRRLKSELQTCHipvILLTAcSLDEQ 795
Cdd:PRK13557  433 MILEDF---GYRTLVASNG----REALEILdshpeVDLLFTDLIMPGgMNGVMLAREARRRQPKIK---VLLTT-GYAEA 501
                         410       420       430
                  ....*....|....*....|....*....|...
gi 2594348833 796 RIQGYDGGADSY--ISKPFSSQLLLARVRNLID 826
Cdd:PRK13557  502 SIERTDAGGSEFdiLNKPYRRAELARRVRMVLD 534
PRK15479 PRK15479
transcriptional regulator TctD;
711-926 7.94e-13

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 68.59  E-value: 7.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVH-GLLHTDYTVIEAADG--SEGIRKAMKYVpdLIISDVMMPGMDGIECCRRLKSELQTchIPVILL 787
Cdd:PRK15479    3 LLLAEDNRELAHWLEkALVQNGFAVDCVFDGlaADHLLQSEMYA--LAVLDINMPGMDGLEVLQRLRKRGQT--LPVLLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIdshRRLKQFFGDGQTLAkEDVCDMDKDFVEKFKALIEAKMGD 867
Cdd:PRK15479   79 TARSAVADRVKGLNVGADDYLPKPFELEELDARLRALL---RRSAGQVQEVQQLG-ELIFHDEGYFLLQGQPLALTPREQ 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2594348833 868 SNLNVEDLGKDMGLSRVQLYRKIKSLTN-YSPNEL-LRIARLKKAaslLASSDM---TVAEIGY 926
Cdd:PRK15479  155 ALLTVLMYRRTRPVSRQQLFEQVFSLNDeVSPESIeLYIHRLRKK---LQGSDVritTLRGLGY 215
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
711-824 9.16e-13

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: 69.44  E-value: 9.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNAD-IRLYVHGL-LHTDYTVIEAA-DGSEGIRKAMKYVPDLIISDVMMPGMDGI---ECCRRLKSELqtcHIPV 784
Cdd:COG5801     7 VLIADDNREfCELLEEYLsSQPDMEVVGVAyNGLEALELIEEKKPDVVILDIIMPHLDGLgvlEKLREMNLEK---RPKV 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2594348833 785 ILLTACSLDE--QRIqgYDGGADSYISKPFSSQLLLARVRNL 824
Cdd:COG5801    84 IMLTAFGQEDitQRA--VELGADYYILKPFDLDVLAERIRQL 123
PRK15395 PRK15395
galactose/glucose ABC transporter substrate-binding protein MglB;
1-283 9.18e-13

galactose/glucose ABC transporter substrate-binding protein MglB;


Pssm-ID: 185293 [Multi-domain]  Cd Length: 330  Bit Score: 70.53  E-value: 9.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833   1 MKYTKWITVLFCLLGLAACRQDAPRfRIGVAQCS-DDSWRHKMNDEILREAMFYDGVSVEIRSAADDNRKQAEDVHYFID 79
Cdd:PRK15395    1 NKKVLTLSALMASMLFGAAAAAADT-RIGVTIYKyDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  80 KGVDLLIISANEAAPMTPIVEEAYQKGIPVILVD----RKILSDKYTA-YIGADNYEIGRAVGNYIASSLK--------- 145
Cdd:PRK15395   80 KGVKALAINLVDPAAAPTVIEKARGQDVPVVFFNkepsRKALDSYDKAyYVGTDSKESGIIQGDLIAKHWKanpawdlnk 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 146 -GKGNVVELTGLGGStPAMERHQGFMAAISNYPDIK----LIDKadAAWEREPAEVEMDSMLR--RHPKIDAVYAHNDRI 218
Cdd:PRK15395  160 dGKIQYVLLKGEPGH-PDAEARTTYVIKELNDKGIKteqlQLDT--AMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAM 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2594348833 219 APGAYQAAKKAGREKEMIFvGIDALPgkgNGLELVLDNVLDATFIYPTN--GDKVMQLAMNILEKKS 283
Cdd:PRK15395  237 AMGAVEALKAHNKSSIPVF-GVDALP---EALALVKSGAMAGTVLNDANnqAKATFDLAKNLADGKG 299
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
711-825 1.43e-12

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: 65.00  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIPVILLTA 789
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR---QISNVPIIFISS 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:cd18159    78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
711-822 1.50e-12

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 67.75  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT--DYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIpvILL 787
Cdd:PRK10651    9 ILLIDDHPMLRTGVKQLISMapDITVVgEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRI--VVF 86
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:PRK10651   87 SVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQ 121
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
711-823 2.32e-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: 64.68  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD--YTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIpvILL 787
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDpdFTVVgEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARI--VIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRN 823
Cdd:cd19931    79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQ 114
PRK10643 PRK10643
two-component system response regulator PmrA;
753-828 3.88e-12

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 66.60  E-value: 3.88e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833 753 DLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSH 828
Cdd:PRK10643   46 SLVVLDLGLPDEDGLHLLRRWRQKKYT--LPVLILTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRH 119
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
711-773 4.55e-12

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 64.14  E-value: 4.55e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRL 773
Cdd:COG2197     4 VLIVDDHPLVREGLRALLeaEPDIEVVgEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
711-811 4.58e-12

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: 62.99  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDN---ADIRLYVhgLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIPVILL 787
Cdd:cd17621     1 VLVVEDEesfSDPLAYL--LRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMV 75
                          90       100
                  ....*....|....*....|....
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKP 811
Cdd:cd17621    76 TAKDSEIDKVVGLELGADDYVTKP 99
PRK10604 PRK10604
sensor protein RstB; Provisional
406-640 6.90e-12

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 68.86  E-value: 6.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 406 QLSHQLEEATHAKLVFFTNISHDFRTPLTlvadPVEHLLADS-SLSEDQRRMLllvQRNVNILLRLVNQILDFRKYENGK 484
Cdd:PRK10604  200 QMADNINALIASKKQLIDGIAHELRTPLV----RLRYRLEMSdNLSAAESQAL---NRDIGQLEALIEELLTYARLDRPQ 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 485 MEYTPISLDILSSFEGWNESFMAVARKKHIHFSFDYMPDTDYrtlADVEKLERIYFNLLSNAFKFTpeNGKVTVRLSsLT 564
Cdd:PRK10604  273 NELHLSEPDLPAWLSTHLADIQAVTPEKTVRLDTPHQGDYGA---LDMRLMERVLDNLLNNALRYA--HSRVRVSLL-LD 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 565 KDDHCwirFTVANTGSMISAEHIRNIFDRFYKIDMHH----AGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:PRK10604  347 GNQAC---LIVEDDGPGIPPEERERVFEPFVRLDPSRdratGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPV 423
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-639 7.09e-12

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: 62.98  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTP-ENGKVTVRLSSLTKDdhcwIRFTVANTGSMISAEHIRNIFDRFY----KIDMHHAGSGIGLA 609
Cdd:cd16953     1 LGQVLRNLIGNAISFSPpDTGRITVSAMPTGKM----VTISVEDEGPGIPQEKLESIFDRFYterpANEAFGQHSGLGLS 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2594348833 610 LVKAFVELHKGTITVES----DEKQGTIFTVDLP 639
Cdd:cd16953    77 ISRQIIEAHGGISVAENhnqpGQVIGARFTVQLP 110
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
711-762 7.44e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.05  E-value: 7.44e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833  711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMP 762
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
509-641 8.80e-12

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: 68.60  E-value: 8.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 509 ARKKHIHFSFDYMpDTDYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRlsslTKDDHCWIRFTVANTGSMISAEHIR 588
Cdd:COG5805   371 AILHNIQIRLELL-DEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIH----TEEEDNSVIIRVIDEGIGIPEERLK 445
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 589 NIFDRFYKidMHHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:COG5805   446 KLGEPFFT--TKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPLS 496
PRK11173 PRK11173
two-component response regulator; Provisional
709-825 9.90e-12

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 65.81  E-value: 9.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 709 PCVLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKselQTCHIPVILL 787
Cdd:PRK11173    4 PHILIVEDELVTRNTLKSIFEAEgYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR---EQANVALMFL 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:PRK11173   81 TGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLL 118
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
711-822 1.38e-11

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 62.17  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIpvILL 787
Cdd:cd17532     1 ALIVDDEPLAREELRYLLeeHPDIEIVgEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLI--VFV 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2594348833 788 TAcsLDEQRIQGYDGGADSYISKPFSSQLL---LARVR 822
Cdd:cd17532    79 TA--YDEYAVEAFELNAVDYLLKPFSEERLaeaLAKLR 114
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
30-283 1.66e-11

ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380656  Cd Length: 296  Bit Score: 66.15  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  30 VAQCSDDSWRHKMNDEIlrEAMFYD-GVSV-EIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGI 107
Cdd:cd20001     5 VVKVTGIAWFDRMETGV--EQFAKDtGVNVyQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 108 PVILVDRKILsdKYTAY-IGA-DNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMERHQGFMAAI-SNYPDIKLI-- 182
Cdd:cd20001    83 VVITHEASNL--KNVDYdVEAfDNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEWANAAVAYQkANYPDMLLVtd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 183 -----DKADAAWERepaeveMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIFVGIdALPGKGNglELVLDNV 257
Cdd:cd20001   161 rvetnDDSETAYEK------AKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGKIAVVGT-GLPSVAG--EYLEDGT 231
                         250       260
                  ....*....|....*....|....*...
gi 2594348833 258 LDATFIY-PTN-GDKVMQLAMNILEKKS 283
Cdd:cd20001   232 IDYIQFWdPADaGYAMNALAVMVLEGEK 259
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
69-240 2.03e-11

ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380658  Cd Length: 298  Bit Score: 66.15  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  69 KQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYE-IGRAVGNYIASSLKGK 147
Cdd:cd20003    44 KQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWDSDVNPDARDFFVNQATPEgIGKTLVDMVAEQTGEK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 148 GNVVELTglggSTPA---MERHQGFMAAI--SNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGA 222
Cdd:cd20003   124 GKVAIVT----SSPTatnQNAWIKAMKAYiaEKYPDMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGA 199
                         170
                  ....*....|....*...
gi 2594348833 223 YQAAKKAGREKEMIFVGI 240
Cdd:cd20003   200 AEAVEQLGRTGKVAVTGL 217
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
711-833 2.22e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 66.33  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLkseLQTCHIPVILL 787
Cdd:PRK00742    6 VLVVDDSAFMRRLISEILnsDPDIEVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKI---MRLRPTPVVMV 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 788 TacSLDEQ----RIQGYDGGADSYISKPFSS---------QLLLARVRNLidSHRRLKQ 833
Cdd:PRK00742   83 S--SLTERgaeiTLRALELGAVDFVTKPFLGislgmdeykEELAEKVRAA--ARARVRA 137
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-639 2.26e-11

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 61.26  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFK----FTPENGKVTVRLSSLTKDdhcWIRFTVANTGSMISAEHIRNIFDRFY--KIDmhhaGSGIGL 608
Cdd:cd16920     1 IQQVLINLVRNGIEamseGGCERRELTIRTSPADDR---AVTISVKDTGPGIAEEVAGQLFDPFYttKSE----GLGMGL 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2594348833 609 ALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16920    74 SICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
404-639 2.56e-11

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 66.14  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 404 LIQLSHQLEEATHAKLVFFTNISHDFRTPLTLVADPVEhLLADSSLSEDQrrmlLLVQRnVNILLRLVNQILDFRKYENg 483
Cdd:PRK10755  123 LNQLVSRLTSTLDQERLFTADVAHELRTPLAGIRLHLE-LLEKQHHIDVA----PLIAR-LDQMMHTVEQLLQLARAGQ- 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 484 KM---EYTPISLD---ILSSFEGWNEsfMAVARKKHIHFSfdyMPDTDYRTLADVEKLERIYFNLLSNAFKFTPENGKVT 557
Cdd:PRK10755  196 SFssgHYQTVKLLedvILPSQDELSE--MLEQRQQTLLLP---ESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTIT 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 558 VRLSSltKDDHCwiRFTVANTGSMISAEHIRNIFDRFYKIDMHHAGSGIGLALVKAFVELHKGTITVES-DEKQGTIFTV 636
Cdd:PRK10755  271 IKLSQ--EDGGA--VLAVEDEGPGIDESKCGELSKAFVRMDSRYGGIGLGLSIVSRITQLHHGQFFLQNrQERSGTRAWV 346

                  ...
gi 2594348833 637 DLP 639
Cdd:PRK10755  347 WLP 349
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
55-276 2.94e-11

monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380621 [Multi-domain]  Cd Length: 278  Bit Score: 65.04  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAP-MTPIVEEAYQKGIPVILVD----RKILSDKYTAYIGADN 129
Cdd:cd19966    30 GVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGaYTPLIEAAKKAGIIVTSFNtdlpKLEYGDCGLGYVGADL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 130 YEIGRAVGNYIA--SSLKgKGNVVELTGL-GGSTPAMERHQGFMAAISNYPDIKLIDKADAAwEREPAEVE--MDSMLRR 204
Cdd:cd19966   110 YAAGYTLAKELVkrGGLK-TGDRVFVPGLlPGQPYRVLRTKGVIDALKEAGIKVDYLEISLE-PNKPAEGIpvMTGYLAA 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 205 HPKIDAVYA-HNDRIAPGAyQAAKKAGREK-EMIFVGIDALPGKGNGLE-----LVLDNVLDATFIYPtngdkVMQLAM 276
Cdd:cd19966   188 NPDVKAIVGdGGGLTANVA-KYLKAAGKKPgEIPVAGFDLSPATVQAIKsgyvnATIDQQPYLQGYLP-----VLQIYL 260
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
535-639 3.07e-11

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: 61.24  E-value: 3.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTPENGKVTVRLSSLTKDD-----HC------WIRFTVANTGSMISAEHIRNIFDRFYKIDMHHAG 603
Cdd:cd16919     1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDAdyalnYRdlipgnYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 604 SGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16919    81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
417-483 3.79e-11

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 59.53  E-value: 3.79e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2594348833 417 AKLVFFTNISHDFRTPLTLVADPVEhLLADSSLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENG 483
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLE-LLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
PRK10337 PRK10337
sensor protein QseC; Provisional
365-636 5.47e-11

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 65.83  E-value: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 365 LNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQrdQLIQLSHQLEEATHAKLV----FFTNISHDFRTPLTlvADPV 440
Cdd:PRK10337  182 LGRELAPLKKLALALRMRDPDSETPLNATGVPSEVR--PLVEALNQLFARTHAMMVrerrFTSDAAHELRSPLA--ALKV 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 441 EHLLADSSLSEDQRRMLLLVQRNVNI--LLRLVNQILDFRKYENGK--MEYTPISL-DILSSfegwneSFMAV---ARKK 512
Cdd:PRK10337  258 QTEVAQLSDDDPQARKKALLQLHAGIdrATRLVDQLLTLSRLDSLDnlQDVAEIPLeDLLQS------AVMDIyhtAQQA 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 513 HIHFSFDyMPDTDYRTLADVEKLERIYFNLLSNAFKFTPENGKVTVRLSSLtkddhcwiRFTVANTGSMISAEHIRNIFD 592
Cdd:PRK10337  332 GIDVRLT-LNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSVVDVTLNAR--------NFTVRDNGPGVTPEALARIGE 402
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2594348833 593 RFYKIDMHHA-GSGIGLALVKAFVELHKGTITVESDEKQGTIFTV 636
Cdd:PRK10337  403 RFYRPPGQEAtGSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKV 447
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
711-833 5.61e-11

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: 60.67  E-value: 5.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADI-RLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTChiPVILLTA 789
Cdd:cd17572     1 VLLVEDSPSLaALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPT--SVIVITA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDsHRRLKQ 833
Cdd:cd17572    79 HGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALK-HRKLTK 121
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
54-244 6.39e-11

ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380519 [Multi-domain]  Cd Length: 270  Bit Score: 64.22  E-value: 6.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  54 DGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIIsanEAAPMT-PIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEI 132
Cdd:cd06296    28 AGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVL---VTSDPTsRQLRLLRSAGIPFVLIDPVGEPDPDLPSVGATNWAG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 133 GRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAIS---NYPDIKLIDKADaaWEREPAEVEMDSMLRRHPKID 209
Cdd:cd06296   105 GRLATEHLLD--LGHRRIAVITGPPRSVSGRARLAGYRAALAeagIAVDPDLVREGD--FTYEAGYRAARELLELPDPPT 180
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2594348833 210 AVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd06296   181 AVFAGNDEQALGVYRAARALGLRvpDDLSVIGFDDTP 217
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
398-640 6.47e-11

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: 65.66  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 398 EEQRDQLIQlSHQLEEATHaklvFFTNISHDFRTPLTLVADPVEHLLADSSLSEDQRR----MLLLVQRNVNIllrlVNQ 473
Cdd:COG5806   186 ILLRKELQR-AEKLEVVSE----LAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQyiriALEELDRAEAI----ITD 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 474 ILDFRKYENGKMEYTPIS------LDILSSFegwnesfmavARKKHIHFSFDYMPdtDYRTLADVEKLERIYFNLLSNAF 547
Cdd:COG5806   257 YLTFAKPQPEKLEKIDVSeelehvIDVLSPY----------ANMNNVEIQTELEP--GLYIEGDRQKLQQCLINIIKNGI 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 548 KFTPENGKVTVRLSSltKDDHCWIRftVANTGSMISAEHIRNIFDRFY--KIDmhhaGSGIGLALVKAFVELHKGTITVE 625
Cdd:COG5806   325 EAMPNGGTLTIDVSI--DKNKVIIS--IKDTGVGMTKEQLERLGEPYFstKEK----GTGLGTMVSYRIIEAMNGTIRVE 396
                         250
                  ....*....|....*
gi 2594348833 626 SDEKQGTIFTVDLPV 640
Cdd:COG5806   397 SEVGKGTTFTITLPL 411
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
711-822 7.45e-11

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: 60.30  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLTA 789
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSvGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLA--RGSNIPIIFITG 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:cd17537    81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIE 113
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
55-244 7.90e-11

ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 63.82  E-value: 7.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISAneAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAyIGADNYEIGR 134
Cdd:cd06280    29 GYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAP--SAGPSRELKRLLKHGIPIVLIDREVEGLELDL-VAGDNREGAY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 -AVGNYIASSLKgkgNVVELTGLGGSTPAMERHQGFMAAISNY---PDIKLIDKADAAweREPAEVEMDSMLRRHPKIDA 210
Cdd:cd06280   106 kAVKHLIELGHR---RIGLITGPLEISTTRERLAGYREALAEAgipVDESLIFEGDST--IEGGYEAVKALLDLPPRPTA 180
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2594348833 211 VYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd06280   181 IFATNNLMAVGALRALRERGLEipQDISVVGFDDSD 216
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
44-244 1.24e-10

ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 63.07  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  44 DEILREAmFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAApmTPIVEEAYQKGIPVILVDRKILSDKYTA 123
Cdd:cd06299    19 SGIEDEA-RAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGEN--SEGLQALIAQGLPVVFVDREVEGLGGVP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 124 YIGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGF---MAAISNYPDIKLIDKADAawEREPAEVEMDS 200
Cdd:cd06299    96 VVTSDNRPGAREAVEYLVS--LGHRRIGYISGPLSTSTGRERLAAFraaLTAAGIPIDEELVAFGDF--RQDSGAAAAHR 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 201 MLRRHPKIDAVYAHNDRIAPGAYQAAKKAG-RE-KEMIFVGIDALP 244
Cdd:cd06299   172 LLSRGDPPTALIAGDSLMALGAIQALRELGlRIgDDVSLISFDDVP 217
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
711-824 1.36e-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: 62.89  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNAD----IRLYVHglLHTDYTVIEAA-DGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVI 785
Cdd:TIGR02875   5 IVIADDNKEfcnlLKEYLA--AQPDMEVVGVAhNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARPRVI 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2594348833 786 LLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNL 824
Cdd:TIGR02875  83 MLSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQL 121
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
542-639 1.37e-10

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


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 59.22  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 542 LLSNAFKFTPENGKVTVRlsSLTKDDHCWIRftVANTGSMISAEHIRNIFDRFYK-IDMHHAG--SGIGLALVKAFVE-- 616
Cdd:cd16948    13 IVSNALKYSKQGGKIEIY--SETNEQGVVLS--IKDFGIGIPEEDLPRVFDKGFTgENGRNFQesTGMGLYLVKKLCDkl 88
                          90       100
                  ....*....|....*....|...
gi 2594348833 617 LHKgtITVESDEKQGTIFTVDLP 639
Cdd:cd16948    89 GHK--IDVESEVGEGTTFTITFP 109
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
54-299 1.46e-10

periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 63.46  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  54 DGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAApMTP-IVEEAYQKGIPVILVDRKILSDKYTA---YIGADN 129
Cdd:cd01540    28 LGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQK-LGPaIAAKAKAAGIPVIAVDDQLVDADPMKivpFVGIDA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 130 YEIGRAVGNYIASSLKGKG-------NVVELTGLGGSTpAMERHQGFMAAI--SNYPDIKLIDKADAAWEREPAEVEMDS 200
Cdd:cd01540   107 YKIGEAVGEWLAKEMKKRGwddvkevGVLAITMDTLSV-CVDRTDGAKDALkaAGFPEDQIFQAPYKGTDTEGAFNAANA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 201 MLRRHPKID--AVYAHNDRIAPGAYQAAKKAGREKE-MIFVGIDALPGKGNGLELVLDNVLDATFIYPTN-GDKVMQLAM 276
Cdd:cd01540   186 VITAHPEVKhwLVVGCNDEGVLGAVRALEQAGFDAEdIIGVGIGGYLAADEEFKKQPTGFKASLYISPDKhGYIAAEELY 265
                         250       260
                  ....*....|....*....|....
gi 2594348833 277 N-ILEKKSYPRETVMNTAVVDRTN 299
Cdd:cd01540   266 NwITDGKPPPAETLTDGVIVTRDN 289
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
711-829 1.53e-10

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: 59.63  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPvILLTAC 790
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLP-ILAVAD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2594348833 791 SLDEQR-IQGYDGGADSYISKPFSSQLLLARVRNLIDSHR 829
Cdd:cd17539    80 PGDRGRlIRALEIGVNDYLVRPIDPNELLARVRTQIRRKR 119
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
417-483 2.02e-10

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 57.19  E-value: 2.02e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2594348833  417 AKLVFFTNISHDFRTPLTLVADPVEhLLADSSLSEDQRRMLLLVQRNVNILLRLVNQILDFRKYENG 483
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLE-LLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
55-244 2.14e-10

periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 62.55  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIIsaneaAP---MTPIVEEAYQKGIPVILVDRKIlSDKYTAYIGADNYE 131
Cdd:cd19977    29 GYHVILCNTDEDPEKEKKYIEMLRAKQVDGIII-----APtggNEDLIEKLVKSGIPVVFVDRYI-PGLDVDTVVVDNFK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 132 IGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISNYpDIKLIDKADAAWEREP-AEVEMDSMLRRHPKIDA 210
Cdd:cd19977   103 GAYQATEHLIE--LGHKRIAFITYPLELSTRQERLEGYKAALADH-GLPVDEELIKHVDRQDdVRKAISELLKLEKPPDA 179
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2594348833 211 VYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd19977   180 IFAANNLITLEVLKAIKELGLRipDDIALIGFDDIP 215
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
711-812 2.25e-10

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: 58.51  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRK-AMKYVPDLIISDVMMPG-MDGIECCRRLKSelQTCHIPVILL 787
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDlGYTVLEAASGDEALDLlESGPDIDLLVTDVIMPGgMNGSQLAEEARR--RRPDLKVLLT 78
                          90       100
                  ....*....|....*....|....*.
gi 2594348833 788 TAcsLDEQRIQGYDGGAD-SYISKPF 812
Cdd:cd18161    79 SG--YAENAIEGGDLAPGvDVLSKPF 102
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
711-812 2.43e-10

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 58.72  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTA 789
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEgYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDEN--IRVIIMTA 80
                          90       100
                  ....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPF 812
Cdd:cd17553    81 YGELDMIQESKELGALTHFAKPF 103
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
711-811 2.59e-10

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 58.15  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADI-RLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTA 789
Cdd:cd17602     1 VACVDDRPSIqKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                          90       100
                  ....*....|....*....|..
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKP 811
Cdd:cd17602    81 KDGLVDRIRAKMAGASGYLTKP 102
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
45-230 2.82e-10

ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 62.27  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  45 EILR---EAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVD-LLIISANEAAPMTPIVEEayQKGIPVILVDRKILSDK 120
Cdd:cd06275    16 EVVRgveDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDgLLLMCSEMTDDDAELLAA--LRSIPVVVLDREIAGDN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 121 yTAYIGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISNyPDIKLIDK--ADAAWEREPAEVEM 198
Cdd:cd06275    94 -ADAVLDDSFQGGYLATRHLIE--LGHRRIGCITGPLEHSVSRERLAGFRRALAE-AGIEVPPSwiVEGDFEPEGGYEAM 169
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2594348833 199 DSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd06275   170 QRLLSQPPRPTAVFACNDMMALGALRAAQEQG 201
pleD PRK09581
response regulator PleD; Reviewed
711-822 3.17e-10

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 63.38  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLTAC 790
Cdd:PRK09581  158 ILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLVDE 237
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2594348833 791 SLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:PRK09581  238 DDDPRLVKALELGVNDYLMRPIDKNELLARVR 269
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
55-242 3.42e-10

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 62.45  E-value: 3.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIGR 134
Cdd:PRK10355   55 GAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 AVGNYIASSlKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPD---IKLI-DKADAAWEREPAEVEMDSMLRRHP-KID 209
Cdd:PRK10355  135 LQAKALVDK-VPQGNYFLMGGSPVDNNAKLFRAGQMKVLKPYIDsgkIKVVgDQWVDGWLPENALKIMENALTANNnKID 213
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2594348833 210 AVYAHNDRIAPGAYQAAKKAGREKEMIFVGIDA 242
Cdd:PRK10355  214 AVVASNDATAGGAIQALSAQGLSGKVAISGQDA 246
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-639 3.62e-10

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: 57.72  E-value: 3.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTPEngkvTVRLSSLTKDDHcwIRFTVANTGSMISAEHIRNIFDRFYKIDMHH----AGSGIGLAL 610
Cdd:cd16949     1 LARALENVLRNALRYSPS----KILLDISQDGDQ--WTITITDDGPGVPEDQLEQIFLPFYRVDSARdresGGTGLGLAI 74
                          90       100
                  ....*....|....*....|....*....
gi 2594348833 611 VKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16949    75 AERAIEQHGGKIKASNRKPGGLRVRIWLP 103
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
873-951 4.83e-10

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 61.62  E-value: 4.83e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 873 EDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPTDL 951
Cdd:PRK13503  191 EALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDI 269
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
709-823 5.23e-10

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 57.80  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 709 PCVLIIDDNADIRLYVHGLLH-TDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILL 787
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRrEGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRE--RYPDTVRILL 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2594348833 788 TACSlDEQRIQGY--DGGADSYISKPFSSQLLLARVRN 823
Cdd:cd17569    79 TGYA-DLDAAIEAinEGEIYRFLTKPWDDEELKETIRQ 115
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-639 5.36e-10

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 57.46  E-value: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFtpenGKVTVRLSSLTkdDHCWIRFTVANTGSMISAEHIRNIFDRFYKIDMHH--AGSGIGLALVK 612
Cdd:cd16950     1 LKRVLSNLVDNALRY----GGGWVEVSSDG--EGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARgtSGTGLGLAIVQ 74
                          90       100
                  ....*....|....*....|....*..
gi 2594348833 613 AFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16950    75 RISDAHGGSLTLANRAGGGLCARIELP 101
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
69-211 5.70e-10

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 61.89  E-value: 5.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  69 KQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEaYQKGIPVILVDRKILSDKYTAYIGADNYEIGRAVGNYIA---SSLK 145
Cdd:PRK10936   92 KQQQQLEQCVAWGADAILLGAVTPDGLNPDLEL-QAANIPVIALVNGIDSPQVTTRVGVSWYQMGYQAGRYLAqwhPKGS 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 146 GKGNVVELTG---LGGSTPAmerHQGFMAAISNyPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAV 211
Cdd:PRK10936  171 KPLNVALLPGpegAGGSKAV---EQGFRAAIAG-SDVRIVDIAYGDNDKELQRNLLQELLERHPDIDYI 235
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
752-822 6.33e-10

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 60.42  E-value: 6.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 752 PDLIISDVMMPGMDGIECCRRLKSELQTchiPVILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:PRK10701   46 PDLVLLDIMLPGKDGMTICRDLRPKWQG---PIVLLTSLDSDMNHILALEMGACDYILKTTPPAVLLARLR 113
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
55-230 7.18e-10

ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 61.03  E-value: 7.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLII----SANEAaPMTPIVEEAYQKGIPVILVDRKILSDKYtAYIGADNY 130
Cdd:cd01541    29 GYSLLLALTNNDVEKEREILESLLDQNVDGLIIeptkSALPN-PNLDLYEELQKKGIPVVFINSYYPELDA-PSVSLDDE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 131 EIGRAVGNYiassLKGKGNvvelTGLGG-----STPAMERHQGFMAAISNY------PDIKLIDKADAAwEREPAEvEMD 199
Cdd:cd01541   107 KGGYLATKH----LIDLGH----RRIAGifksdDLQGVERYQGFIKALREAglpiddDRILWYSTEDLE-DRFFAE-ELR 176
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2594348833 200 SMLRRHPKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd01541   177 EFLRRLSRCTAIVCYNDEIALRLIQALREAG 207
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
711-833 7.69e-10

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 62.17  E-value: 7.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD-YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLTA 789
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQgFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRS--HETRTPVILMTA 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPF---SSQLLLAR---VRNLIDSHRRLKQ 833
Cdd:PRK11361   85 YAEVETAVEALRCGAFDYVIKPFdldELNLIVQRalqLQSMKKEIRHLHQ 134
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
509-641 7.91e-10

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 62.62  E-value: 7.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 509 ARKKHIHFSFD---YMPDTDYRTLadVEKLERIYFNLLSNAFKFTP--ENGKVTVRLSSLtkddHCWIRFTVANTGSMIS 583
Cdd:PRK11086  407 ARELGITLIISedsQLPDSGDEDQ--VHELITILGNLIENALEAVGgeEGGEISVSLHYR----NGWLHCEVSDDGPGIA 480
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 584 AEHIRNIFDRFY--KIDmhhaGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:PRK11086  481 PDEIDAIFDKGYstKGS----NRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIPWD 536
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
706-822 8.53e-10

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 58.77  E-value: 8.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 706 SSKPCVLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKsELQtCHIPV 784
Cdd:COG4567     2 AEDRSLLLVDDDEAFARVLARALERrGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALR-ERD-PDARI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2594348833 785 ILLTacsldeqriqGYDG----------GADSYISKPFSSQLLLARVR 822
Cdd:COG4567    80 VVLT----------GYASiataveaiklGADDYLAKPADADDLLAALE 117
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
55-245 1.40e-09

ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380488 [Multi-domain]  Cd Length: 265  Bit Score: 59.90  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAED-VHYFIDKGVDLLIIsaneAAPMTPIVEEAYQ--KGIPVILVDRKILSDkyTAYIGADNYE 131
Cdd:cd01574    29 GYSVSIATVDEDDPASVREaLDRLLSQRVDGIIV----IAPDEAVLEALRRlpPGLPVVIVGSGPSPG--VPTVSIDQEE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 132 IGRAVGNYIASSlkGKGNVVELTGLGGSTPAMERHQGFMAAISNYP-DIKLIDKADaaWEREPAEVEMDSMLRRHPkIDA 210
Cdd:cd01574   103 GARLATRHLLEL--GHRRIAHIAGPLDWVDARARLRGWREALEEAGlPPPPVVEGD--WSAASGYRAGRRLLDDGP-VTA 177
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2594348833 211 VYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALPG 245
Cdd:cd01574   178 VFAANDQMALGALRALHERGLRvpEDVSVVGFDDIPE 214
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
713-811 1.52e-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: 56.13  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 713 IIDDNADIRLYVHGLLHTDY--TVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLTA 789
Cdd:cd17565     3 IVDDDKNIIKILSDIIEDDDlgEVVgEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKD--TGSNGKFIMISQ 80
                          90       100
                  ....*....|....*....|..
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKP 811
Cdd:cd17565    81 VSDKEMIGKAYQAGIEFFINKP 102
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
44-230 1.92e-09

ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380631 [Multi-domain]  Cd Length: 268  Bit Score: 59.57  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  44 DEILREAmfydGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIIsaneaAPMTPIVEEAYQ----KGIPVILVDRKIlSD 119
Cdd:cd19976    22 EDTLNEL----GYNIILCNTYNDFEREKKYIQELKERNVDGIII-----ASSNISDEAIIKllkeEKIPVVVLDRYI-ED 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 120 KYTAYIGADNYEigravGNYIASSL---KGKGNVVELTGLGGSTPAMERHQGFMAAI--SNYPdiklIDKAD---AAWER 191
Cdd:cd19976    92 NDSDSVGVDDYR-----GGYEATKYlieLGHTRIGCIVGPPSTYNEHERIEGYKNALqdHNLP----IDESWiysGESSL 162
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2594348833 192 EPAEVEMDSMLRRHPkIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd19976   163 EGGYKAAEELLKSKN-PTAIFAGNDLIAMGVYRAALELG 200
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
711-823 1.96e-09

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 56.13  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGL--LHTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIpVILL 787
Cdd:cd19930     1 VLIAEDQEMVRGALAALleLEDDLEVVaQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKV-LIVT 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 788 TACSLDEQRiQGYDGGADSYISKPFSSQLLLARVRN 823
Cdd:cd19930    80 TFGRPGYFR-RALAAGVDGYVLKDRPIEELADAIRT 114
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
421-479 2.75e-09

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: 54.14  E-value: 2.75e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 421 FFTNISHDFRTPLTLVADPVEHLLADSSLSEDQRRMLLLVQRNVNILLRLVNQILDFRK 479
Cdd:cd00082     7 FLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
711-812 4.63e-09

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: 54.82  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLY-VHGLLHTDYTVIEAADGSEGIRKAMKYVP-DLIISDVMMPGMDGIECCRRLKsELQTcHIPVILLT 788
Cdd:cd18160     2 ILLADDEPSVRKFiVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREAR-KIDP-DVKILFIS 79
                          90       100
                  ....*....|....*....|....
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPF 812
Cdd:cd18160    80 GGAAAAPELLSDAVGDNATLKKPF 103
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
711-833 4.75e-09

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 59.88  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVH-GLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTA 789
Cdd:PRK10923    6 VWVVDDDSSIRWVLErALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTA 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQ 833
Cdd:PRK10923   84 HSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQ 127
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
508-636 5.59e-09

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 55.33  E-value: 5.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 508 VARKKHIHFSFDYMPDTdyRTLADVEKLERIYFNLLSNAFKFTPENgkvtVRLSSLTKDDHcwIRFTVANTGSMISAEHI 587
Cdd:cd16954    13 VYQRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCLEF----VEVTARQTDGG--LHLIVDDDGPGVPESQR 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2594348833 588 RNIFDRFYKIDMHHAGSGIGLALVKAFVELHKGTITVESDEKQGTIFTV 636
Cdd:cd16954    85 SKIFQRGQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEV 133
PRK10336 PRK10336
two-component system response regulator QseB;
711-825 5.89e-09

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 57.21  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVH-GLLHTDYTVIEAADGSEGiRKAMKYVP-DLIISDVMMPGMDGIECCRRLKSELQtcHIPVILLT 788
Cdd:PRK10336    3 ILLIEDDMLIGDGIKtGLSKMGFSVDWFTQGRQG-KEALYSAPyDAVILDLTLPGMDGRDILREWREKGQ--REPVLILT 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:PRK10336   80 ARDALAERVEGLRLGADDYLCKPFALIEVAARLEALM 116
envZ PRK09467
osmolarity sensor protein; Provisional
425-640 7.07e-09

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 59.15  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 425 ISHDFRTPLT---LVAD---PVEHLLADSsLSEDQRRMlllvqrNVNIllrlvNQILDFRKYENgKMEYTPISLDILSsf 498
Cdd:PRK09467  236 VSHDLRTPLTrirLATEmmsEEDGYLAES-INKDIEEC------NAII-----EQFIDYLRTGQ-EMPMEMADLNALL-- 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 499 egwNESFMAVA-RKKHIHFSF-DYMPDTDYRTLAdvekLERIYFNLLSNAFKFTpeNGKVTVRlsslTKDDHCWIRFTVA 576
Cdd:PRK09467  301 ---GEVIAAESgYEREIETALqPGPIEVPMNPIA----IKRALANLVVNAARYG--NGWIKVS----SGTEGKRAWFQVE 367
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833 577 NTGSMISAEHIRNIFDRFYKIDMHHA--GSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:PRK09467  368 DDGPGIPPEQLKHLFQPFTRGDSARGssGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPL 433
PRK10816 PRK10816
two-component system response regulator PhoP;
711-825 1.06e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 56.67  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR--LYVHgLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLT 788
Cdd:PRK10816    3 VLVVEDNALLRhhLKVQ-LQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVLT 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLI 825
Cdd:PRK10816   80 ARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALM 116
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-640 1.09e-08

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: 53.59  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTpengKVTVRLSSLTKDDhcWIRFTVANTGSMISAEHIRNIFDRFYKID----MHHAGSGIGLAL 610
Cdd:cd16939     1 MARALDNLLRNALRYA----HRTVRIALLVSGG--RLTLIVEDDGPGIPAAARERVFEPFVRLDpsrdRATGGFGLGLAI 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 2594348833 611 VKAFVELHKGTITVESDEKQGTIFTVDLPV 640
Cdd:cd16939    75 VHRVALWHGGHVECDDSELGGACFRLTWPR 104
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
711-812 1.47e-08

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 53.38  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADI--RLYVHGLLHTDYTVIEAA-DGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILL 787
Cdd:cd17561     4 VLIADDNREFvqLLEEYLNSQPDMEVVGVAhNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIML 83
                          90       100
                  ....*....|....*....|....*
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPF 812
Cdd:cd17561    84 TAFGQEDITQRAVELGASYYILKPF 108
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-638 1.56e-08

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 53.23  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFKFTPENGKVTVRLSSLTKDDHCWIRftVANTGSMISAEHIRNIFDRFYKIDMHHAGSGIGLALVKAF 614
Cdd:cd16976     1 IQQVLMNLLQNALDAMGKVENPRIRIAARRLGGRLVLV--VRDNGPGIAEEHLSRVFDPFFTTKPVGKGTGLGLSISYGI 78
                          90       100
                  ....*....|....*....|....
gi 2594348833 615 VELHKGTITVESDEKQGTIFTVDL 638
Cdd:cd16976    79 VEEHGGRLSVANEEGAGARFTFDL 102
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
711-822 1.91e-08

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 55.63  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTD--YTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIpvILL 787
Cdd:PRK10403    9 VLIVDDHPLMRRGVRQLLELDpgFEVVaEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQI--IIL 86
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:PRK10403   87 TVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIR 121
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
78-231 3.90e-08

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 56.26  E-value: 3.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  78 IDKGVDLLIIsANEAAPMTPIVEEAYQKGIPVILVDR-KILSDkyTAYIGADNYEIGRAVGNYIASslKGKGNVVELTGL 156
Cdd:PRK10014  117 LNQGVDGVVI-AGAAGSSDDLREMAEEKGIPVVFASRaSYLDD--VDTVRPDNMQAAQLLTEHLIR--NGHQRIAWLGGQ 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 157 GGSTPAMERHQGFMAAISNYpdiKLIDKAD-----AAWEREPAEVeMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGR 231
Cdd:PRK10014  192 SSSLTRAERVGGYCATLLKF---GLPFHSEwvlecTSSQKQAAEA-ITALLRHNPTISAVVCYNETIAMGAWFGLLRAGR 267
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
55-230 4.33e-08

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 55.31  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  55 GVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISAneaAPMTPIVEEAYQKGIPVILVDRKILSDKYtAYIGADNYEIGR 134
Cdd:cd06290    29 GYTLIVSTSHWNADRELEILRLLLARKVDGIIVVG---GFGDEELLKLLAEGIPVVLVDRELEGLNL-PVVNVDNEQGGY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 135 AVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISNYP---DIKLIDKADaaWEREPAEVEMDSMLRRHPKIDAV 211
Cdd:cd06290   105 NATNHLID--LGHRRIVHISGPEDHPDAQERYAGYRRALEDAGlevDPRLIVEGD--FTEESGYEAMKKLLKRGGPFTAI 180
                         170
                  ....*....|....*....
gi 2594348833 212 YAHNDRIAPGAYQAAKKAG 230
Cdd:cd06290   181 FAANDLMALGAMKALREAG 199
PRK13856 PRK13856
two-component response regulator VirG; Provisional
711-822 4.84e-08

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 54.82  E-value: 4.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSElqtCHIPVILLTA 789
Cdd:PRK13856    4 VLVIDDDVAMRhLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATK---SDVPIIIISG 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2594348833 790 CSLDE-QRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:PRK13856   81 DRLEEaDKVVALELGATDFIAKPFGTREFLARIR 114
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
44-291 4.94e-08

ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 55.19  E-value: 4.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  44 DEILREAmfydGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEaapMTPIVEEAYQK-GIPVILVDRKilsDKYT 122
Cdd:cd01542    22 DEVLKEN----GYQPLIANTNLDEEREIEYLETLARQKVDGIILFATE---ITDEHRKALKKlKIPVVVLGQE---HEGF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 123 AYIGADNYEIGRAVGNYIASslKGKGNVVELtGLGGSTPAM--ERHQGFMAAISNYPDIK-LIDKADAAWERepAEVEMD 199
Cdd:cd01542    92 SCVYHDDYGAGKLLGEYLLK--KGHKNIAYI-GVDEEDIAVgvARKQGYLDALKEHGIDEvEIVETDFSMES--GYEAAK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 200 SMLRRHpKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDalpgkgnglelvlDNVLdATFIYP----------TN 267
Cdd:cd01542   167 ELLKEN-KPDAIICATDNIALGAIKALRELGIKipEDISVAGFG-------------GYDL-SEFVSPslttvkfdyeEA 231
                         250       260
                  ....*....|....*....|....
gi 2594348833 268 GDKVMQLAMNILEKKSYPRETVMN 291
Cdd:cd01542   232 GEKAAELLLDMIEGEKVPKKQKLP 255
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
44-230 5.58e-08

ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380506 [Multi-domain]  Cd Length: 266  Bit Score: 55.25  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  44 DEILREAmfydGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPMTPIVEEayQKGIPVILVDRKILSDKYtA 123
Cdd:cd06283    22 EDVCREA----GYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELA--QKGLPVVLVDRQIEPLNW-D 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 124 YIGADNYEIGRAVGNYIASslKGKGNVVELTG-LGGSTPAMERHQGFMAAISNY-PDIKLI---DKADAAWEREPAEVEM 198
Cdd:cd06283    95 TVVTDNYDATYEATEHLKE--QGYERIVFVTEpIKGISTRRERLQGFLDALARYnIEGDVYvieIEDTEDLQQALAAFLS 172
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2594348833 199 DSmlrrHPKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd06283   173 QH----DGGKTAIFAANGVVLLRVLRALKALG 200
fixJ PRK09390
response regulator FixJ; Provisional
706-830 5.95e-08

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 53.85  E-value: 5.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 706 SSKPCVLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPV 784
Cdd:PRK09390    1 SDKGVVHVVDDDEAMRDSLAFLLDSaGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSP--LPV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 785 ILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRR 830
Cdd:PRK09390   79 IVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPE 124
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
711-833 6.13e-08

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: 52.41  E-value: 6.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILLT 788
Cdd:cd17575     3 VLLVDDQAIIGEAVRRALadEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVLS 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKPFSSQLLLARVRNLIDSHRRLKQ 833
Cdd:cd17575    83 TKEEPEVKSEAFALGANDYLVKLPDKIELVARIRYHSRSYINLLQ 127
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
711-812 7.70e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 55.81  E-value: 7.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSelQTCHIPVILLTA 789
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKA--LNPAIPVLIMTA 85
                          90       100
                  ....*....|....*....|...
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKPF 812
Cdd:PRK10365   86 YSSVETAVEALKTGALDYLIKPL 108
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
542-642 7.91e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 55.79  E-value: 7.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 542 LLSNAFK--FTPENGKVTVRLSSLTKDDhcWIRFTVANTGSMISAEHIRNIFDRFykiDMHHAGSGIGLALVKAFVELH- 618
Cdd:COG2972   344 LVENAIEhgIEPKEGGGTIRISIRKEGD--RLVITVEDNGVGMPEEKLEKLLEEL---SSKGEGRGIGLRNVRERLKLYy 418
                          90       100
                  ....*....|....*....|....*.
gi 2594348833 619 --KGTITVESDEKQGTIFTVDLPVQT 642
Cdd:COG2972   419 geEYGLEIESEPGEGTTVTIRIPLEE 444
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
44-230 8.91e-08

ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 54.45  E-value: 8.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  44 DEILREAmfydGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANeaAPMTPIVEEAYQKGIPVILVDRKI--LSDKY 121
Cdd:cd06270    22 ERVARAH----GKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSR--ALSDEELILIAEKIPPLVVINRYIpgLADRC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 122 tayIGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISNY---PDIKLIDKADaaWEREPAEVEM 198
Cdd:cd06270    96 ---VWLDNEQGGRLAAEHLLD--LGHRRIACITGPLDIPDARERLAGYRDALAEAgipLDPSLIIEGD--FTIEGGYAAA 168
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2594348833 199 DSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd06270   169 KQLLARGLPFTALFAYNDDMAIGALAALHEAG 200
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
711-819 9.54e-08

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 51.67  E-value: 9.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLH--TDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKseLQTCHIPVILLT 788
Cdd:cd17530     3 VLVLDDDPFQCMMAATILEdlGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLA--ESHSNAAVILMS 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2594348833 789 AcsLDEQRIQGYDGGADSY-------ISKPFSSQLLLA 819
Cdd:cd17530    81 G--LDGGILESAETLAGANglnllgtLSKPFSPEELTE 116
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
856-954 1.34e-07

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 54.27  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 856 KFKALIEAKMGDSNLNVEDLGKDMGLSRVQLYRkIKSLTNYSPNELLRIARLKKAASLL--ASSDMTVAEIGYEVGFSSP 933
Cdd:PRK09685  201 KVVALIDQSIQEEILRPEWIAGELGISVRSLYR-LFAEQGLVVAQYIRNRRLDRCADDLrpAADDEKITSIAYKWGFSDS 279
                          90       100
                  ....*....|....*....|.
gi 2594348833 934 SYFTKCYREQFGESPTDLLKR 954
Cdd:PRK09685  280 SHFSTAFKQRFGVSPGEYRRK 300
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
709-831 1.63e-07

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 51.21  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 709 PCVLIIDDNADIRLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchiPV-ILL 787
Cdd:cd17596     1 PTILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPE---VVrIII 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 788 TACSLDEQRIQGY-DGGADSYISKPF-SSQLLL-----ARVRNLIDSHRRL 831
Cdd:cd17596    78 SGYTDSEDIIAGInEAGIYQYLTKPWhPDQLLLtvrnaARLFELQRENERL 128
PRK15369 PRK15369
two component system response regulator;
711-819 2.66e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 52.39  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVIEAA-DGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIpvILL 787
Cdd:PRK15369    6 ILLVDDHELIINGIKNMLapYPRYKIVGQVdNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNI--LVL 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2594348833 788 TACSLDEQRIQGYDGGADSYISKPFSSQLLLA 819
Cdd:PRK15369   84 TARQEEHMASRTLAAGALGYVLKKSPQQILLA 115
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
711-824 2.94e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 53.73  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLkseLQTCHIPVILL 787
Cdd:PRK12555    3 IGIVNDSPLAVEALRRALarDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRI---MAERPCPILIV 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2594348833 788 TACSLD--EQRIQGYDGGADSYISKPF---------SSQLLLARVRNL 824
Cdd:PRK12555   80 TSLTERnaSRVFEAMGAGALDAVDTPTlgigagleeYAAELLAKIDQI 127
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
711-821 3.94e-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: 49.35  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR------LYVHGLlHTDytVIEAADGSEGIRKAMKYvpDLIISDVMMPGMDGIECCRRLKSelQTCHIPV 784
Cdd:cd17573     1 ILLIEDDSTLGkeiskgLNEKGY-QAD--VAESLKDGEYYIDIRNY--DLVLVSDKLPDGNGLSIVSRIKE--KHPSIVV 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 785 ILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARV 821
Cdd:cd17573    74 IVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
125-230 7.54e-07

ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 51.73  E-value: 7.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 125 IGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTP-AMERHQGFMAAIS--NYPDIKLIDKADAAWEREPAEVeMDSM 201
Cdd:cd01575    96 VGFSNFAAGRAMARHLIE--RGYRRIAFVGARLDGDSrARQRLEGFRDALAeaGLPLPLVLLVELPSSFALGREA-LAEL 172
                          90       100
                  ....*....|....*....|....*....
gi 2594348833 202 LRRHPKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd01575   173 LARHPDLDAIFCSNDDLALGALFECQRRG 201
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
78-233 8.24e-07

rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380655  Cd Length: 298  Bit Score: 51.87  E-value: 8.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  78 IDKGVDLLIISANEAAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIG-ADNYEIGRAVGNYIASSLKGKGNVVELtgl 156
Cdd:cd20000    53 IQQGVDAIAISANDPDALAPALKKARAAGIKVVTFDSDVAPEARDLFVNqADADGIGRAQVDMMAELIGGEGEFAIL--- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 157 gGSTPAMERHQGFMAAI------SNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVyahndrIAPG--AYQAAKK 228
Cdd:cd20000   130 -SATPTATNQNAWIDAMkkelasPEYAGMKLVKVAYGDDDAQKSYQEAEALLQAYPDLKGI------IAPTtvGIAAAAR 202

                  ....*
gi 2594348833 229 AGREK 233
Cdd:cd20000   203 ALEDS 207
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
49-244 8.76e-07

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 51.50  E-value: 8.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  49 EAMFYDGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAAPmtPIVEEAYQKGIPVILVDRKILSDKYTAyIGAD 128
Cdd:cd06293    23 DAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDL--SHLARLRARGTAVVLLDRPAPGPAGCS-VSVD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 129 NYEIGR-AVGNYIAsslKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPdiklIDKADAAWE--REPAEVE-----MDS 200
Cdd:cd06293   100 DVQGGAlAVDHLLE---LGHRRIAFVSGPLRTRQVAERLAGARAAVAEAG----LDPDEVVRElsAPDANAElgraaAAQ 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2594348833 201 MLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd06293   173 LLAMPPRPTAVFAANDLLALGLLAGLRRAGLRvpDDVSVVGYDDLP 218
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
872-952 1.17e-06

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 51.22  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 872 VEDLGKDMGLSRVQLYRKIKSlTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPTDL 951
Cdd:PRK15186  200 LKDISDSLYMSCSTLKRKLKQ-ENTSFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278

                  .
gi 2594348833 952 L 952
Cdd:PRK15186  279 L 279
PRK15115 PRK15115
response regulator GlrR; Provisional
711-811 1.28e-06

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 52.15  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIEccrrLKSELQTCH--IPVILLT 788
Cdd:PRK15115    9 LLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQ----LFAEIQKVQpgMPVIILT 84
                          90       100
                  ....*....|....*....|...
gi 2594348833 789 ACSLDEQRIQGYDGGADSYISKP 811
Cdd:PRK15115   85 AHGSIPDAVAATQQGVFSFLTKP 107
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
711-813 2.34e-06

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: 47.24  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIEAADGSEG---IRKAMKYVpDLIISDVMMPGMDGIECCRRLKSElqtCHIPVIL 786
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRcGYQVTTCTDAEEAlsmLRENKDEF-DLVITDVHMPDMDGFEFLELIRLE---MDLPVIM 76
                          90       100
                  ....*....|....*....|....*..
gi 2594348833 787 LTACSLDEQRIQGYDGGADSYISKPFS 813
Cdd:cd17584    77 MSADGSTSTVMKGLAHGACDYLLKPVS 103
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
123-241 2.63e-06

ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 49.84  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 123 AYIGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAA-----ISNYPDIKL-----IDKADAAwere 192
Cdd:cd06284    93 PSVSIDNEAAAYDATEYLIS--LGHRRIAHINGPLDNVYARERLEGYRRAlaeagLPVDEDLIIegdfsFEAGYAA---- 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 193 paeveMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGID 241
Cdd:cd06284   167 -----ARALLALPERPTAIFCASDELAIGAIKALRRAGLRvpEDVSVIGFD 212
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
401-641 2.77e-06

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 51.47  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 401 RDQ----LI----QLSHQL-EEATHAKLVFFTNISHDFRTPLTLVADPVEHLLADSSLSEDQRRMLLLVQRNvNILLRLV 471
Cdd:PRK10618  424 RDQdrevLVnkklQQAQREyEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQS-DVLVRLV 502
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 472 NQILDFRKYENG--KMEYTPISL-----DILSsfegwnESFMAVARKK---HIHFSFDymPDTDYRtlADVEKLERIYFN 541
Cdd:PRK10618  503 DNIQLLNMLETQdwKPEQELFSLqdlidEVLP------EVLPAIKRKGlqlLIHNHLK--AEQLRI--GDRDALRKILLL 572
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 542 LLSNAFKFTPEnGKVTVRLSSLTKDDHCwIRFTVANTGSMISAEHIRNI---------FDRFYKidmhhaGSGIGLALVK 612
Cdd:PRK10618  573 LLNYAITTTAY-GKITLEVDQDESSPDR-LTIRILDTGAGVSIKELDNLhfpflnqtqGDRYGK------ASGLTFFLCN 644
                         250       260
                  ....*....|....*....|....*....
gi 2594348833 613 AFVELHKGTITVESDEKQGTIFTVDLPVQ 641
Cdd:PRK10618  645 QLCRKLGGHLTIKSREGLGTRYSIHLKML 673
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
915-953 3.23e-06

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: 44.84  E-value: 3.23e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2594348833 915 ASSDMTVAEIGYEVGFSsPSYFTKCYREQFGESPTDLLK 953
Cdd:pfam00165   5 LSTNLTIADIADELGFS-RSYFSRLFKKYTGVTPSQYRH 42
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-639 4.87e-06

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 46.24  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 535 LERIYFNLLSNAFK-FTPENGKVTVR------LSSLTKDDHCWIRFTVANTGSMISAEHIRNIFDRFykIDMHHAGSGIG 607
Cdd:cd16918     1 LIQVFLNLVRNAAQaLAGSGGEIILRtrtqrqVTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPM--VSGRENGTGLG 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2594348833 608 LALVKAFVELHKGTITVESDEKQgTIFTVDLP 639
Cdd:cd16918    79 LAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
PRK10693 PRK10693
two-component system response regulator RssB;
736-791 5.14e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 49.60  E-value: 5.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833 736 EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTACS 791
Cdd:PRK10693    2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQ--TPVLVISATE 55
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
711-819 7.58e-06

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 45.90  E-value: 7.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIpvILLTa 789
Cdd:cd17563     3 LLLVDDDEVFAeRLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARI--VVLT- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2594348833 790 csldeqriqGYdG-----------GADSYISKPFSSQLLLA 819
Cdd:cd17563    80 ---------GY-AsiataveaiklGADDYLAKPADADEILA 110
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
711-819 7.87e-06

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: 45.99  E-value: 7.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTDY--TVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVIllt 788
Cdd:cd17593     3 VLICDDSSMARKQLARALPADWdvEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVV--- 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2594348833 789 acSLDEQ-----RIQGYdgGADSYISKPFSSQLLLA 819
Cdd:cd17593    80 --SGDVQpeakeRVLEL--GALAFLKKPFDPEKLAQ 111
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
712-810 8.14e-06

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 47.58  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 712 LIIDDNADIRLYVHGLLHT-DYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVIllta 789
Cdd:PRK09958    4 IIIDDHPLAIAAIRNLLIKnDIEILaELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIV---- 79
                          90       100
                  ....*....|....*....|....
gi 2594348833 790 cSLDEQRIQG---YDGGADSYISK 810
Cdd:PRK09958   80 -SAKNDHFYGkhcADAGANGFVSK 102
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
46-232 9.32e-06

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 48.43  E-value: 9.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  46 ILREAMFYdGVSVEIRSAADDNRKQAEDVHYFIDKGVDLLIISANEAApMTPIVEEAYQKGIPVILVDRKILSDKYtAYI 125
Cdd:cd06282    21 IQRAARAA-GYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQ-GSEALELLEEEGVPYVLLFNQTENSSH-PFV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 126 GADNYEIGRAVGNYIASslKGKGNVVELTG-LGGSTPAMERHQGFMAAIsNYPDIKLID--KADAAWEREPAEVEmdSML 202
Cdd:cd06282    98 SVDNRLASYDVAEYLIA--LGHRRIAMVAGdFSASDRARLRYQGYRDAL-KEAGLKPIPivEVDFPTNGLEEALT--SLL 172
                         170       180       190
                  ....*....|....*....|....*....|
gi 2594348833 203 RRHPKIDAVYAHNDRIAPGAYQAAKKAGRE 232
Cdd:cd06282   173 SGPNPPTALFCSNDLLALSVISALRRLGIR 202
PBP1_LuxPQ_Quorum_Sensing cd06303
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ...
124-261 1.16e-05

periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.


Pssm-ID: 380526 [Multi-domain]  Cd Length: 320  Bit Score: 48.52  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 124 YIGADNYEIGRAVGNYIASSLKGKGNVVELTGLGGSTPAMeRHQGFMAAISNYPDIKLIDKADAAWEREPAEVEMDSMLR 203
Cdd:cd06303   136 YVGFDHAEGSRMLAKHFIKIFPEEGKYAILYLTEGYVSDQ-RGDTFIDEVARHSNLELVSAYYTDFDRESAREAARALLA 214
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2594348833 204 RHPKIDAVYAHNDRIAPGAYQAAKKAGREKEMIfvgIDALPGKGNGLELVLDNVLDAT 261
Cdd:cd06303   215 RHPDLDFIYACSTDIALGAIDALQELGRETDIM---INGWGGGSAELDALQKGGLDVT 269
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
711-820 1.44e-05

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: 45.31  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDnaDIRLyvhGLLHTDY-------TVIEAADGSEGIRKAMK-YVPDLIISDVMMPGMDGIECCRRLKSelQTCHI 782
Cdd:cd19925     3 VLIVED--DPMV---AEIHRAYveqvpgfTVIGTAGTGEEALKLLKeRQPDLILLDIYLPDGNGLDLLRELRA--AGHDV 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2594348833 783 PVILLTACSlDEQRIQ-GYDGGADSYISKPFSSQLLLAR 820
Cdd:cd19925    76 DVIVVTAAN-DVETVReALRLGVVDYLIKPFTFERLRQR 113
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
66-244 1.60e-05

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 47.50  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  66 DNRKQAEDVHYFIDKGVDLLIISANEAAPmtpiveEAY----QKGIPVILV-----DRKILSdkytayIGADNYEIGRAV 136
Cdd:cd06273    40 DPARELEQVRALIERGVDGLILVGSDHDP------ELFelleQRQVPYVLTwsydeDSPHPS------IGFDNRAAAARA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 137 GNYIASSlkGKGNVVELTG-LGGSTPAMERHQGFMAAISNY----PDIKLIdkaDAAWEREPAEVEMDSMLRRHPKIDAV 211
Cdd:cd06273   108 AQHLLDL--GHRRIAVISGpTAGNDRARARLAGIRDALAERglelPEERVV---EAPYSIEEGREALRRLLARPPRPTAI 182
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2594348833 212 YAHNDRIAPGAYQAAKKAGRE--KEMIFVGIDALP 244
Cdd:cd06273   183 ICGNDVLALGALAECRRLGISvpEDLSITGFDDLE 217
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
542-641 1.82e-05

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 48.36  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 542 LLSNAFKF---TPENGKVTVrlsSLTKDDHcWIRFTVANTGSMISAEhirniFDRfykidmhHAGSGIGLALVKAFVELH 618
Cdd:COG3920   407 LVTNALKHaflSGEGGRIRV---SWRREDG-RLRLTVSDNGVGLPED-----VDP-------PARKGLGLRLIRALVRQL 470
                          90       100
                  ....*....|....*....|...
gi 2594348833 619 KGTITVESDEkqGTIFTVDLPVQ 641
Cdd:COG3920   471 GGTLELDRPE--GTRVRITFPLA 491
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
711-813 1.83e-05

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 44.70  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYTVIEAADGSEGIR----KAMKYvpDLIISDVMMPGMDGIECCRRLKSELQTCHIPVI 785
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLeKLGCEVTTVSSGEECLNllasAEHSF--QLVLLDLCMPEMDGFEVALRIRKLFGRRERPLI 80
                          90       100
                  ....*....|....*....|....*....
gi 2594348833 786 L-LTACSLDEQRIQGYDGGADSYISKPFS 813
Cdd:cd19933    81 VaLTANTDDSTREKCLSLGMNGVITKPVS 109
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
97-231 2.76e-05

ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380502 [Multi-domain]  Cd Length: 284  Bit Score: 47.20  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  97 PIVEEAYQKGIPVILVDRKILSDkyTAYIGADNYEIGRAVGNYiassLKGKG--NVVELT---GLGGSTPAM-------- 163
Cdd:cd06279    70 PAVAALRRRGLPLVVVDGPAPPG--IPSVGIDDRAAARAAARH----LLDLGhrRIAILSlrlDRGRERGPVsaerlaaa 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 164 ------ERHQGFMAAIsnyPDIKLIDKADAAWEREPAEVE-----MDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGR 231
Cdd:cd06279   144 tnsvarERLAGYRDAL---EEAGLDLDDVPVVEAPGNTEEagraaARALLALDPRPTAILCMSDVLALGALRAARERGL 219
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
711-811 3.70e-05

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: 44.28  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHTDYTVIEAAD---------GSEGIRKAMKYVP---DLIISDVMMPGMDGIECCRRLKSELQ 778
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDsgkraleflGLEDEEDSSNFNEpkvNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2594348833 779 TCHIPVILLTACSLdEQRI-QGYDGGADSYISKP 811
Cdd:cd17581    81 LKEIPVVIMSSENI-PTRIsRCLEEGAEDFLLKP 113
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
505-639 6.17e-05

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 46.75  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 505 FMAVARKKHIHFSFDYMPDTDYRTLA---DVEKLERIYFNLLSNAFKF---TPENGKVTVRLSSLTKDDhcwIRFTVANT 578
Cdd:PRK15053  400 FGKVQRARELGLKMVIVPGSQLSQLPpglDSTEFAAIVGNLLDNAFEAslrSDEGNKIVELFLSDEGDD---VVIEVADQ 476
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 579 GSMISAEHIRNIFDRFYKIDMHHAGS-GIGLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:PRK15053  477 GCGVPESLRDKIFEQGVSTRADEPGEhGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
162-244 7.21e-05

Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 45.62  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 162 AMERHQGFMAAISNYPDiklidKADAAWEREPAEVE------MDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--K 233
Cdd:cd20010   135 AHQRRDGYRAALAEAGL-----PVDPALVREGPLTEeggyqaARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSpgK 209
                          90
                  ....*....|.
gi 2594348833 234 EMIFVGIDALP 244
Cdd:cd20010   210 DVSVIGHDDLL 220
PRK11697 PRK11697
two-component system response regulator BtsR;
711-822 7.86e-05

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 45.22  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL--HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIEccrrLKSELQTCHIP-VIL 786
Cdd:PRK11697    4 VLIVDDEPLAREELRELLqeEGDIEIVgECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLE----LVGMLDPEHMPyIVF 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2594348833 787 LTAcsLDEQRIQGYDGGADSYISKPFSSQLL---LARVR 822
Cdd:PRK11697   80 VTA--FDEYAIKAFEEHAFDYLLKPIDPARLaktLARLR 116
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
97-230 9.40e-05

ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 45.27  E-value: 9.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  97 PIVEEAYQKGIPVILVDRKiLSDKYTAYIGADNYEIGRAVGNYIASslKGKGNVVELTGLGGSTPAMERHQGFMAAISny 176
Cdd:cd06294    74 PLIEYLKEEGFPFVVIGKP-LDDNDVLYVDNDNVQAGYEATEYLID--KGHKRIAFIGGDKNLVVSIDRLQGYKQALK-- 148
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2594348833 177 pDIKLIDKADAAW----EREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:cd06294   149 -EAGLPLDDDYILlldfSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELG 205
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
868-954 9.43e-05

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 45.35  E-value: 9.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 868 SNLNVEDLGKDMGLS--RV-QLYRKIKSLTNYSPNELLRIARLKKaasLLASSDMTVAEIGYEVGFSSPSYFTKCYREQF 944
Cdd:PRK10572  198 SEFDIESVAQHVCLSpsRLaHLFRQQLGISVLRWREDQRISRAKL---LLQTTRMPIATIGRNVGYDDQLYFSRVFKKCT 274
                          90
                  ....*....|
gi 2594348833 945 GESPTDLLKR 954
Cdd:PRK10572  275 GASPSEFRAR 284
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
98-241 9.46e-05

ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380486 [Multi-domain]  Cd Length: 269  Bit Score: 45.21  E-value: 9.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  98 IVEEAYQKGIPVILVDRKILSDKYTAyIGADNYEIGRAVGNYIASslKGKGNV-----VELTGLGGSTPAMERHQGFMAA 172
Cdd:cd01544    67 EIEKLKKLNPNIVFVDSNPDPDGFDS-VVPDFEQAVRQALDYLIE--LGHRRIgfiggKEYTSDDGEEIEDPRLRAFREY 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 173 ISNYPDIKLIDKADAAWEREPAEVEMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGRE--KEMIFVGID 241
Cdd:cd01544   144 MKEKGLYNEEYIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKvpEDISIISFN 214
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
531-639 1.11e-04

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 42.52  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 531 DVEKLERIYFNLLSNAFKFTPEN----GKVTVRLSSltkDDHCWIRFTVANTGSMISAEHIRNIFDRFykIDMHHAGSGI 606
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGRpsdvGEVRIRVEA---DQDGRIVLIVCDNGKGFPREMRHRATEPY--VTTRPKGTGL 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2594348833 607 GLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16944    76 GLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
711-811 1.29e-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: 42.11  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIR-LYVHGLLHTDYTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTchIPVILLTA 789
Cdd:cd19928     1 ILVADDDRAIRtVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPD--LPIIVMSA 78
                          90       100
                  ....*....|....*....|..
gi 2594348833 790 CSLDEQRIQGYDGGADSYISKP 811
Cdd:cd19928    79 QNTLMTAVKAAERGAFEYLPKP 100
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
357-415 1.59e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 357 KSLRSKNRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEAT 415
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
867-953 1.94e-04

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 44.60  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 867 DSNLNVEDLGKDMGLSRVQLYRKIKSL-TNYSpnELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFG 945
Cdd:PRK15185  220 SRQWKLTDVADHIFMSTSTLKRKLAEEgTSFS--DIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFK 297

                  ....*...
gi 2594348833 946 ESPTDLLK 953
Cdd:PRK15185  298 TTPSTFIK 305
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
709-821 2.31e-04

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


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 41.85  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 709 PCVLIIDDNADIRLYVHGLL-HTDYTVI-EAADGSEGIRKAMKYVPDLIISDVMMP-GMDGIECCRRLkseLQTCHIPVI 785
Cdd:cd17540     1 TRVLIIEDEPLIAMDLEQIVeDLGHQVVgIARTRDEAVALARRERPDLILADIQLAdGSSGIDAVNEI---LTTHDVPVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2594348833 786 LLTA---CSLDEQRIQgydggaDSY-ISKPFSSQLLLARV 821
Cdd:cd17540    78 FVTAypeRLLTGERPE------PTFlITKPFDPEMVKAAI 111
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
411-625 2.31e-04

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 44.92  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 411 LEEATHAKLVFFTNISHDFRTPLT---LVADPVEHLLADSS-LS----EDQR--RM---LLLVQRNV--NILLRlvnqil 475
Cdd:PRK09470  236 LERMMTSQQRLLSDISHELRTPLTrlqLATALLRRRQGESKeLErietEAQRldSMindLLVLSRNQqkNHLER------ 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 476 dfrkyengkmEYTPISL---DIL--SSFEgwnesfmavARKKHIHFSFDYMPDTdYRTLADVEKLERIYFNLLSNAFKFT 550
Cdd:PRK09470  310 ----------ETFKANSlwsEVLedAKFE---------AEQMGKSLTVSAPPGP-WPINGNPNALASALENIVRNALRYS 369
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 551 peNGKVTVRLSsLTKDDhcwIRFTVANTGSMISAEHIRNIFDRFYKI----DMHHAGSGIGLALVKAFVELHKGTITVE 625
Cdd:PRK09470  370 --HTKIEVAFS-VDKDG---LTITVDDDGPGVPEEEREQIFRPFYRVdearDRESGGTGLGLAIVENAIQQHRGWVKAE 442
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
363-414 2.41e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 2.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 363 NRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEA 414
Cdd:COG3883   132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
602-639 2.92e-04

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 42.57  E-value: 2.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2594348833 602 AGSGIGLALVKAFVELHKGTITVESDEKQGTIFTVDLP 639
Cdd:cd16916   141 SGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
292-418 3.17e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 292 TAVVDRTNAHVMQLQTThISELDQKIETLNGRIGGYLSRVATQQVVMYG----GLVILLLVAGLLLVVYKSLRSKNRLNK 367
Cdd:COG4942    68 ARRIRALEQELAALEAE-LAELEKEIAELRAELEAQKEELAELLRALYRlgrqPPLALLLSPEDFLDAVRRLQYLKYLAP 146
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2594348833 368 ELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEATHAK 418
Cdd:COG4942   147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
64-230 5.46e-04

ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380487 [Multi-domain]  Cd Length: 270  Bit Score: 42.93  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  64 ADDNRKQAEDVHYFIDKGVDLLIISA--NEAAPMTPIVEEayqKGIPVILVDRKILsDKYTAYIGADNYEIGRAVGNYIA 141
Cdd:cd01545    39 SDDEDLADRLRRFLSRSRPDGVILTPplSDDPALLDALDE---LGIPYVRIAPGTD-DDRSPSVRIDDRAAAREMTRHLI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 142 SslKGKGNVVELTGLGGSTPAMERHQGFMAAISNYPdikliDKADAAWEREPA------EVEMDSMLRRHPKIDAVYAHN 215
Cdd:cd01545   115 A--LGHRRIGFIAGPPDHGASAERLEGFRDALAEAG-----LPLDPDLVVQGDftfesgLEAAEALLDLPDRPTAIFASN 187
                         170
                  ....*....|....*
gi 2594348833 216 DRIAPGAYQAAKKAG 230
Cdd:cd01545   188 DEMAAGVLAAAHRLG 202
PRK11303 PRK11303
catabolite repressor/activator;
66-213 6.35e-04

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 42.94  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  66 DNRKQAedVHYFIDKGVDLLIISAneAAPM-TPIVEEAYQKGIPVILVDRKILSDKYTAYIGAD---NYEIGRAVGNYIA 141
Cdd:PRK11303  104 DNEMRC--AEHLLQRQVDALIVST--SLPPeHPFYQRLQNDGLPIIALDRALDREHFTSVVSDDqddAEMLAESLLKFPA 179
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833 142 SSLkgkgnvveltGLGGSTPAM----ERHQGFMAAISNYPDIKLIDKADaAWEREPAEVEMDSMLRRHPKIDAVYA 213
Cdd:PRK11303  180 ESI----------LLLGALPELsvsfEREQGFRQALKDDPREVHYLYAN-SFEREAGAQLFEKWLETHPMPDALFT 244
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
357-415 7.29e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.29  E-value: 7.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 357 KSLRSKNRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLI----QLSHQLEEAT 415
Cdd:pfam20492  27 EELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAeekeQLEAELAEAQ 89
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
363-414 7.41e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 7.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 363 NRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEA 414
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
PRK09483 PRK09483
response regulator; Provisional
711-822 7.59e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 42.02  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLhTDYTVI----EAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLkseLQTC-HIPVI 785
Cdd:PRK09483    4 VLLVDDHELVRAGIRRIL-EDIKGIkvvgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKI---LRYTpDVKII 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 786 LLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARVR 822
Cdd:PRK09483   80 MLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIR 116
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
364-418 1.02e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.90  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2594348833 364 RLNKELSEQkkqvEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEATHAK 418
Cdd:pfam20492  24 KAQEELEES----EETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEME 74
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
97-231 1.13e-03

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 42.02  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  97 PIVEEAYQKGIPVILVDRKILSDKYTAYigadnYEI-GRAVGNYIASSLKGKG--NVVELTGLGGSTPAMERHQGFMAAI 173
Cdd:cd06287    70 PILARLRQRGVPVVSIGRAPGTDEPVPY-----VDLqSAATARLLLEHLHGAGarQVALLTGSSRRNSSLESEAAYLRFA 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2594348833 174 SNYPDIKLIDKADAAW-EREPAEVeMDSMLRRHPKIDAVYAHNDRIAPGAYQAAKKAGR 231
Cdd:cd06287   145 QEYGTTPVVYKVPESEgERAGYEA-AAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGR 202
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
357-418 1.58e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 357 KSLRSKNRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEATHAK 418
Cdd:COG4372    87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
362-419 1.75e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 1.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833  362 KNRLNKELSEQKKQVEQQRDKLEEQRDILE-EQRDKLEEQRDQLIQLSHQ-------LEEATHAKL 419
Cdd:pfam12128  666 KDKKNKALAERKDSANERLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEkqaywqvVEGALDAQL 731
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
711-789 1.80e-03

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: 38.92  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLL-HTDYTVIEAADGSEGIR--KAMKYVPDLIISDVMMPGMDGIECCRRLKSELQTCHIPVILL 787
Cdd:cd17582     1 VLLVENDDSTRQIVTALLrKCSYEVTAASDGLQAWDvlEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80

                  ..
gi 2594348833 788 TA 789
Cdd:cd17582    81 SS 82
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
541-626 1.83e-03

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 41.93  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 541 NLLSNAFKFTPENGKVTVRLSsltkDDHCWIrfTVANTGSMISAEHIRNIFDRFYKIDMHHAGSGIGLALVKAFVELHKG 620
Cdd:PRK10815  385 NVLDNACKYCLEFVEISARQT----DEHLHI--VVEDDGPGIPESKRELIFDRGQRADTLRPGQGLGLSVAREITEQYEG 458

                  ....*.
gi 2594348833 621 TITVES 626
Cdd:PRK10815  459 KISAGD 464
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
357-418 1.86e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 40.41  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 357 KSLRSKNRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEATHAK 418
Cdd:pfam09756   1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERK 62
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
711-821 1.92e-03

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: 39.17  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 711 VLIIDDNADIRLYVHGLLHT-DYTVIE-AADGSEGIRKAMKYVPDLIISDVMM-PGMDG---IECCRRLKSELQTChiPV 784
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSlGVTRIDtASSGEEALRMCENKTYDIVLCDYNLgKGKNGqqlLEELRHKKLISPST--VF 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2594348833 785 ILLTACSLDEQRIQGYDGGADSYISKPFSSQLLLARV 821
Cdd:cd17589    79 IMVTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
62-241 2.13e-03

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 41.07  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  62 SAADDNRKQAEDVHYFIDKGVDLLIISA-NEAAPMtpiVEEAYQK-GIPVILVDRKILSDKYTayIGADNYEIGRAVGNY 139
Cdd:cd06281    36 STGNDEERELELLSLFQRRRVDGLILTPgDEDDPE---LAAALARlDIPVVLIDRDLPGDIDS--VLVDHRSGVRQATEY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 140 IASSlkGKGNVVELTGLGGSTPAMERHQGFMAAISNY---PDIKLIDKADAAWEREPAEVEMdsMLRRHPKIDAVYAHND 216
Cdd:cd06281   111 LLSL--GHRRIALLTGGPDIRPGRERIAGFKAAFAAAglpPDPDLVRLGSFSADSGFREAMA--LLRQPRPPTAIIALGT 186
                         170       180
                  ....*....|....*....|....*..
gi 2594348833 217 RIAPGAYQAAKKAGRE--KEMIFVGID 241
Cdd:cd06281   187 QLLAGVLRAVRAAGLRipGDLSVVSIG 213
ftrA PRK09393
transcriptional activator FtrA; Provisional
869-954 2.24e-03

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 41.10  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 869 NLNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESP 948
Cdd:PRK09393  234 PHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSP 313

                  ....*.
gi 2594348833 949 TDLLKR 954
Cdd:PRK09393  314 AAYRKR 319
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
855-954 2.40e-03

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 41.04  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 855 EKFKALIEAKMGD--SNLNVEDLGKDMGLSRVQLYRKIKSLTNYSPNELLRIARLKKAASLLASSDMTVAEIGYEVGFSS 932
Cdd:PRK13501  176 EQLDLIMSALQQSlgAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFED 255
                          90       100
                  ....*....|....*....|..
gi 2594348833 933 PSYFTKCYREQFGESPTDLLKR 954
Cdd:PRK13501  256 SNYFSAVFTREAGMTPRDYRQR 277
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
362-414 2.73e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2594348833 362 KNRLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEEA 414
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
HATPase_AgrC-ComD-like cd16935
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
504-638 2.96e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Staphylococcus aureus AgrC and Streptococcus pneumoniae ComD which are involved in quorum sensing; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Staphylococcus aureus AgrC which is an HK of the accessory gene regulator (agr) quorum sensing two-component regulatory system (TCS) AgrC-AgrA. The agr system plays a part in the transition from persistent to virulent phenotype. This family also includes Streptococcus pneumoniae ComD HK of the ComD-ComE TCS, involved in quorum sensing and genetic competence.


Pssm-ID: 340412 [Multi-domain]  Cd Length: 134  Bit Score: 38.71  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 504 SFMAVARKKHIHFSFD-------YMPDTDyrtladvekLERIYFNLLSNAF----KFTPENGKVTVrlsSLTKDDHcWIR 572
Cdd:cd16935     8 EKLELAREKGIEFTIEidipillPISPLD---------LCIIFGNLLDNAIeacaKIDKENRFIHL---KIRQKKG-FLI 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2594348833 573 FTVANTgsmiSAEHIRNIFDRFY--KIDMHHagsGIGLALVKAFVELHKGTITVESDEKqgtIFTVDL 638
Cdd:cd16935    75 ISIENS----YEGELKKKNGLFLstKKDKNH---GIGLKSIREIVKKYNGNLSIEYENG---IFTLSI 132
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
360-413 3.60e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 3.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2594348833 360 RSKNRLnKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEE 413
Cdd:COG4372    98 QAQEEL-ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
364-415 4.27e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.09  E-value: 4.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833  364 RLNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQ----RDQLIQLSHQLEEAT 415
Cdd:COG3096    536 RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaaeaVEQRSELRQQLEQLR 591
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
708-810 4.88e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 39.47  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 708 KPC-VLIIDDNADIRLYVHGLLHTD---YTVIEAADGSEGIRKAMKYVPDLIISDVMMPGMDGIECCRRLKSeLQTcHIP 783
Cdd:PRK09935    2 KPAsVIIMDTHPIIRMSIEVLLQKNselQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQ-IQS-TVK 79
                          90       100
                  ....*....|....*....|....*..
gi 2594348833 784 VILLTACSLDEQRIQGYDGGADSYISK 810
Cdd:PRK09935   80 VLFLSSKSECFYAGRAIQAGANGFVSK 106
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
367-414 5.01e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 5.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2594348833 367 KELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLSHQL-EEA 414
Cdd:COG1340    11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELrEEA 59
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
356-406 5.31e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.16  E-value: 5.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2594348833 356 YKSLRSKNR-LNKELSEQKKQVEQQRDK---LEEQRDILEEQRDKLEEQRDQLIQ 406
Cdd:cd22887    20 LASLEEEIKdLEEELKEKNKANEILNDEliaLQIENNLLEEKLRKLQEENDELVE 74
PBP1_ABC_unchar_transporter cd06325
type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems ...
56-147 5.46e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally.


Pssm-ID: 380548  Cd Length: 282  Bit Score: 39.79  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833  56 VSVEIRSAADDnrKQAedVHYFIDKGVDLLIISANE--AAPMTPIVEEAYQKGIPVILVDRKILSDKYTAYIGADNYEIG 133
Cdd:cd06325   164 VEVPVSSPADI--EQA--FASLAGKVADALYVPTDNtvASARPRIAALALKARIPVIYSDREFVEAGALMSYGPDYYDLG 239
                          90
                  ....*....|....
gi 2594348833 134 RAVGNYIASSLKGK 147
Cdd:cd06325   240 RQAARYVDRILKGA 253
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
894-955 5.52e-03

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 39.91  E-value: 5.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 894 TNYSpnELLRIARLKKAASLLASSDMTVAEIGYEVGFSSPSYFTKCYREQFGESPTDLLKRK 955
Cdd:PRK09978  184 TSYS--QLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERS 243
CREPT pfam16566
Cell-cycle alteration and expression-elevated protein in tumour; CREPT (Cell-cycle alteration ...
363-413 5.98e-03

Cell-cycle alteration and expression-elevated protein in tumour; CREPT (Cell-cycle alteration and expression-elevated protein in tumour) is a family of eukaryotic transcriptional regulators that ptromote the binding of RNA-polymerase to the CYCLIN D1, CCDN1, promoter and other genes involved in the cell-cycle. It promotes the formation of a chromatin loop in the CYCLIN D1 gene, and is preferentially expressed in a range of different human tumours.


Pssm-ID: 465181 [Multi-domain]  Cd Length: 147  Bit Score: 38.37  E-value: 5.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2594348833 363 NRLNKELsEQKKQVEQQ-RDKLEEQRDILEEQRDKLEEQRDQLIQLSHQLEE 413
Cdd:pfam16566  65 GRLAAEL-EDRKKVAQMlRDFLQLQKELLAQAEERLEEYKEKLEKVSQVRKE 115
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
154-230 6.70e-03

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 38.47  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594348833 154 TGLGGSTPAMERHQGFMAAIS--NYPDIKLIDKADaaweREPAEVEMDSMLRRH-PKIDAVYAHNDRIAPGAYQAAKKAG 230
Cdd:pfam13377  16 EGDRDDPYSDLRERGFREAARelGLDVEPTLYAGD----DEAEAAAARERLRWLgALPTAVFVANDEVALGVLQALREAG 91
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
358-412 7.55e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.77  E-value: 7.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833 358 SLRSKNR-LNKELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQRDQLIQLshQLE 412
Cdd:cd22887     1 ELESELQeLEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIAL--QIE 54
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
367-414 7.64e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.04  E-value: 7.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2594348833 367 KELSEQKKQVEQQRDKLEEQRDILEEQRDKLeeqRDQLIQLSHQLEEA 414
Cdd:COG1842    87 REALERKAELEAQAEALEAQLAQLEEQVEKL---KEALRQLESKLEEL 131
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
368-418 8.71e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 8.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2594348833  368 ELSEQKKQVEQQRDKLEEQRDILEEQRDKLEEQR-----DQLIQLSHQLEEATHAK 418
Cdd:COG4913    299 ELRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLEREL 354
 
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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