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Conserved domains on  [gi|496047307|ref|WP_008771814|]
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substrate-binding domain-containing protein [Parabacteroides distasonis]

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 ...
30-299 2.10e-101

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: 316.80  E-value: 2.10e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRA 109
Cdd:cd06308    1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 GIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-REL 188
Cdd:cd06308   81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPGIKIvASQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 189 DGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDglLGGGLGVEAVAQGKLDASFY 267
Cdd:cd06308  161 DGDWLRDKAIKVMEDlLQAHPDIDAVYAHNDEMALGAYQALKKAG--REKEIKIIGVD--GLPEAGEKAVKDGILAATFL 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 496047307 268 YPTGGGVAIKVAWQILSGQAYTKKYALSTAMI 299
Cdd:cd06308  237 YPTGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
293-619 5.05e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 235.19  E-value: 5.05e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 293 ALSTAMIDKTNAGTLYLQSDRLAEYQRQIEKQRANLSQLLSKYNFLYSSLIIILILALLLGGSAIYMVYINRKVRQNNLL 372
Cdd:COG0642    2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 373 LNERNRLVQQQKEELSVANQRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAfADDIRIVKKNAERLKRV 452
Cdd:COG0642   82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQ-REYLETILRSADRLLRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 453 IDQLLDFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTP 532
Cdd:COG0642  161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 533 EQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQS-YAPGTGIGLHLTREFVLMHKGSIHVESEQGERTV 611
Cdd:COG0642  241 EGGTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSrRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTT 320

                 ....*...
gi 496047307 612 FTVQIPKG 619
Cdd:COG0642  321 FTVTLPLA 328
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
659-871 1.32e-39

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: 146.46  E-value: 1.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTlGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNRLREVFLKESQSPAGLSIETKGKVeSLDDLFMRKFIALI 817
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLHDIGKI-GIPDAILLKPGKLT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 818 EENYSdpDFSIEKGSEKLGLSRVHLYRKVKEL------SGITPTDFLRNYRLKKASALLK 871
Cdd:COG3437  167 PEEWE--ITHAHIGAEILSGSLLPLLQLAAEIherwdgSGLSARDALTSKKLEEALEEIR 224
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
872-908 1.08e-05

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


:

Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 43.30  E-value: 1.08e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 496047307  872 QRSGTISEVAYATGFgSPAYFSKCFKAVYNITPTEFI 908
Cdd:pfam00165   6 STNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
 
Name Accession Description Interval E-value
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
30-299 2.10e-101

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: 316.80  E-value: 2.10e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRA 109
Cdd:cd06308    1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 GIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-REL 188
Cdd:cd06308   81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPGIKIvASQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 189 DGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDglLGGGLGVEAVAQGKLDASFY 267
Cdd:cd06308  161 DGDWLRDKAIKVMEDlLQAHPDIDAVYAHNDEMALGAYQALKKAG--REKEIKIIGVD--GLPEAGEKAVKDGILAATFL 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 496047307 268 YPTGGGVAIKVAWQILSGQAYTKKYALSTAMI 299
Cdd:cd06308  237 YPTGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
293-619 5.05e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 235.19  E-value: 5.05e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 293 ALSTAMIDKTNAGTLYLQSDRLAEYQRQIEKQRANLSQLLSKYNFLYSSLIIILILALLLGGSAIYMVYINRKVRQNNLL 372
Cdd:COG0642    2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 373 LNERNRLVQQQKEELSVANQRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAfADDIRIVKKNAERLKRV 452
Cdd:COG0642   82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQ-REYLETILRSADRLLRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 453 IDQLLDFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTP 532
Cdd:COG0642  161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 533 EQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQS-YAPGTGIGLHLTREFVLMHKGSIHVESEQGERTV 611
Cdd:COG0642  241 EGGTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSrRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTT 320

                 ....*...
gi 496047307 612 FTVQIPKG 619
Cdd:COG0642  321 FTVTLPLA 328
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
6-304 8.01e-61

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: 209.01  E-value: 8.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   6 LYILLWLSLILcFACS------PGKKEKKYVIGVSQCSMTDIWRQSMIRDMEvEALNHPEIELVVMDAIQDNDTQISQIK 79
Cdd:COG1879    6 LAAVLALALAL-AACGsaaaeaAAAAAKGKTIGFVVKTLGNPFFVAVRKGAE-AAAKELGVELIVVDAEGDAAKQISQIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  80 GFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWG 159
Cdd:COG1879   84 DLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 160 RRGSSSATERHQGFVDAMSIDPNVKI-RELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEERDssLVG 237
Cdd:COG1879  164 SPGAPAANERTDGFKEALKEYPGIKVvAEQYADWDREKALEVMEDlLQAHPDIDGIFAANDGMALGAAQALKAAG--RKG 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496047307 238 HVEFIGVDgllGGGLGVEAVAQGKLDAS-FYYPTG-GGVAIKVAWQILSGQAYTKKYALSTAMIDKTNA 304
Cdd:COG1879  242 DVKVVGFD---GSPEALQAIKDGTIDATvAQDPYLqGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
659-871 1.32e-39

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: 146.46  E-value: 1.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTlGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNRLREVFLKESQSPAGLSIETKGKVeSLDDLFMRKFIALI 817
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLHDIGKI-GIPDAILLKPGKLT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 818 EENYSdpDFSIEKGSEKLGLSRVHLYRKVKEL------SGITPTDFLRNYRLKKASALLK 871
Cdd:COG3437  167 PEEWE--ITHAHIGAEILSGSLLPLLQLAAEIherwdgSGLSARDALTSKKLEEALEEIR 224
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
31-287 2.25e-36

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: 138.21  E-value: 2.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   31 IGVSQCSMTDIWRQSMIRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAG 110
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  111 IPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAM-SIDPNVKI--RE 187
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLkEKYPGIKVvaEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  188 LDGYWYRKNAYEEVLKL--DSIEDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGGLGVEAVAQGKLDAS 265
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALltAYPNPLDGIISPNDGMAGGAAQALEAAG--LAGKVVVTGFD---ATPEALEAIKDGTIDAT 235
                         250       260
                  ....*....|....*....|....
gi 496047307  266 FYYPTG--GGVAIKVAWQILSGQA 287
Cdd:pfam13407 236 VLQDPYgqGYAAVELAAALLKGKK 259
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
661-760 1.51e-35

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: 129.84  E-value: 1.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 661 LIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVILLTAL 739
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREK--GSDIPIIMLTAK 78
                         90       100
                 ....*....|....*....|.
gi 496047307 740 SDDSQRLYGFEGGADEYIQKP 760
Cdd:cd17574   79 DEEEDKVLGLELGADDYITKP 99
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
512-618 7.40e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 128.54  E-value: 7.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   512 DTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQ--SYAPGTGIGLHLT 589
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKrsRKIGGTGLGLSIV 81
                           90       100
                   ....*....|....*....|....*....
gi 496047307   590 REFVLMHKGSIHVESEQGERTVFTVQIPK 618
Cdd:smart00387  82 KKLVELHGGEISVESEPGGGTTFTITLPL 110
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
394-807 3.07e-34

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 140.85  E-value: 3.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 394 IEQVTTQKLQFFTNVSHEIKTPLTLILGpLNKMAQDAPAgafaDD-----IRIVKKNAERLKRVIDQLLDFRKIENNKMG 468
Cdd:PRK11091 276 LEKASRDKTTFISTISHELRTPLNGIVG-LSRILLDTEL----TAeqrkyLKTIHVSAITLGNIFNDIIDMDKMERRKLQ 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 469 LRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTF-LHEMDSLFVWVDTDKMEKILTNLLSNAFKFTpEQGKITIRLREEETE 547
Cdd:PRK11091 351 LDNQPIDFTDFLADLENLSGLQAEQKGLRFDLePLLPLPHKVITDGTRLRQILWNLISNAVKFT-QQGGVTVRVRYEEGD 429
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 548 VVL-SVEDNGEGIPPENLASVFERFF----TSGQSYAPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPKGKSH 622
Cdd:PRK11091 430 MLTfEVEDSGIGIPEDELDKIFAMYYqvkdSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVA 509
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 623 FDESCVFLSNatesssgvahldiSQVQETLNkkydytILIVEddwDI-------RAYLqhELSGNfNVLVAENGAKALDI 695
Cdd:PRK11091 510 EEVEDAFDED-------------DMPLPALN------ILLVE---DIelnvivaRSVL--EKLGN-SVDVAMTGKEALEM 564
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 696 LLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHI-PVILLTA--LSDDSQRLygfEGGADEYIQKPFNIeivklriik 772
Cdd:PRK11091 565 FDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTAnvLKDKKEYL---DAGMDDVLSKPLSV--------- 632
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 496047307 773 lleerNRLREVFLKESQSPAGLSIETKGKVESLDD 807
Cdd:PRK11091 633 -----PALTAMIKKFWDTQDDEESTVTTEESSKAN 662
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
516-616 2.71e-33

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


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 123.48  E-value: 2.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSYA-PGTGIGLHLTREFVL 594
Cdd:cd00075    1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREgGGTGLGLAIVRRIVE 80
                         90       100
                 ....*....|....*....|..
gi 496047307 595 MHKGSIHVESEQGERTVFTVQI 616
Cdd:cd00075   81 AHGGRITVESEPGGGTTFTVTL 102
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
392-617 5.55e-32

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: 130.59  E-value: 5.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  392 QRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLN-KMAQDAPAGAFADdirIVKKNAE---RLKRVIDQLLDFRKIENNKM 467
Cdd:TIGR01386 232 GRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQvALSQPRTGEEYRE---VLESNLEeleRLSRMVSDMLFLARADNGQL 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  468 GLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFlheMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETE 547
Cdd:TIGR01386 309 ALERVRLDLAAELAKVAEYFEPLAEERGVRIRV---EGEGLVRGDPQMFRRAISNLLSNALRHTPDGGTITVRIERRSDE 385
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047307  548 VVLSVEDNGEGIPPENLASVFERFF--TSGQSYA-PGTGIGLHLTREFVLMHKGSIHVESEQGeRTVFTVQIP 617
Cdd:TIGR01386 386 VRVSVSNPGPGIPPEHLSRLFDRFYrvDPARSNSgEGTGLGLAIVRSIMEAHGGRASAESPDG-KTRFILRFP 457
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
512-617 5.83e-31

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: 117.47  E-value: 5.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  512 DTDKMEKILTNLLSNAFKFTPEQGKITIRLREEEtEVVLSVEDNGEGIPPENLASVFERFFTSGQSYAPGTGIGLHLTRE 591
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGEITVTLSEGG-ELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTGLGLSIVRK 80
                          90       100
                  ....*....|....*....|....*.
gi 496047307  592 FVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:pfam02518  81 LVELLGGTITVESEPGGGTTVTLTLP 106
pleD PRK09581
response regulator PleD; Reviewed
659-762 3.17e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 116.15  E-value: 3.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVED-DWDIRaYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:PRK09581   4 RILVVDDiPANVK-LLEAKLLAEyYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMV 82
                         90       100
                 ....*....|....*....|....*.
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:PRK09581  83 TALDDPEDRVRGLEAGADDFLTKPIN 108
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
660-775 2.57e-23

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: 95.68  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  660 ILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVILLTA 738
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 496047307  739 LSDDSQRLYGFEGGADEYIQKPFNIEivklRIIKLLE 775
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPD----ELLAAIR 111
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
825-907 4.26e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 91.08  E-value: 4.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   825 DFSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSKCFKAVYNITP 904
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ...
gi 496047307   905 TEF 907
Cdd:smart00342  81 SEY 83
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
61-301 2.88e-17

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 83.22  E-value: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  61 ELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSI 140
Cdd:PRK10653  58 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 141 GMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSI-DPNVKIRELDGYWYRK--NAYEEVLKldSIEDVDIVFAHN 217
Cdd:PRK10653 138 GDFIAKKLGEGAKVIQLEGIAGTSAARERGEGFKQAVAAhKFNVLASQPADFDRTKglNVMQNLLT--AHPDVQAVFAQN 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 218 DMMALGAREAIEERDSSLVGHVEFIGVDgllgggLGVEAVAQGKLDASFYYPTG--GGVAIKVAWQILSGQAYTKKYALS 295
Cdd:PRK10653 216 DEMALGALRALQTAGKSDVMVVGFDGTP------DGIKAVNRGKLAATIAQQPDqiGAIGVETADKVLKGEKVEAKIPVD 289

                 ....*.
gi 496047307 296 TAMIDK 301
Cdd:PRK10653 290 LKLVTK 295
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
660-778 7.68e-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: 60.58  E-value: 7.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  660 ILIVEDDWDIRAYLQHELSG--NFNVL-VAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdMALSHIP-VIL 735
Cdd:TIGR02875   5 IVIADDNKEFCNLLKEYLAAqpDMEVVgVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNE-IELSARPrVIM 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 496047307  736 LTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERN 778
Cdd:TIGR02875  84 LSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQLAWGTN 126
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
872-908 1.08e-05

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 43.30  E-value: 1.08e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 496047307  872 QRSGTISEVAYATGFgSPAYFSKCFKAVYNITPTEFI 908
Cdd:pfam00165   6 STNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
 
Name Accession Description Interval E-value
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
30-299 2.10e-101

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: 316.80  E-value: 2.10e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRA 109
Cdd:cd06308    1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 GIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-REL 188
Cdd:cd06308   81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPGIKIvASQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 189 DGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDglLGGGLGVEAVAQGKLDASFY 267
Cdd:cd06308  161 DGDWLRDKAIKVMEDlLQAHPDIDAVYAHNDEMALGAYQALKKAG--REKEIKIIGVD--GLPEAGEKAVKDGILAATFL 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 496047307 268 YPTGGGVAIKVAWQILSGQAYTKKYALSTAMI 299
Cdd:cd06308  237 YPTGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
293-619 5.05e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 235.19  E-value: 5.05e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 293 ALSTAMIDKTNAGTLYLQSDRLAEYQRQIEKQRANLSQLLSKYNFLYSSLIIILILALLLGGSAIYMVYINRKVRQNNLL 372
Cdd:COG0642    2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 373 LNERNRLVQQQKEELSVANQRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAfADDIRIVKKNAERLKRV 452
Cdd:COG0642   82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQ-REYLETILRSADRLLRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 453 IDQLLDFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTP 532
Cdd:COG0642  161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 533 EQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQS-YAPGTGIGLHLTREFVLMHKGSIHVESEQGERTV 611
Cdd:COG0642  241 EGGTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSrRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTT 320

                 ....*...
gi 496047307 612 FTVQIPKG 619
Cdd:COG0642  321 FTVTLPLA 328
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
386-621 1.12e-68

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 228.25  E-value: 1.12e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 386 ELSVANQRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDA--PAGAFADDIRIVKKNAERLKRVIDQLLDFRKIE 463
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 464 NNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLRE 543
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARR 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496047307 544 EETEVVLSVEDNGEGIPPENLASVFERFFTSGQSY-APGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPKGKS 621
Cdd:COG2205  161 EGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRgEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAES 239
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
274-621 1.72e-64

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 222.12  E-value: 1.72e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 274 VAIKVAWQILSGQAYTKKYALSTAMIDKTNAGTLYLQSDRLAEYQRQIEKQRANLSQLLSKYNFLYSSLIIILILALLLG 353
Cdd:COG5002   34 LLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLIL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 354 GSAIYMVYINRKVRQNNLLLNERNRLVQQQKEELSVANQR----IEQVTTQKLQFFTNVSHEIKTPLTLILGPLnKMAQD 429
Cdd:COG5002  114 LAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERditeLERLEQMRREFVANVSHELRTPLTSIRGYL-ELLLD 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 430 APAG---AFADDIRIVKKNAERLKRVIDQLLDFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDS 506
Cdd:COG5002  193 GAADdpeERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDP 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 507 LFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSYA---PGTG 583
Cdd:COG5002  273 LLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSretGGTG 352
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 496047307 584 IGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPKGKS 621
Cdd:COG5002  353 LGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
6-304 8.01e-61

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: 209.01  E-value: 8.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   6 LYILLWLSLILcFACS------PGKKEKKYVIGVSQCSMTDIWRQSMIRDMEvEALNHPEIELVVMDAIQDNDTQISQIK 79
Cdd:COG1879    6 LAAVLALALAL-AACGsaaaeaAAAAAKGKTIGFVVKTLGNPFFVAVRKGAE-AAAKELGVELIVVDAEGDAAKQISQIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  80 GFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWG 159
Cdd:COG1879   84 DLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 160 RRGSSSATERHQGFVDAMSIDPNVKI-RELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEERDssLVG 237
Cdd:COG1879  164 SPGAPAANERTDGFKEALKEYPGIKVvAEQYADWDREKALEVMEDlLQAHPDIDGIFAANDGMALGAAQALKAAG--RKG 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496047307 238 HVEFIGVDgllGGGLGVEAVAQGKLDAS-FYYPTG-GGVAIKVAWQILSGQAYTKKYALSTAMIDKTNA 304
Cdd:COG1879  242 DVKVVGFD---GSPEALQAIKDGTIDATvAQDPYLqGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
30-292 2.96e-53

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: 186.62  E-value: 2.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDME--VEALNhpeIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAY 107
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEaaAKELG---VELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKAN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 108 RAGIPTIILDRKIN-SDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI- 185
Cdd:cd01536   78 AAGIPVVAVDTDIDgGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYPDIEIv 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 186 RELDGYWYRKNAY---EEVLKLDSieDVDIVFAHNDMMALGAREAIEErdSSLVGHVEFIGVDgllGGGLGVEAVAQGKL 262
Cdd:cd01536  158 AEQPANWDRAKALtvtENLLQANP--DIDAVFAANDDMALGAAEALKA--AGRTGDIKIVGVD---GTPEALKAIKDGEL 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 496047307 263 DAS-FYYPTG-GGVAIKVAWQILSGQAYTKKY 292
Cdd:cd01536  231 DATvAQDPYLqGYLAVEAAVKLLNGEKVPKEI 262
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
30-308 2.05e-51

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: 182.03  E-value: 2.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDME--VEALNhpeIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAY 107
Cdd:cd06309    1 TVGFSQAGSESPWRVANTKSIKeaAKKRG---YELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 108 RAGIPTIILDRKIN---SDEYTTYIGADNYEIGRSIGMYVS-SLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNV 183
Cdd:cd06309   78 DAGIPVILVDRTIDgedGSLYVTFIGSDFVEEGRRAAEWLVkNYKGGKGNVVELQGTAGSSVAIDRSKGFREVIKKHPNI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 184 KI-RELDGYWYRKNAYEEVLKLDSIE--DVDIVFAHNDMMALGAREAIEERDSSLVGHVEFIGVDgllGGGLGVEAVAQG 260
Cdd:cd06309  158 KIvASQSGNFTREKGQKVMENLLQAGpgDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGID---GQKDALEAIKAG 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 496047307 261 KLDASFYY-PTGGGVAIKVAWQILSGQAYTKKYALSTAMIDKTNAGTLY 308
Cdd:cd06309  235 ELNATVECnPLFGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNAAEEL 283
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
408-621 3.69e-43

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: 162.82  E-value: 3.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 408 VSHEIKTPLTLILGPLNKMAQDAPAGAFADD------IRIVKKNAERLKRVIDQLLDFRKIENNKMglrvIKMDLVFLIQ 481
Cdd:COG5000  208 IAHEIKNPLTPIQLSAERLRRKLADKLEEDRedleraLDTIIRQVDRLKRIVDEFLDFARLPEPQL----EPVDLNELLR 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 482 EVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPP 561
Cdd:COG5000  284 EVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDGRVRIEVSDNGPGIPE 363
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 562 ENLASVFERFFTSGQSyapGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPKGKS 621
Cdd:COG5000  364 EVLERIFEPFFTTKPK---GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEE 420
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
304-617 3.39e-42

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 158.04  E-value: 3.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 304 AGTLYLQSDRLAEYQRQIEKQRANLSQLLSKYNFLYSSLIIILILALLLGGSAIYMVYINRKVRQNNLL--LNERNRLVQ 381
Cdd:COG4191   41 ALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELeeLERDITELE 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 382 QQKEELSVANQRIEQvtTQKL----QFFTNVSHEIKTPLTLILG---PLNKMAQDAPAGA-FADDIRIVKKNAERLKRVI 453
Cdd:COG4191  121 RAEEELRELQEQLVQ--SEKLaalgELAAGIAHEINNPLAAILGnaeLLRRRLEDEPDPEeLREALERILEGAERAAEIV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 454 DQLLDF-RKienNKMGLRVIkmDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTP 532
Cdd:COG4191  199 RSLRAFsRR---DEEEREPV--DLNELIDEALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAME 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 533 E--QGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFT---SGQsyapGTGIGLHLTREFVLMHKGSIHVESEQG 607
Cdd:COG4191  274 EgeGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTtkpVGK----GTGLGLSISYGIVEKHGGRIEVESEPG 349
                        330
                 ....*....|
gi 496047307 608 ERTVFTVQIP 617
Cdd:COG4191  350 GGTTFTITLP 359
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
659-871 1.32e-39

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: 146.46  E-value: 1.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTlGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNRLREVFLKESQSPAGLSIETKGKVeSLDDLFMRKFIALI 817
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLHDIGKI-GIPDAILLKPGKLT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 818 EENYSdpDFSIEKGSEKLGLSRVHLYRKVKEL------SGITPTDFLRNYRLKKASALLK 871
Cdd:COG3437  167 PEEWE--ITHAHIGAEILSGSLLPLLQLAAEIherwdgSGLSARDALTSKKLEEALEEIR 224
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
658-770 3.69e-39

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: 143.51  E-value: 3.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:COG3706    2 ARILVVDDDPTNRKLLRRLLEAaGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFL 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRI 770
Cdd:COG3706   82 TALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
30-299 5.73e-39

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: 145.99  E-value: 5.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNhPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRA 109
Cdd:cd19968    1 KIGFSFPNLSFPFFVYMHEQAVDEAAK-LGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 GIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-REL 188
Cdd:cd19968   80 GIPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGPKIKVvFEQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 189 DGYWYRKNAY---EEVLKLDSiEDVDIVFAHNDMMALGAREAIeeRDSSL-VGHVEFIGVDgllGGGLGVEAVAQGKLDA 264
Cdd:cd19968  160 TGNFERDEGLtvmENILTSLP-GPPDAIICANDDMALGAIEAM--RAAGLdLKKVKVIGFD---AVPDALQAIKDGELYA 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 496047307 265 SFYYPTGG--GVAIKVAWQILSGQAYTKKYALSTAMI 299
Cdd:cd19968  234 TVEQPPGGqaRTALRILVDYLKDKKAPKKVNLKPKLI 270
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
60-300 1.30e-38

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: 144.75  E-value: 1.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  60 IELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRS 139
Cdd:cd06323   30 VELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSVTGGKVVSHIASDNVAGGEM 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 140 IGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-RELDGYWYRKNAYeEVLK--LDSIEDVDIVFAH 216
Cdd:cd06323  110 AAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYPKINVvASQTADFDRTKGL-NVMEnlLQAHPDIDAVFAH 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 217 NDMMALGAREAIEERDSSlvgHVEFIGVDgllGGGLGVEAVAQGKLDASF-YYPTG-GGVAIKVAWQILSGQAYTKKYAL 294
Cdd:cd06323  189 NDEMALGAIQALKAAGRK---DVIVVGFD---GTPDAVKAVKDGKLAATVaQQPEEmGAKAVETADKYLKGEKVPKKIPV 262

                 ....*.
gi 496047307 295 STAMID 300
Cdd:cd06323  263 PLKLVT 268
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
407-617 1.78e-38

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 147.30  E-value: 1.78e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 407 NVSHEIKTPLTLILGPLNKMAQDAPAGAFADDIRIVKKNAERLKRVIDQLLDFRKiennKMGLRVIKMDLVFLIQEVKSY 486
Cdd:COG3852  141 GLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSR----PRPPEREPVNLHEVLERVLEL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 487 FNN-LAQSKRIDYTFLhemDSL-FVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETE----------VVLSVED 554
Cdd:COG3852  217 LRAeAPKNIRIVRDYD---PSLpEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQVtlgglrprlyVRIEVID 293
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047307 555 NGEGIPPENLASVFERFFTSGQSyapGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:COG3852  294 NGPGIPEEILDRIFEPFFTTKEK---GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLP 353
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
359-618 4.94e-38

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 149.55  E-value: 4.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 359 MVYINRKVRQNNLLLNERNRLVQQQKEELSVANQRIEQvttqklqfFTN-VSHEIKTPLTLILGPLNKMAQDApAGAFAD 437
Cdd:COG4251  247 LLILVLELLELRLELEELEEELEERTAELERSNEELEQ--------FAYvASHDLREPLRKISGFSQLLEEDY-GDKLDE 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 438 D----IRIVKKNAERLKRVIDQLLDFRKIENNKMGLRVIKMDLvfLIQEVKSYFNNLAQSK--RIDYTFLHEmdslfVWV 511
Cdd:COG4251  318 EgreyLERIRDAAERMQALIDDLLAYSRVGRQELEFEPVDLNE--LLEEVLEDLEPRIEERgaEIEVGPLPT-----VRG 390
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 512 DTDKMEKILTNLLSNAFKFTP--EQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFT--SGQSYaPGTGIGLH 587
Cdd:COG4251  391 DPTLLRQVFQNLISNAIKYSRpgEPPRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRlhSRDEY-EGTGIGLA 469
                        250       260       270
                 ....*....|....*....|....*....|.
gi 496047307 588 LTREFVLMHKGSIHVESEQGERTVFTVQIPK 618
Cdd:COG4251  470 IVKKIVERHGGRIWVESEPGEGATFYFTLPK 500
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
31-308 1.16e-37

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: 142.41  E-value: 1.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  31 IGVSQCSMTDIWRQSMIRDMEvEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAG 110
Cdd:cd06313    2 IGFTVYGLSSEFITNLVEAMK-AVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 111 IPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVK-IRELD 189
Cdd:cd06313   81 IPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYPDIKvLAEQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 190 GYWYRKNAY---EEVLKLDSIEdVDIVFAHNDMMALGAREAIEERDsslVGHVEFIGVDgllGGGLGVEAVAQGKLDASF 266
Cdd:cd06313  161 ANWSRDEAMslmENWLQAYGDE-IDGIIAQNDDMALGALQAVKAAG---RDDIPVVGID---GIEDALQAVKSGELIATV 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 496047307 267 YY--PTGGGVAIKVAWQILSGQAYTKKYALSTAMIDKTNAGTLY 308
Cdd:cd06313  234 LQdaEAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDNVDDYL 277
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
372-617 2.34e-37

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


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 146.43  E-value: 2.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 372 LLNERNRLVQQQKEElsvanQRIEQVTTQKL----QFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFADDIRIVKKNAE 447
Cdd:COG5808  213 LLLQYNLLKRKTLLE-----RVIQEINTQKLeligTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFDIIQEEIQ 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 448 RLKRVIDQLLDFRKIENNKMGLRvikmDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNA 527
Cdd:COG5808  288 RINQIVSEFLVLGKPTAKKLELD----DLNELIEEILSIIDSEANLKNIRVEKQSLDEPLHIKCDKDRIKQVLLNLIKNA 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 528 FKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSyapGTGIGLHLTREFVLMHKGSIHVESEQG 607
Cdd:COG5808  364 IEAMKEGGKLTISIENDDEKAVIEVIDNGEGIPEDIIDEIFEPFVTTKEG---GTGLGLSVCKRIVEMHGGEIDIESEEG 440
                        250
                 ....*....|
gi 496047307 608 ERTVFTVQIP 617
Cdd:COG5808  441 KGTTFTIRLP 450
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
658-779 3.65e-37

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: 138.55  E-value: 3.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVILL 736
Cdd:COG0745    2 PRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPIIML 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNR 779
Cdd:COG0745   80 TARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAA 122
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
31-287 2.25e-36

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: 138.21  E-value: 2.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   31 IGVSQCSMTDIWRQSMIRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAG 110
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  111 IPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAM-SIDPNVKI--RE 187
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLkEKYPGIKVvaEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  188 LDGYWYRKNAYEEVLKL--DSIEDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGGLGVEAVAQGKLDAS 265
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALltAYPNPLDGIISPNDGMAGGAAQALEAAG--LAGKVVVTGFD---ATPEALEAIKDGTIDAT 235
                         250       260
                  ....*....|....*....|....
gi 496047307  266 FYYPTG--GGVAIKVAWQILSGQA 287
Cdd:pfam13407 236 VLQDPYgqGYAAVELAAALLKGKK 259
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
661-760 1.51e-35

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: 129.84  E-value: 1.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 661 LIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVILLTAL 739
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREK--GSDIPIIMLTAK 78
                         90       100
                 ....*....|....*....|.
gi 496047307 740 SDDSQRLYGFEGGADEYIQKP 760
Cdd:cd17574   79 DEEEDKVLGLELGADDYITKP 99
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
659-779 5.71e-35

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: 129.59  E-value: 5.71e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:COG0784    7 RILVVDDNPDNRELLRRLLERlGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALT 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNR 779
Cdd:COG0784   87 AYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
30-303 7.22e-35

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: 134.46  E-value: 7.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEAlNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRA 109
Cdd:cd06318    1 KIGFSQRTLASPYYAALVAAAKAEA-KKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 GIPTIILDRKINSD-EYTTYIGADNYEIGRSIGMYVSSLIKK-ETTILEIWGRRGSSSATERHQGFVDAMS-------ID 180
Cdd:cd06318   80 GIPVITVDSALDPSaNVATQVGRDNKQNGVLVGKEAAKALGGdPGKIIELSGDKGNEVSRDRRDGFLAGVNeyqlrkyGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 181 PNVKIRELD-GYWYRK---NAYEEVLKLDsiEDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGGLGVEA 256
Cdd:cd06318  160 SNIKVVAQPyGNWIRSgavAAMEDLLQAH--PDINVVYAENDDMALGAMKALKAAG--MLDKVKVAGAD---GQKEALKL 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496047307 257 VAQGKLDAsfyypTG-------GGVAIKVAWQILSGQAYTKKYALS-TAMIDKTN 303
Cdd:cd06318  233 IKDGKYVA-----TGlndpdllGKTAVDTAAKVVKGEESFPEFTYTpTALITKDN 282
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
512-618 7.40e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 128.54  E-value: 7.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   512 DTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQ--SYAPGTGIGLHLT 589
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKrsRKIGGTGLGLSIV 81
                           90       100
                   ....*....|....*....|....*....
gi 496047307   590 REFVLMHKGSIHVESEQGERTVFTVQIPK 618
Cdd:smart00387  82 KKLVELHGGEISVESEPGGGTTFTITLPL 110
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
30-245 1.24e-34

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: 133.56  E-value: 1.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHpEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRA 109
Cdd:cd06322    1 TIGVSLLTLQHPFFVDIKDAMKKEAAEL-GVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 GIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-REL 188
Cdd:cd06322   80 GIPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKKYPNIEIvAEQ 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 189 DGYWYRKNAY---EEVLKldSIEDVDIVFAHNDMMALGAREAIEERDSSlvGHVEFIGVD 245
Cdd:cd06322  160 PGDGRREEALaatEDMLQ--ANPDLDGIFAIGDPAALGALTAIESAGKE--DKIKVIGFD 215
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
30-308 1.75e-34

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: 133.91  E-value: 1.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHPEI--ELVVMDAiqDNDT--QISQIKGFIKKKVDLLIISSNETEPVTPVAVE 105
Cdd:cd19996    1 TIGFSNAGLGNSWRVQMIAEFEAEAAKLKKLikELIYTDA--QGDTqkQIADIQDLIAQGVDAIIVSPNSPTALLPAIEK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 106 AYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI 185
Cdd:cd19996   79 AAAAGIPVVLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPGIKI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 186 -RELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEERDSSLVGHVefiGVDG-----LLGGGLGVEAVA 258
Cdd:cd19996  159 vGEVYADWDYAKAKQAVESlLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMT---GEDNngflkAWKELPGFKSIA 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496047307 259 QGkldasfyYPTG-GGVAIKVAWQILSGQAYTKKYALSTAMIDKTNAGTLY 308
Cdd:cd19996  236 PS-------YPPWlGATALDAALAALEGEPVPKYVYIPLPVITDENLDQYV 279
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
394-807 3.07e-34

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 140.85  E-value: 3.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 394 IEQVTTQKLQFFTNVSHEIKTPLTLILGpLNKMAQDAPAgafaDD-----IRIVKKNAERLKRVIDQLLDFRKIENNKMG 468
Cdd:PRK11091 276 LEKASRDKTTFISTISHELRTPLNGIVG-LSRILLDTEL----TAeqrkyLKTIHVSAITLGNIFNDIIDMDKMERRKLQ 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 469 LRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTF-LHEMDSLFVWVDTDKMEKILTNLLSNAFKFTpEQGKITIRLREEETE 547
Cdd:PRK11091 351 LDNQPIDFTDFLADLENLSGLQAEQKGLRFDLePLLPLPHKVITDGTRLRQILWNLISNAVKFT-QQGGVTVRVRYEEGD 429
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 548 VVL-SVEDNGEGIPPENLASVFERFF----TSGQSYAPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPKGKSH 622
Cdd:PRK11091 430 MLTfEVEDSGIGIPEDELDKIFAMYYqvkdSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVA 509
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 623 FDESCVFLSNatesssgvahldiSQVQETLNkkydytILIVEddwDI-------RAYLqhELSGNfNVLVAENGAKALDI 695
Cdd:PRK11091 510 EEVEDAFDED-------------DMPLPALN------ILLVE---DIelnvivaRSVL--EKLGN-SVDVAMTGKEALEM 564
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 696 LLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHI-PVILLTA--LSDDSQRLygfEGGADEYIQKPFNIeivklriik 772
Cdd:PRK11091 565 FDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTAnvLKDKKEYL---DAGMDDVLSKPLSV--------- 632
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 496047307 773 lleerNRLREVFLKESQSPAGLSIETKGKVESLDD 807
Cdd:PRK11091 633 -----PALTAMIKKFWDTQDDEESTVTTEESSKAN 662
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
659-761 3.26e-34

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 126.46  E-value: 3.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAeGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                         90       100
                 ....*....|....*....|....
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPF 761
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKPI 104
PRK15347 PRK15347
two component system sensor kinase;
369-790 1.11e-33

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 139.78  E-value: 1.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 369 NNLL--LNER-----NRlVQQQKEELSVANQRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLN--KMAQ-DAPAGAFADD 438
Cdd:PRK15347 360 NQLLdtLNEQydtleNK-VAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALEllQNTPlTAEQMDLADT 438
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 439 IRivkKNAERLKRVIDQLLDFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRID-YTFLHEMDSLFVWVDTDKME 517
Cdd:PRK15347 439 AR---QCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTlRTFVGAHVPLYLHLDSLRLR 515
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 518 KILTNLLSNAFKFTpEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSgQSYAPGTGIGLHLTREFVLMHK 597
Cdd:PRK15347 516 QILVNLLGNAVKFT-ETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQA-DTHSQGTGLGLTIASSLAKMMG 593
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 598 GSIHVESEQGERTVFTVQIP--------KGKSHFD--------------------ESCVFLSNATESSSG--VAHLD-IS 646
Cdd:PRK15347 594 GELTLFSTPGVGSCFSLVLPlneyappePLKGELSaplalhrqlsawgitcqpghQNPALLDPELAYLPGrlYDLLQqII 673
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 647 QVQETLNKK------YDYTILIVED---DWDIRAYLQHELsGNfNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFE 717
Cdd:PRK15347 674 QGAPNEPVInlplqpWQLQILLVDDvetNRDIIGMMLVEL-GQ-QVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLE 751
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496047307 718 LCRRVKSDMAL--SHIPVILLTA--LSDDSQRLYgfEGGADEYIQKPFNIEIVKlRIIKLLEERNRLREVFLKESQS 790
Cdd:PRK15347 752 TTQLWRDDPNNldPDCMIVALTAnaAPEEIHRCK--KAGMNHYLTKPVTLAQLA-RALELAAEYQLLRGIELSPQDS 825
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
406-617 1.30e-33

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 137.79  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 406 TNVSHEIKTPLTLILGPLnKMAQDAPAGAFADD-IRIVKKNAERLKRVIDQLLDFRKIENNKMglrvIKMDLVFLIQEVK 484
Cdd:PRK11360 395 AGVAHEIRNPLTAIRGYV-QIWRQQTSDPPSQEyLSVVLREVDRLNKVIDQLLEFSRPRESQW----QPVSLNALVEEVL 469
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 485 SYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRL-REEETEVVLSVEDNGEGIPPEN 563
Cdd:PRK11360 470 QLFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTwQYSDGQVAVSIEDNGCGIDPEL 549
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496047307 564 LASVFERFFTSGQSyapGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:PRK11360 550 LKKIFDPFFTTKAK---GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
387-773 1.72e-33

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 139.87  E-value: 1.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  387 LSVANQRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAG-AFADDIRIVKKNAERLKRVIDQLLDFRKIENN 465
Cdd:PRK09959  698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKeQRVEAISLAYATGQSLLGLIGEILDVDKIESG 777
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  466 KMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEM-DSLFVWVDTDKMEKILTNLLSNAFKFTPEQG-KIT---IR 540
Cdd:PRK09959  778 NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFpDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAvKITtslGH 857
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  541 LREEETEVVLSVEDNGEGIPPENLASVFERFF-TSGQSYAPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPkg 619
Cdd:PRK09959  858 IDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSqTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP-- 935
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  620 kshfdescvflsnaTESSSGVAHLDiSQVQETLNKKYDYTILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLK 698
Cdd:PRK09959  936 --------------VEISQQVATVE-AKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLlGYDVDEATDGVQALHKVSM 1000
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496047307  699 ENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVILLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKL 773
Cdd:PRK09959 1001 QHYDLLITDVNMPNMDGFELTRKLREQN--SSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
516-616 2.71e-33

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


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 123.48  E-value: 2.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSYA-PGTGIGLHLTREFVL 594
Cdd:cd00075    1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREgGGTGLGLAIVRRIVE 80
                         90       100
                 ....*....|....*....|..
gi 496047307 595 MHKGSIHVESEQGERTVFTVQI 616
Cdd:cd00075   81 AHGGRITVESEPGGGTTFTVTL 102
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
29-292 4.02e-33

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: 129.27  E-value: 4.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  29 YVIGVSQCSMTDIWrQSMIRD-MEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAY 107
Cdd:cd06301    1 IKIGVSMQNFSDEF-LTYLRDaIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 108 RAGIPTIILDRK-INSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI- 185
Cdd:cd06301   80 DAGIPLVYVNREpDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYPGMKIv 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 186 RELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEerDSSLVGHVEFIGVDgllGGGLGVEAVAQGKLDA 264
Cdd:cd06301  160 AEQTANWSREKAMDIVENwLQSGDKIDAIVANNDEMAIGAILALE--AAGKKDDILVAGID---ATPDALKAMKAGRLDA 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 496047307 265 S-FYYPTG-GGVAIKVAWQILSGQAYTKKY 292
Cdd:cd06301  235 TvFQDAAGqGETAVDVAVKAAKGEEVESDI 264
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
660-774 2.47e-32

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: 121.66  E-value: 2.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLTA 738
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
392-617 5.55e-32

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: 130.59  E-value: 5.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  392 QRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLN-KMAQDAPAGAFADdirIVKKNAE---RLKRVIDQLLDFRKIENNKM 467
Cdd:TIGR01386 232 GRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQvALSQPRTGEEYRE---VLESNLEeleRLSRMVSDMLFLARADNGQL 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  468 GLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFlheMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETE 547
Cdd:TIGR01386 309 ALERVRLDLAAELAKVAEYFEPLAEERGVRIRV---EGEGLVRGDPQMFRRAISNLLSNALRHTPDGGTITVRIERRSDE 385
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047307  548 VVLSVEDNGEGIPPENLASVFERFF--TSGQSYA-PGTGIGLHLTREFVLMHKGSIHVESEQGeRTVFTVQIP 617
Cdd:TIGR01386 386 VRVSVSNPGPGIPPEHLSRLFDRFYrvDPARSNSgEGTGLGLAIVRSIMEAHGGRASAESPDG-KTRFILRFP 457
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
383-617 7.12e-32

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


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 127.98  E-value: 7.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 383 QKEELSVANQrieqvttqklqFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFADDIRIVKKNAERLKRVIDQLLDFRKI 462
Cdd:COG5807  140 RSEKLSVAGE-----------LAAGIAHEIRNPLTSIKGFLQLLQESREDSEREEYFNIIISEIDRINTIITELLVLSKP 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 463 ENNKMGlrviKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLR 542
Cdd:COG5807  209 KKFNFK----KLNLNDVLEDVIALLSTEAILKNISIKYDLADDEPVINGDKNQLKQVFINLIKNAIEAMETGGNITIKTY 284
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496047307 543 EEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSyapGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:COG5807  285 VEGDFVVISVKDEGIGIPEEVLEKIGEPFFTTKEE---GTGLGLSICKKIIEEHNGTIEVESKPGKGTTFTIYLP 356
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
512-617 5.83e-31

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: 117.47  E-value: 5.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  512 DTDKMEKILTNLLSNAFKFTPEQGKITIRLREEEtEVVLSVEDNGEGIPPENLASVFERFFTSGQSYAPGTGIGLHLTRE 591
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGEITVTLSEGG-ELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTGLGLSIVRK 80
                          90       100
                  ....*....|....*....|....*.
gi 496047307  592 FVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:pfam02518  81 LVELLGGTITVESEPGGGTTVTLTLP 106
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
660-761 4.42e-30

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 114.53  E-value: 4.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLTA 738
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAgYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                         90       100
                 ....*....|....*....|...
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPF 761
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
408-617 1.16e-29

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 123.36  E-value: 1.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 408 VSHEIKTPLTLILGPLNKMAQDAPAGAFADDI-RIVKKNAERLKRVIDQLLDFRKIENnkmgLRVIKMDLVFLIQEVKSY 486
Cdd:PRK10364 244 VAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLaQVMAKEADRLNRVVSELLELVKPTH----LALQAVDLNDLINHSLQL 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 487 FNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLAS 566
Cdd:PRK10364 320 VSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEA 399
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496047307 567 VFERFFTSGqsyAPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:PRK10364 400 IFTPYFTTK---AEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLP 447
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
69-301 7.13e-29

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: 116.93  E-value: 7.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  69 QDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLI 148
Cdd:cd20006   43 EDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 149 KKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKIrelDGYWY----RKNAYEEVLK-LDSIEDVDIVFAHNDMMALG 223
Cdd:cd20006  123 GEKGKVAIVSFVKGSSTAIEREEGFKQALAEYPNIKI---VETEYcdsdEEKAYEITKElLSKYPDINGIVALNEQSTLG 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 224 AREAIEERdsSLVGHVEFIGVDgllGGGLGVEAVAQGKLDA-----SFyypTGGGVAIKVAWQILSGQAYTKKYALSTAM 298
Cdd:cd20006  200 AARALKEL--GLGGKVKVVGFD---SSVEEIQLLEEGIIDAlvvqnPF---NMGYLSVQAAVDLLNGKKIPKRIDTGSVV 271

                 ...
gi 496047307 299 IDK 301
Cdd:cd20006  272 ITK 274
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
661-760 3.48e-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: 108.85  E-value: 3.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 661 LIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVILLTAL 739
Cdd:cd00156    1 LIVDDDPAIRELLKSLLErEGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLREL--PPDIPVIVLTAK 78
                         90       100
                 ....*....|....*....|.
gi 496047307 740 SDDSQRLYGFEGGADEYIQKP 760
Cdd:cd00156   79 ADEEDAVRALELGADDYLVKP 99
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
70-300 4.11e-28

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: 114.75  E-value: 4.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIK 149
Cdd:cd06310   42 DVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 150 KETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKIRELDGY---WYRKNAYEEVLKLDSIEDVDIVFAHNDMMALGARE 226
Cdd:cd06310  122 GKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVLASQYagsDYAKAANETEDLLGKYPDIDGIFATNEITALGAAV 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 227 AIEERDSSlvGHVEFIGVDGLLGGGLGVEAvaqGKLDASF----YYPtgGGVAIKVAWQILSGQAYTKKYALSTAMID 300
Cdd:cd06310  202 AIKSRKLS--GQIKIVGFDSQEELLDALKN---GKIDALVvqnpYEI--GYEGIKLALKLLKGEEVPKNIDTGAELIT 272
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
516-617 1.11e-27

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: 107.96  E-value: 1.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEqGKITIRLR---EEETEVVL--SVEDNGEGIPPENLASVFERFFTSGQSYAP---GTGIGLH 587
Cdd:cd16922    1 LRQILLNLLGNAIKFTEE-GEVTLRVSleeEEEDGVQLrfSVEDTGIGIPEEQQARLFEPFSQADSSTTRkygGTGLGLA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 496047307 588 LTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:cd16922   80 ISKKLVELMGGDISVESEPGQGSTFTFTLP 109
PRK13557 PRK13557
histidine kinase; Provisional
379-762 1.54e-27

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 118.23  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 379 LVQQQKEElsvanqRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFA-DDIRivkKNAERLKRVIDQLL 457
Cdd:PRK13557 154 LRQAQKME------ALGQLTGGIAHDFNNLLQVMSGYLDVIQAALSHPDADRGRMARSvENIR---AAAERAATLTQQLL 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 458 DF-RKienNKMGLRVIKM-DLVfliqevkSYFNNLAqsKRI---DYTFLHEMDSLfVW---VDTDKMEKILTNLLSNAFK 529
Cdd:PRK13557 225 AFaRK---QRLEGRVLNLnGLV-------SGMGELA--ERTlgdAVTIETDLAPD-LWncrIDPTQAEVALLNVLINARD 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 530 FTPEQGKITIRLREEETE---------------VVLSVEDNGEGIPPENLASVFERFFTS---GQsyapGTGIGLHLTRE 591
Cdd:PRK13557 292 AMPEGGRVTIRTRNVEIEdedlamyhglppgryVSIAVTDTGSGMPPEILARVMDPFFTTkeeGK----GTGLGLSMVYG 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 592 FVLMHKGSIHVESEQGERTVFTVQIPkgkshfdescvflsnateSSSGVAHLDISQVQETLNKKYDYTILIVEDDWDI-- 669
Cdd:PRK13557 368 FAKQSGGAVRIYSEVGEGTTVRLYFP------------------ASDQAENPEQEPKARAIDRGGTETILIVDDRPDVae 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 670 --RAYLQhelSGNFNVLVAENGAKALDILLKEN-VSLVVSDVMMP-EMNGFELCRRVKSdmALSHIPVILLTALSDDSQR 745
Cdd:PRK13557 430 laRMILE---DFGYRTLVASNGREALEILDSHPeVDLLFTDLIMPgGMNGVMLAREARR--RQPKIKVLLTTGYAEASIE 504
                        410
                 ....*....|....*..
gi 496047307 746 LYGFEGGADEYIQKPFN 762
Cdd:PRK13557 505 RTDAGGSEFDILNKPYR 521
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
46-299 1.63e-27

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: 112.92  E-value: 1.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  46 MIRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLI-ISSNETEPVTPVAVeAYRAGIPTIILDRKINSDE 124
Cdd:cd19972   16 QIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIyIPAGATAAAVPVKA-ARAAGIPVIAVDRNPEDAP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 125 YTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVK-IRELDGYWYRKNAYEEVLK 203
Cdd:cd19972   95 GDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEAPGIKvVAEQTADWDQDEGFKVAQD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 204 -LDSIEDVDIVFAHNDMMALGAREAIeeRDSSLVGHVEFIGVDgllGGGLGVEAVAQGKLDASFYYPTG--GGVAIKVAW 280
Cdd:cd19972  175 mLQANPNITVFFGQSDAMALGAAQAV--KVAGLDHKIWVVGFD---GDVAGLKAVKDGVLDATMTQQTQkmGRLAVDSAI 249
                        250
                 ....*....|....*....
gi 496047307 281 QILSGQAYTKKYALSTAMI 299
Cdd:cd19972  250 DLLNGKAVPKEQLQDAVLT 268
pleD PRK09581
response regulator PleD; Reviewed
659-762 3.17e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 116.15  E-value: 3.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVED-DWDIRaYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:PRK09581   4 RILVVDDiPANVK-LLEAKLLAEyYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMV 82
                         90       100
                 ....*....|....*....|....*.
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:PRK09581  83 TALDDPEDRVRGLEAGADDFLTKPIN 108
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
408-626 3.71e-27

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: 116.23  E-value: 3.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 408 VSHEIKTPLTLILGPLnKMAQDAPAGAFADDIRIVKKNAERLKRVIDQLLDFRKIENnkmgLRVIKMDLVFLIQEVKSYF 487
Cdd:COG5809  277 IAHEIRNPLTSLKGFI-QLLKDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQA----IKYEPKDLNTLIEEVIPLL 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 488 NNLAQSKRID--YTFLHEMDSlfVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLR-EEETEVVLSVEDNGEGIPPENL 564
Cdd:COG5809  352 QPQALLKNVQieLELEDDIPD--ILGDENQLKQVFINLLKNAIEAMPEGGNITIETKaEDDDKVVISVTDEGCGIPEERL 429
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496047307 565 ASVFERFFTSGQSyapGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPKGKSHFDES 626
Cdd:COG5809  430 KKLGEPFYTTKEK---GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
659-792 6.57e-27

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 114.68  E-value: 6.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLT 737
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVILLT 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNRLREVFLKES---QSPA 792
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGligRSPA 139
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
661-774 8.31e-27

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 105.82  E-value: 8.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 661 LIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLTAL 739
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEkEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496047307 740 SDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
42-304 1.22e-26

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: 110.82  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  42 WrQSMIRDMEVEALNHpEIELVVMDAIQDNDT--QISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRK 119
Cdd:cd06320   14 W-VAMKDGIEAEAKKL-GVKVDVQAAPSETDTqgQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKKGIPVINLDDA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 120 INSDE-------YTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKIRE-LDGY 191
Cdd:cd06320   92 VDADAlkkaggkVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKAPGLKLVAsQPAD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 192 WYRKNAY---EEVLKLDSieDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGGLGVEAVAQGKLDA--SF 266
Cdd:cd06320  172 WDRTKALdaaTAILQAHP--DLKGIYAANDTMALGAVEAVKAAG--KTGKVLVVGTD---GIPEAKKSIKAGELTAtvAQ 244
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 496047307 267 YYPTGGGVAIKVAWQILSGQAYTKKYALSTAMIDKTNA 304
Cdd:cd06320  245 YPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKDNV 282
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
395-767 1.26e-26

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 117.38  E-value: 1.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 395 EQVTTQKLQFFTNVSHEIKTPLTLILGPLNKM-AQDAPAGAfaddIRIVK--KNAERLK-RVIDQLLDFRKIENNKMGLR 470
Cdd:PRK10841 441 EQASQSKSMFLATVSHELRTPLYGIIGNLDLLqTKELPKGV----DRLVTamNNSSSLLlKIISDILDFSKIESEQLKIE 516
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 471 VIKmdlvFLIQEVKSYFNN----LAQSKRID-YTFLhEMDsLFVWVDTDKM--EKILTNLLSNAFKFTpEQGKITIRLRE 543
Cdd:PRK10841 517 PRE----FSPREVINHITAnylpLVVKKRLGlYCFI-EPD-VPVALNGDPMrlQQVISNLLSNAIKFT-DTGCIVLHVRV 589
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 544 EETEVVLSVEDNGEGIPPENLASVFERFF---TSGQSYAPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPKGK 620
Cdd:PRK10841 590 DGDYLSFRVRDTGVGIPAKEVVRLFDPFFqvgTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLYG 669
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 621 SHF-------------------------------------------------------DESC--------VFLSN----- 632
Cdd:PRK10841 670 AQYpqkkgveglqgkrcwlavrnasleqfletllqrsgiqvqryegqeptpedvlitdDPVQkkwqgravITFCRrhigi 749
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 633 ATESSSGVAHLDISQVQET---LNKKY------------------------DYTILIVeDDWDI-RAYLQHEL-SGNFNV 683
Cdd:PRK10841 750 PLEIAPGEWVHSTATPHELpalLARIYrielesddsanalpstdkavsdndDMMILVV-DDHPInRRLLADQLgSLGYQC 828
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 684 LVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsDMALsHIPVILLT--ALSDDSQRLygFEGGADEYIQKPF 761
Cdd:PRK10841 829 KTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLR-QLGL-TLPVIGVTanALAEEKQRC--LEAGMDSCLSKPV 904

                 ....*.
gi 496047307 762 NIEIVK 767
Cdd:PRK10841 905 TLDVLK 910
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
30-298 1.31e-26

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: 109.98  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWrQSMIRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRA 109
Cdd:cd19971    1 KFGFSYMTMNNPF-FIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 GIPTIILDRKINSDEY-TTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGsSSATERHQGFVDAMSIDPNVKI-RE 187
Cdd:cd19971   80 GIPVINVDTPVKDTDLvDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPTA-ESCVDRIDGFLDAIKKNPKFEVvAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 188 LDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEErdSSLVGHVEFIGVDGLLGGGlgvEAVAQGKLDASF 266
Cdd:cd19971  159 QDGKGQLEVAMPIMEDiLQAHPDLDAVFALNDPSALGALAALKA--AGKLGDILVYGVDGSPDAK---AAIKDGKMTATA 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 496047307 267 -YYPTG-GGVAIKVAWQILSGQAYTKKYALSTAM 298
Cdd:cd19971  234 aQSPIEiGKKAVETAYKILNGEKVEKEIVVPTFL 267
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
659-774 1.84e-26

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 104.64  E-value: 1.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLErAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd17618   82 ARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
410-617 2.22e-26

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 113.79  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 410 HEIKTPLTLILGPLNKMAQDAPAGA---FADDIRivkKNAERLKRVIDQLLDFRKIENNKMGLRVIKMDLVFLIQEVKSY 486
Cdd:PRK11100 265 HELKSPLAAIRGAAELLQEDPPPEDrarFTGNIL---TQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 487 FNNLAQSKRIDYTFlhEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLAS 566
Cdd:PRK11100 342 REAQAAAKGITLRL--RPDDARVLGDPFLLRQALGNLLDNAIDFSPEGGTITLSAEVDGEQVALSVEDQGPGIPDYALPR 419
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 567 VFERFFT-----SGQSyapGTGIGLHLTREFVLMHKGSIHVES--EQGERTVFTVQIP 617
Cdd:PRK11100 420 IFERFYSlprpaNGRK---STGLGLAFVREVARLHGGEVTLRNrpEGGVLATLTLPRH 474
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
30-287 2.39e-26

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: 109.98  E-value: 2.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEA--LNhpeIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAY 107
Cdd:cd19992    1 KIGVSFPTQQEERWQKDKEYMEEEAkeLG---VELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 108 RAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILeIWGRRGSSSATERHQGFVDamSIDPNVKIRE 187
Cdd:cd19992   78 AAGVPVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAVPKGNYVI-LSGDPGDNNAQLITAGAMD--VLQPAIDSGD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 188 ----LDGY---WYRKNAY---EEVLKLDSiEDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGGLGVEAV 257
Cdd:cd19992  155 ikivLDQYvkgWSPDEAMklvENALTANN-NNIDAVLAPNDGMAGGAIQALKAQG--LAGKVFVTGQD---AELAALKRI 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 496047307 258 AQGKLDASFYYPT--GGGVAIKVAWQILSGQA 287
Cdd:cd19992  229 VEGTQTMTVWKDLkeLARAAADAAVKLAKGEK 260
orf27 CHL00148
Ycf27; Reviewed
653-779 3.07e-26

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 108.27  E-value: 3.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 653 NKKYDYTILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHI 731
Cdd:CHL00148   2 MENSKEKILVVDDEAYIRKILETRLSiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE---SDV 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 496047307 732 PVILLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNR 779
Cdd:CHL00148  79 PIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNK 126
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
392-618 3.91e-26

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 113.33  E-value: 3.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 392 QRIEQVTTQKLQFFTNVSHEIKTPLT-LILGPLNKMAQDAPAGAFADDIRIVKKNAERLKRVIDQLLDFRKIENNKMGLR 470
Cdd:PRK09835 253 ERIEDVFTRQSNFSADIAHEIRTPITnLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPE 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 471 VIKMDLVFLIQEVKSYFNNLAQSKRIDYTFlhEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVL 550
Cdd:PRK09835 333 KKMLDLADEVGKVFDFFEAWAEERGVELRF--VGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEAITVRCQEVDHQVQL 410
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496047307 551 SVEDNGEGIPPENLASVFERFF---TSGQSYAPGTGIGLHLTREFVLMHKGSIHVESEqGERTVFTVQIPK 618
Cdd:PRK09835 411 VVENPGTPIAPEHLPRLFDRFYrvdPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSD-ARGTRFVISLPR 480
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
50-230 8.47e-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: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 107.84  E-value: 8.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  50 MEVEALNHPEIELVVMDAIQDndtQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYI 129
Cdd:cd06311   23 KQAKELADLEYKLVTSSNANE---QVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDLYV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 130 GADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAM-SIDPNVKIRELDGYWYRKNAYEEVLK-LDSI 207
Cdd:cd06311  100 AGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIkGNPGIKILAMQAGDWTREDGLKVAQDiLTKN 179
                        170       180
                 ....*....|....*....|...
gi 496047307 208 EDVDIVFAHNDMMALGAREAIEE 230
Cdd:cd06311  180 KKIDAVWAADDDMAIGVLQAIKE 202
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
660-762 1.05e-25

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 102.38  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHIPVILLTA 738
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEgFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT---SQVPVLMLTA 77
                         90       100
                 ....*....|....*....|....
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:cd17623   78 RGDDIDRILGLELGADDYLPKPFN 101
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
512-617 4.12e-25

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: 100.64  E-value: 4.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 512 DTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETE-VVLSVEDNGEGIPPENLASVFERFFTSGQSYAP---GTGIGLH 587
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFRLNrFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRahgGTGLGLS 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 496047307 588 LTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:cd16925   81 IVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
660-774 4.41e-25

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 100.92  E-value: 4.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLTA 738
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRfEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
399-619 1.35e-24

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 107.79  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 399 TQKLQ-------FFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFADD-IRIVKKNAERLKRVIDQLLDFRKIE---NNKM 467
Cdd:PRK11006 195 TQMHQlegarrnFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKaLHTMREQTQRMEGLVKQLLTLSKIEaapTIDL 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 468 GLRV-IKMDLVFLIQEVKSyfnnLAQSKridYTFLHEMD-SLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEE 545
Cdd:PRK11006 275 NEKVdVPMMLRVLEREAQT----LSQGK---HTITFEVDnSLKVFGNEDQLRSAISNLVYNAVNHTPEGTHITVRWQRVP 347
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496047307 546 TEVVLSVEDNGEGIPPENLASVFERFF-----TSGQSyaPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPKG 619
Cdd:PRK11006 348 QGAEFSVEDNGPGIAPEHIPRLTERFYrvdkaRSRQT--GGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPER 424
ompR PRK09468
osmolarity response regulator; Provisional
658-762 1.38e-24

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 103.52  E-value: 1.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELS-GNFNVLVAENgAKALD-ILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVIL 735
Cdd:PRK09468   6 YKILVVDDDMRLRALLERYLTeQGFQVRSAAN-AEQMDrLLTRESFHLMVLDLMLPGEDGLSICRRLRS--QNNPTPIIM 82
                         90       100
                 ....*....|....*....|....*..
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:PRK09468  83 LTAKGEEVDRIVGLEIGADDYLPKPFN 109
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
380-621 1.50e-24

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 106.86  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 380 VQQQKEELSVANQRIEQVTTQKlqfftnvsHEIKTPLTLILGpLNKMAQDAPAGAFADDIrivkknAERLKRVIDQLLdf 459
Cdd:COG3290  176 LERLEEELEGVKELAEALRAQR--------HDFRNHLHTISG-LLQLGEYDEALEYIDEI------SEELQELIDSLL-- 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 460 RKIENnkmglrvikmdlvFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAF----KFTPEQG 535
Cdd:COG3290  239 SRIGN-------------PVLAALLLGKAARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIeaveKLPEEER 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 536 KITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSyaPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQ 615
Cdd:COG3290  306 RVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLG--EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVR 383

                 ....*.
gi 496047307 616 IPKGKS 621
Cdd:COG3290  384 LPKEGE 389
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
375-632 1.76e-24

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 110.15  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 375 ERNRLvQQQKEELSVA---NQRIEQVTTqklqFFTNVSHEIKTPLTLILGpLNKMAQD--APAGAFADDIRIVKKNAERL 449
Cdd:PRK13837 426 ERRRL-ETERDALERRlehARRLEAVGT----LASGIAHNFNNILGAILG-YAEMALNklARHSRAARYIDEIISAGARA 499
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 450 KRVIDQLLDF-RKIEnnkmglRVIK-MDLVFLIQEVKSYFNnLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNA 527
Cdd:PRK13837 500 RLIIDQILAFgRKGE------RNTKpFDLSELVTEIAPLLR-VSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNA 572
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 528 FKFTPEQGKITIRLREEETE---------------VVLSVEDNGEGIPPENLASVFERFFTsgqSYAPGTGIGLHLTREF 592
Cdd:PRK13837 573 AQAMDGAGRVDISLSRAKLRapkvlshgvlppgryVLLRVSDTGAGIDEAVLPHIFEPFFT---TRAGGTGLGLATVHGI 649
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 496047307 593 VLMHKGSIHVESEQGERTVFTVQIP-------KGKSHFDESCVFLSN 632
Cdd:PRK13837 650 VSAHAGYIDVQSTVGRGTRFDVYLPpsskvpvAPQAFFGPGPLPRGR 696
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
660-760 4.00e-24

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: 97.45  E-value: 4.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLTA 738
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLeDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
519-617 1.23e-23

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: 96.20  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 519 ILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTS--GQSYAPGTGIGLHLTREFV--L 594
Cdd:cd16948    9 IIGQIVSNALKYSKQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGenGRNFQESTGMGLYLVKKLCdkL 88
                         90       100
                 ....*....|....*....|...
gi 496047307 595 MHKgsIHVESEQGERTVFTVQIP 617
Cdd:cd16948   89 GHK--IDVESEVGEGTTFTITFP 109
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
803-911 1.53e-23

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 101.01  E-value: 1.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 803 ESLDDLFMRKFIALIEENYSDPDFSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAY 882
Cdd:COG2207  146 LLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAY 225
                         90       100
                 ....*....|....*....|....*....
gi 496047307 883 ATGFGSPAYFSKCFKAVYNITPTEFIESL 911
Cdd:COG2207  226 ELGFSSQSHFSRAFKKRFGVTPSEYRKRL 254
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
658-782 1.75e-23

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 96.96  E-value: 1.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDD----WDIRAYLQhELSGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMAlsHIPV 733
Cdd:COG4565    4 IRVLIVEDDpmvaELLRRYLE-RLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGP--DVDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 496047307 734 ILLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNRLRE 782
Cdd:COG4565   81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
518-617 1.78e-23

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: 95.95  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 518 KILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSgQSYAPGTGIGLHLTREFVLMHK 597
Cdd:cd16943    6 QVLLNLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTT-KPVGEGTGLGLSLSYRIIQKHG 84
                         90       100
                 ....*....|....*....|
gi 496047307 598 GSIHVESEQGERTVFTVQIP 617
Cdd:cd16943   85 GTIRVASVPGGGTRFTIILP 104
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
660-775 2.57e-23

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: 95.68  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  660 ILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVILLTA 738
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 496047307  739 LSDDSQRLYGFEGGADEYIQKPFNIEivklRIIKLLE 775
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPD----ELLAAIR 111
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
49-286 5.52e-23

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: 99.63  E-value: 5.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  49 DMEVEALNHPE----IELVV--MDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINS 122
Cdd:cd19970   16 EMEKGARKHAKeangYELLVkgIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNRLDA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 123 DEYTT------YIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSiDPNVKIRELD-GYWYRK 195
Cdd:cd19970   96 DALKEgginvpFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFE-EAGMKIVASQsANWEID 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 196 NAYEEVLKLDSIE-DVDIVFAHNDMMALGAREAIEErdSSLVGHVEFIGVDgllGGGLGVEAVAQGKLDASF-YYPTGGG 273
Cdd:cd19970  175 EANTVAANLLTAHpDIRGILCANDNMALGAIKAVDA--AGKAGKVLVVGFD---NIPAVRPLLKDGKMLATIdQHPAKQA 249
                        250
                 ....*....|....
gi 496047307 274 V-AIKVAWQILSGQ 286
Cdd:cd19970  250 VyGIEYALKMLNGE 263
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
659-760 6.91e-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: 94.07  E-value: 6.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSGNFN---VLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVIL 735
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAGfevVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL--DPDTKIII 78
                         90       100
                 ....*....|....*....|....*
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKP 760
Cdd:COG4753   79 LSGYSDFEYAQEAIKLGADDYLLKP 103
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
379-724 6.98e-23

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 104.99  E-value: 6.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 379 LVQQQKEELSV-------ANQRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFADDIRIVKKNAERLKR 451
Cdd:PRK11466 415 QVKARTAELQElviehrqARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLT 494
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 452 VIDQLLDFRKIENNkmGLRVIKMDLVFLIQEVKSYFNNLAQSK------RIDYTFlheMDSLFVWVDTD--KMEKILTNL 523
Cdd:PRK11466 495 ILNDILDYSAIEAG--GKNVSVSDEPFEPRPLLESTLQLMSGRvkgrpiRLATDI---ADDLPTALMGDprRIRQVITNL 569
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 524 LSNAFKFTpEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFF-TSGQSyaPGTGIGLHLTREFVLMHKGSIHV 602
Cdd:PRK11466 570 LSNALRFT-DEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVqVSGKR--GGTGLGLTISSRLAQAMGGELSA 646
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 603 ESEQGERTVFTVQIPkgkshfdescvfLSNATESSSGVAHLDISQVqetlnkkyDYTILIVEDD-WDIRAYLQHELSGNF 681
Cdd:PRK11466 647 TSTPEVGSCFCLRLP------------LRVATAPVPKTVNQAVRLD--------GLRLLLIEDNpLTQRITAEMLNTSGA 706
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 496047307 682 NVLVAENGAKALDILLKE---NVSLVvsDVMMPEMNGFELCRRVKS 724
Cdd:PRK11466 707 QVVAVGNAAQALETLQNSepfAAALV--DFDLPDYDGITLARQLAQ 750
HTH_18 pfam12833
Helix-turn-helix domain;
832-907 1.03e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 92.65  E-value: 1.03e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496047307  832 SEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSG-TISEVAYATGFGSPAYFSKCFKAVYNITPTEF 907
Cdd:pfam12833   2 AAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTGlSVAEIALALGFSDASHFSRAFRRLFGLTPSEY 78
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
70-266 1.86e-22

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: 98.07  E-value: 1.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIK 149
Cdd:cd20004   42 DVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLN 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 150 KETTILEIWGRRGSSSATERHQGFVDAM-SIDPNVKIRElDGY--WYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAR 225
Cdd:cd20004  122 GKGKVALLRLAKGSASTTDRERGFLEALkKLAPGLKVVD-DQYagGTVGEARSSAENlLNQYPDVDGIFTPNESTTIGAL 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 496047307 226 EAIEERDSSlvGHVEFIGVDgllGGGLGVEAVAQGKLDASF 266
Cdd:cd20004  201 RALRRLGLA--GKVKFIGFD---ASDLLLDALRAGEISALV 236
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
660-774 2.41e-22

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: 93.17  E-value: 2.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGNF--NVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGfnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVT 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd19923   83 AEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
408-618 3.06e-22

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: 101.35  E-value: 3.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 408 VSHEIKTPLTLILGPLNKMaqdaPAGAFADD--IRIVKKNAERLKRVIDQLLDFRKIENNKMglrvIKMDLVFLIQEVKS 485
Cdd:COG5805  294 IAHEIRNPLTSIKGFLQLL----QPGIEDKEeyFDIMLSELDRIESIISEFLALAKPQAVNK----EKENINELIQDVVT 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 486 YFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLA 565
Cdd:COG5805  366 LLETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLK 445
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496047307 566 SVFERFFTSGQSyapGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIPK 618
Cdd:COG5805  446 KLGEPFFTTKEK---GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
825-907 4.26e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 91.08  E-value: 4.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   825 DFSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSKCFKAVYNITP 904
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ...
gi 496047307   905 TEF 907
Cdd:smart00342  81 SEY 83
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
31-303 6.80e-22

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: 96.66  E-value: 6.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  31 IGVSQCSMTDIWRQSMIRDMEVEAlNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAG 110
Cdd:cd06319    2 IGYSVYDLDNPFWQIMERGVQAAA-EELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 111 IPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIK------KETTILEIwgRRGSSSATERHQGFVDAM------- 177
Cdd:cd06319   81 IPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKengwggGSVGIIAI--PQSRVNGQARTAGFEDALeeagvee 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 178 ---SIDPNVKIREldGYwyrkNAYEEVLKLDsiEDVDIVFAHNDMMALGAREAIEErdSSLVGHVEFIGVDgllGGGLGV 254
Cdd:cd06319  159 valRQTPNSTVEE--TY----SAAQDLLAAN--PDIKGIFAQNDQMAQGALQAIEE--AGRTGDILVVGFD---GDPEAL 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496047307 255 EAVAQGKLDASFYY-PTG-GGVAIKVAWQILSG-QAYTKKYALSTAMIDKTN 303
Cdd:cd06319  226 DLIKDGKLDGTVAQqPFGmGARAVELAIQALNGdNTVEKEIYLPVLLVTSEN 277
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
660-760 7.04e-22

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: 90.96  E-value: 7.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLTA 738
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEgYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLMLTA 78
                         90       100
                 ....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd19935   79 RDSVEDRVKGLDLGADDYLVKP 100
PRK09303 PRK09303
histidine kinase;
365-617 1.16e-21

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 98.10  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 365 KVRQNNLLLNERNRLVQQQKEELsvanqrIEQVTTQKlQFFTNVSHEIKTPLT--------LILGPLNKMAQDAPAGaFA 436
Cdd:PRK09303 122 RYSQELLQLSDELFVLRQENETL------LEQLKFKD-RVLAMLAHDLRTPLTaaslaletLELGQIDEDTELKPAL-IE 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 437 DDIRIVKKNAERLKRVIDQLLDFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKM 516
Cdd:PRK09303 194 QLQDQARRQLEEIERLITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVYADQERI 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 517 EKILTNLLSNAFKFTPEQGKITIRLREEETE-VVLSVEDNGEGIPPENLASVFE-RFFTSGQSYAPGTGIGLHLTREFVL 594
Cdd:PRK09303 274 RQVLLNLLDNAIKYTPEGGTITLSMLHRTTQkVQVSICDTGPGIPEEEQERIFEdRVRLPRDEGTEGYGIGLSVCRRIVR 353
                        250       260
                 ....*....|....*....|...
gi 496047307 595 MHKGSIHVESEQGERTVFTVQIP 617
Cdd:PRK09303 354 VHYGQIWVDSEPGQGSCFHFTLP 376
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
659-768 1.22e-21

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: 90.79  E-value: 1.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdMALSHIPVILLT 737
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGaGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIK--QRHPDLPVIIMT 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNI-EIVKL 768
Cdd:cd19919   80 AHSDLDSAVSAYQGGAFEYLPKPFDIdEAVAL 111
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
31-305 1.70e-21

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: 95.52  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  31 IGVSQCSMTDIWRQSMIRDMEvEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAG 110
Cdd:cd06317    2 IALVQINQQAQFFNQINQGAQ-AAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 111 IPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKE---TTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-R 186
Cdd:cd06317   81 IPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGKYAADYIKAElggQAKIGVVGALSSLIQNQRQKGFEEALKANPGVEIvA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 187 ELDGywyrKNAYEEVLK-----LDSIEDVDIVFAHNDMMALGAREAIeeRDSSLVGHVEFIGVDGLLGGGLGV--EAVAQ 259
Cdd:cd06317  161 TVDG----QNVQEKALSaaenlLTANPDLDAIYATGEPALLGAVAAV--RSQGRQGKIKVFGWDLTKQAIFLGidEGVLQ 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 496047307 260 GKLDASFYypTGGGVAIKVAWQILSGQAYTKKYALSTAMIDKTNAG 305
Cdd:cd06317  235 AVVQQDPE--KMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTKENVD 278
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
659-763 2.00e-21

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: 90.29  E-value: 2.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDwDIRAYLQHEL--SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:cd17548    1 KILIVEDN-PLNMKLARDLleSAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIAL 79
                         90       100
                 ....*....|....*....|....*....
gi 496047307 737 T--ALSDDSQRLygFEGGADEYIQKPFNI 763
Cdd:cd17548   80 TayAMKGDREKI--LEAGCDGYISKPIDT 106
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
660-764 2.34e-21

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: 89.84  E-value: 2.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRV-KSDMALSHIPVILLT 737
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKlGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIrELEGGGRRTPIIALT 80
                         90       100
                 ....*....|....*....|....*..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIE 764
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLD 107
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
509-615 3.14e-21

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: 89.77  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 509 VWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLrEEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSYAPGTGIGLHL 588
Cdd:cd16940    7 VQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKL-SADDGAVIRVEDNGPGIDEEELEALFERFYRSDGQNYGGSGLGLSI 85
                         90       100
                 ....*....|....*....|....*..
gi 496047307 589 TREFVLMHKGSIHVESEQGERTVFTVQ 615
Cdd:cd16940   86 VKRIVELHGGQIFLGNAQGGGLEAWVR 112
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
660-774 4.08e-21

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: 89.35  E-value: 4.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDI----RAYLQHelsGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHIPVIL 735
Cdd:cd19939    2 ILIVEDELELarltRDYLIK---AGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILM 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd19939   76 LTARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
PRK10490 PRK10490
sensor protein KdpD; Provisional
371-617 4.51e-21

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 99.34  E-value: 4.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 371 LLLNERNRLVQQQKEELSVANQRIEQVTTQKLqffTNVSHEIKTPLTLILGP-----LNKMAQDAPAGAFADDIRIVKKN 445
Cdd:PRK10490 637 LIANALERLTLTASEEQARLASEREQLRNALL---AALSHDLRTPLTVLFGQaeiltLDLASEGSPHARQASEIRQQVLN 713
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 446 AERLkrvIDQLLDFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEMdsLFVWVDTDKMEKILTNLLS 525
Cdd:PRK10490 714 TTRL---VNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSLPEPL--TLIHVDGPLFERVLINLLE 788
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 526 NAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERfFTSG--QSYAPGTGIGLHLTREFVLMHKGSIHVE 603
Cdd:PRK10490 789 NAVKYAGAQAEIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDK-FARGnkESAIPGVGLGLAICRAIVEVHGGTIWAE 867
                        250
                 ....*....|....
gi 496047307 604 SEQGERTVFTVQIP 617
Cdd:PRK10490 868 NRPEGGACFRVTLP 881
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
519-617 6.17e-21

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: 88.50  E-value: 6.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 519 ILTNLLSNAFKFTPEQG----KITIRLREEETEVVLSVEDNGEGIPPENLASVFER-FFTSGQSyapGTGIGLHLTREFV 593
Cdd:cd16915    4 IVGNLIDNALDALAATGapnkQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERgVSTKGQG---ERGIGLALVRQSV 80
                         90       100
                 ....*....|....*....|....
gi 496047307 594 LMHKGSIHVESEQGERTVFTVQIP 617
Cdd:cd16915   81 ERLGGSITVESEPGGGTTFSIRIP 104
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
659-770 8.58e-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: 88.65  E-value: 8.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELS--GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRsaGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRI 770
Cdd:cd17551   82 TADTDREVRLRALEAGATDFLTKPFDPVELLARV 115
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
30-287 1.43e-20

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: 93.16  E-value: 1.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHPEI----ELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVE 105
Cdd:cd06300    1 TIGLSNTYAGNSWREQMIASLKADAAQSGQKglvkELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 106 AYRAGIPTIILDRKINSDEytTYIGADNY-EIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVK 184
Cdd:cd06300   81 AADAGIPVVAFDGAVTSPD--AYNVSNDQvEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYPGIK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 185 I-RELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDmMALGAREAIEERdsslvGH--VEFIGVDGLLGGGLGVEAVAQG 260
Cdd:cd06300  159 VvGEVFGGWDEATAQTAMLDfLATHPQVDGVWTQGG-EDTGVLQAFQQA-----GRppVPIVGGDENGFAKQWWKHPKKG 232
                        250       260
                 ....*....|....*....|....*...
gi 496047307 261 -KLDASFYYPTGGGVAIKVAWQILSGQA 287
Cdd:cd06300  233 lTGAAVWPPPAIGAAGLEVALRLLEGQG 260
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
520-617 2.17e-20

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: 87.26  E-value: 2.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 520 LTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFF---TSGQSYAPGTGIGLHLTREFVLMH 596
Cdd:cd16952    5 FSNLVSNAVKYTPPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYrvdIERCRNTGGTGLGLAIVKHVMSRH 84
                         90       100
                 ....*....|....*....|.
gi 496047307 597 KGSIHVESEQGERTVFTVQIP 617
Cdd:cd16952   85 DARLLIASELGKGSRFTCLFP 105
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
60-272 2.49e-20

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: 93.05  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  60 IELVVMDAIQDNDTQISQIKGFI--KKKVDLLIISsNETEPVTPVAVEAYRAGIPTIILDRKINSDE----------YTT 127
Cdd:cd06324   31 IELEVLYANRNRFKMLELAEELLarPPKPDYLILV-NEKGVAPELLELAEQAKIPVFLINNDLTDEErallgkprekFKY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 128 YIGA---DNYEIGRSIGMYvssLIK--------KETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-RELDGYWYRK 195
Cdd:cd06324  110 WLGSivpDNEQAGYLLAKA---LIKaarkksddGKIRVLAISGDKSTPASILREQGLRDALAEHPDVTLlQIVYANWSED 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 196 NAYEEVLKLDSI-EDVDIVFAHNDMMALGAREAIEER-----DSSLVGhvefiGVDgllGGGLGVEAVAQGKLDASFyyp 269
Cdd:cd06324  187 EAYQKTEKLLQRyPDIDIVWAANDAMALGAIDALEEAglkpgKDVLVG-----GID---WSPEALQAVKDGELTASV--- 255

                 ...
gi 496047307 270 tGG 272
Cdd:cd06324  256 -GG 257
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
660-762 2.55e-20

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: 87.22  E-value: 2.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQH--ELSGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:cd17552    4 ILVIDDEEDIREVVQAclEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLT 83
                         90       100
                 ....*....|....*....|....*..
gi 496047307 738 A--LSDDSQRLYGFegGADEYIQKPFN 762
Cdd:cd17552   84 AkaQPSDRQRFASL--GVAGVIAKPFD 108
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
518-617 2.88e-20

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: 86.86  E-value: 2.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 518 KILTNLLSNAFKFTP-EQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFT---SGQSYAPGTGIGLHLTREFV 593
Cdd:cd16953    3 QVLRNLIGNAISFSPpDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTerpANEAFGQHSGLGLSISRQII 82
                         90       100
                 ....*....|....*....|....*...
gi 496047307 594 LMHKGSIHVESEQGERTV----FTVQIP 617
Cdd:cd16953   83 EAHGGISVAENHNQPGQVigarFTVQLP 110
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
659-774 3.07e-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: 87.05  E-value: 3.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDI----RAYLQHElsgNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdmALSHIPVI 734
Cdd:cd19938    1 RILIVEDEPKLaqllIDYLRAA---GYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR---RFSDVPII 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496047307 735 LLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd19938   75 MVTARVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
659-774 3.50e-20

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: 87.02  E-value: 3.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVILLT 737
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRyEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLT 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd17615   79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL 115
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
660-766 4.15e-20

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: 86.57  E-value: 4.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmaLSHIPVILLTA 738
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFISS 77
                         90       100
                 ....*....|....*....|....*...
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIV 766
Cdd:cd18159   78 RDDNMDQVMAINMGGDDYITKPFDLDVL 105
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
660-760 6.31e-20

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: 85.89  E-value: 6.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDIL---------LKENVSLVVSDVMMPEMNGFELCRRVKSDMALS 729
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLkNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 496047307 730 HIPVILLTALSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
360-617 7.40e-20

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: 93.01  E-value: 7.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 360 VYINRKVRQNNLLlneRNRLvqQQKEELSVANQrieqvttqklqFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFADD- 438
Cdd:COG5806  176 VYLIENLIENILL---RKEL--QRAEKLEVVSE-----------LAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQy 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 439 IRIVKKNAERLKRVIDQLLDFRKIENNKMglrvIKMDLVFLIQEVKSYFNNLAQSKRIDYTflHEM-DSLFVWVDTDKME 517
Cdd:COG5806  240 IRIALEELDRAEAIITDYLTFAKPQPEKL----EKIDVSEELEHVIDVLSPYANMNNVEIQ--TELePGLYIEGDRQKLQ 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 518 KILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSyapGTGIGLHLTREFVLMHK 597
Cdd:COG5806  314 QCLINIIKNGIEAMPNGGTLTIDVSIDKNKVIISIKDTGVGMTKEQLERLGEPYFSTKEK---GTGLGTMVSYRIIEAMN 390
                        250       260
                 ....*....|....*....|
gi 496047307 598 GSIHVESEQGERTVFTVQIP 617
Cdd:COG5806  391 GTIRVESEVGKGTTFTITLP 410
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
657-775 1.06e-19

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 85.62  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 657 DYTILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVIL 735
Cdd:COG5803    2 MKKILIVDDQAGIRMLLKEVLKKEgYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEID--PDIPVIM 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLE 775
Cdd:COG5803   80 MTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
659-767 1.08e-19

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: 85.43  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGaGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFN----IEIVK 767
Cdd:cd17562   82 TESSDEKKQEGKAAGATGWLVKPFDpeqlLEVVK 115
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
30-230 1.23e-19

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: 90.83  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHPE----IELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVE 105
Cdd:cd19999    1 VIGVSNGYVGNEWRAQMIADFEEVAAEYKEegviSDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 106 AYRAGIPTIILDRKINSdEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI 185
Cdd:cd19999   81 AQAAGILVVSFDQPVSS-PDAINVVIDQYKWAAIQAQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKYPGIKV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 496047307 186 -RELDGYWYRKNAyEEVLK--LDSIEDVDIVFAHnDMMALGAREAIEE 230
Cdd:cd19999  160 lASVPGGWDQATA-QQVMAtlLATYPDIDGVLTQ-DGMAEGVLRAFQA 205
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
661-774 1.87e-19

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: 84.58  E-value: 1.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 661 LIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLTAL 739
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKeGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTAL 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496047307 740 SDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd17625   79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
512-603 1.88e-19

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: 84.44  E-value: 1.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 512 DTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFF---TSGQSYAPGTGIGLHL 588
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYrveSSRNRASGGSGLGLAI 80
                         90
                 ....*....|....*
gi 496047307 589 TREFVLMHKGSIHVE 603
Cdd:cd16946   81 CHNIALAHGGTISAE 95
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
660-770 1.98e-19

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: 84.46  E-value: 1.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLTA 738
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTA 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRI 770
Cdd:cd17624   79 RDGVDDRVAGLDAGADDYLVKPFALEELLARL 110
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
810-907 2.66e-19

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: 89.83  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 810 MRKFIALIEENYSDPdFSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSP 889
Cdd:COG4977  212 LARAQAWMEANLEEP-LSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSA 290
                         90
                 ....*....|....*...
gi 496047307 890 AYFSKCFKAVYNITPTEF 907
Cdd:COG4977  291 SHFRRAFRRRFGVSPSAY 308
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
659-764 3.02e-19

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 84.39  E-value: 3.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDD-WDIRAYLQ--HELSGNFNVLVAENGAKALDILLKEN-------VSLVVSDVMMPEMNGFELCRRVKSDMAL 728
Cdd:cd17557    1 TILLVEDNpGDAELIQEafKEAGVPNELHVVRDGEEALDFLRGEGeyadaprPDLILLDLNMPRMDGFEVLREIKADPDL 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496047307 729 SHIPVILLTALSDDSQRLYGFEGGADEYIQKPFNIE 764
Cdd:cd17557   81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFE 116
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
659-792 5.42e-19

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 86.94  E-value: 5.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLT 737
Cdd:PRK11083   5 TILLVEDEQAIADTLVYALQSEgFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLA--FHPALPVIFLT 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIiklleeRNRLREVFLKESQSPA 792
Cdd:PRK11083  83 ARSDEVDRLVGLEIGADDYVAKPFSPREVAARV------RTILRRVKKFAAPSPV 131
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-617 5.96e-19

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: 82.76  E-value: 5.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEQ--GKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFT-SGQSYAPGTGIGLHLTREF 592
Cdd:cd16921    1 LGQVLTNLLGNAIKFRRPRrpPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRlHSREEYEGTGVGLAIVRKI 80
                         90       100
                 ....*....|....*....|....*
gi 496047307 593 VLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:cd16921   81 IERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
507-616 6.68e-19

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: 83.33  E-value: 6.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 507 LFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFT---SGQSYAPGTG 583
Cdd:cd16947   12 IYANANTEALQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTledSRNSAKQGNG 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 496047307 584 IGLHLTREFVLMHKGSIHVESEQGERTVFTVQI 616
Cdd:cd16947   92 LGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
62-237 8.46e-19

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: 87.19  E-value: 8.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  62 LVVMDAIQDNDTQISQIKGFIKKKVD-LLIISSNETEPVtpvAVEAYRAGIPTIILDRKINSDEYTtYIGADNYEIGRSI 140
Cdd:cd06267   32 LLLCNTDEDPEREREYLRLLLSRRVDgIILAPSSLDDEL---LEELLAAGIPVVLIDRRLDGLGVD-SVVVDNYAGAYLA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 141 GMYvssLIKK-ETTILEIWGRRGSSSATERHQGFVDAMS-----IDPNvkiRELDGYWYRKNAYEEVLK-LDSIEDVDIV 213
Cdd:cd06267  108 TEH---LIELgHRRIAFIGGPLDLSTSRERLEGYRDALAeaglpVDPE---LVVEGDFSEESGYEAARElLALPPRPTAI 181
                        170       180       190
                 ....*....|....*....|....*....|
gi 496047307 214 FAHNDMMALGAREAIEER------DSSLVG 237
Cdd:cd06267  182 FAANDLMAIGALRALRELglrvpeDISVVG 211
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
27-238 1.04e-18

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 88.33  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  27 KKYVIGVSQCSMTDIWRQSMIRDMEVEALNHpEIELVVMDAIQDNDTQISQIKGFIKKKVD-LLIISSNETEPVTPvavE 105
Cdd:COG1609   60 RTRTIGVVVPDLSNPFFAELLRGIEEAARER-GYQLLLANSDEDPEREREALRLLLSRRVDgLILAGSRLDDARLE---R 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 106 AYRAGIPTIILDRKINSDEYTtYIGADNYEIGRSIgmyVSSLIKK-ETTILEIWGRRGSSSATERHQGFVDAMSiDPNVK 184
Cdd:COG1609  136 LAEAGIPVVLIDRPLPDPGVP-SVGVDNRAGARLA---TEHLIELgHRRIAFIGGPADSSSARERLAGYREALA-EAGLP 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496047307 185 IRE---LDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEER------DSSLVGH 238
Cdd:COG1609  211 PDPelvVEGDFSAESGYEAARRlLARGPRPTAIFCANDLMALGALRALREAglrvpeDVSVVGF 274
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
660-774 1.43e-18

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 82.04  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWD----IRAYL-QHelsgNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALshiPVI 734
Cdd:cd17622    3 ILLVEDDPKlarlIADFLeSH----GFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG---PIL 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496047307 735 LLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd17622   76 LLTALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
658-775 1.57e-18

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: 82.07  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILL 736
Cdd:cd17569    1 PTILLVDDEPNILKALKRLLRReGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRE--RYPDTVRILL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496047307 737 TALSDDSQRLYGF-EGGADEYIQKPFNIEIVKLRIIKLLE 775
Cdd:cd17569   79 TGYADLDAAIEAInEGEIYRFLTKPWDDEELKETIRQALE 118
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
660-764 2.29e-18

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 81.35  E-value: 2.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQH--ELSGnFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLT 737
Cdd:cd17580    1 ILVVDDNEDAAEMLALllELEG-AEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALT 79
                         90       100
                 ....*....|....*....|....*..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIE 764
Cdd:cd17580   80 GYGQPEDRERALEAGFDAHLVKPVDPD 106
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
660-774 2.32e-18

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 81.56  E-value: 2.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMAlsHIPVILLTA 738
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDaGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLILTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd19934   79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALI 114
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
660-775 2.39e-18

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: 81.80  E-value: 2.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILlKEN--VSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRhNFQVLEAANGQEALEVL-EQHpdIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLE 775
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKPFLPEEFYCRVTQNLE 120
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
658-762 4.16e-18

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 80.89  E-value: 4.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHIPVILL 736
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQeGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ---SEVGIILV 77
                         90       100
                 ....*....|....*....|....*.
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:cd17619   78 TGRDDEVDRIVGLEIGADDYVTKPFN 103
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
30-285 6.86e-18

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: 85.33  E-value: 6.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEpVTPVAVEAYR- 108
Cdd:cd01539    2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRT-AAQTIIDKAKa 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 109 AGIPTIILDRK-----INSDEYTTYIGADNYEIGRSIGMYVSSLIKK------------ETTILEiwGRRGSSSATERHQ 171
Cdd:cd01539   81 ANIPVIFFNREpsredLKSYDKAYYVGTDAEESGIMQGEIIADYWKAnpeidkngdgkiQYVMLK--GEPGHQDAIARTK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 172 GFVDAMsIDPNVKIRELD---GYWYRKNAYEEVLKLDSI--EDVDIVFAHNDMMALGAREAIEERDSSLVGHVEFI---G 243
Cdd:cd01539  159 YSVKTL-NDAGIKTEQLAedtANWDRAQAKDKMDAWLSKygDKIELVIANNDDMALGAIEALKAAGYNTGDGDKYIpvfG 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 496047307 244 VDgllGGGLGVEAVAQGKLDASFY--YPTGGGVAIKVAWQILSG 285
Cdd:cd01539  238 VD---ATPEALEAIKEGKMLGTVLndAKAQAKAIYELAKNLANG 278
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
660-762 7.97e-18

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: 80.21  E-value: 7.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHIPVILLTA 738
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE---SGVPIVMLTA 79
                         90       100
                 ....*....|....*....|....
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:cd17626   80 KSDTVDVVLGLESGADDYVAKPFK 103
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
660-778 8.10e-18

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 83.70  E-value: 8.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQH--ELSGnFNVLVAENGAKALDiLLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHIPVILLT 737
Cdd:PRK10955   4 ILLVDDDRELTSLLKEllEMEG-FNVIVAHDGEQALD-LLDDSIDLLLLDVMMPKKNGIDTLKELRQT---HQTPVIMLT 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERN 778
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSH 119
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
660-782 9.57e-18

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 80.23  E-value: 9.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQH--ELSGnFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKS-DmalSHIPVILL 736
Cdd:cd17549    1 VLLVDDDADVREALQQtlELAG-FRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRElD---PDLPVILI 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496047307 737 TALSD-----DSQRLygfegGADEYIQKPFN----IEIVK--LRIIKLLEERNRLRE 782
Cdd:cd17549   77 TGHGDvpmavEAMRA-----GAYDFLEKPFDperlLDVVRraLEKRRLVLENRRLRQ 128
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
660-776 1.43e-17

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: 79.30  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQH---ELSGNFN-VLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVIL 735
Cdd:cd17536    1 VLIVDDEPLIREGLKKlidWEELGFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL--YPDIKIII 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 496047307 736 LTALSDdsqrlygFE-------GGADEYIQKPFNIEIVKLRIIKLLEE 776
Cdd:cd17536   79 LSGYDD-------FEyaqkairLGVVDYLLKPVDEEELEEALEKAKEE 119
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
660-761 1.50e-17

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 79.39  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdmALSHIPVILLTA 738
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEgYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR---KTSNVPIIMLTA 77
                         90       100
                 ....*....|....*....|...
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPF 761
Cdd:cd17614   78 KDSEVDKVLGLELGADDYVTKPF 100
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-607 1.52e-17

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: 79.04  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFT-----SGQSyapGTGIGLHLTR 590
Cdd:cd16945    5 LRQAINNLLDNAIDFSPEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSlprphSGQK---STGLGLAFVQ 81
                         90
                 ....*....|....*..
gi 496047307 591 EFVLMHKGSIHVESEQG 607
Cdd:cd16945   82 EVAQLHGGRITLRNRPD 98
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
70-300 1.77e-17

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: 83.44  E-value: 1.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKIN-SDEYTTYIGADNYEIGRSIGMYVSSLI 148
Cdd:cd20007   41 DPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDTTLGdPSFVLSQIASDNVAGGALAAEALAELI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 149 KKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKIRELDgywYRKN----AYEEVLK-LDSIEDVDIVFAHNDMMALG 223
Cdd:cd20007  121 GGKGKVLVINSTPGVSTTDARVKGFAEEMKKYPGIKVLGVQ---YSENdpakAASIVAAaLQANPDLAGIFGTNTFSAEG 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 224 AREAIeeRDSSLVGHVEFIGVDgllGGGLGVEAVAQGKLDA----SFYypTGGGVAIKVAWQILSGQAYTKKYALSTAMI 299
Cdd:cd20007  198 AAAAL--RNAGKTGKVKVVGFD---ASPAQVEQLKAGTIDAliaqKPA--EIGYLAVEQAVAALTGKPVPKDILTPFVVI 270

                 .
gi 496047307 300 D 300
Cdd:cd20007  271 T 271
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
61-301 2.88e-17

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 83.22  E-value: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  61 ELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSI 140
Cdd:PRK10653  58 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 141 GMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSI-DPNVKIRELDGYWYRK--NAYEEVLKldSIEDVDIVFAHN 217
Cdd:PRK10653 138 GDFIAKKLGEGAKVIQLEGIAGTSAARERGEGFKQAVAAhKFNVLASQPADFDRTKglNVMQNLLT--AHPDVQAVFAQN 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 218 DMMALGAREAIEERDSSLVGHVEFIGVDgllgggLGVEAVAQGKLDASFYYPTG--GGVAIKVAWQILSGQAYTKKYALS 295
Cdd:PRK10653 216 DEMALGALRALQTAGKSDVMVVGFDGTP------DGIKAVNRGKLAATIAQQPDqiGAIGVETADKVLKGEKVEAKIPVD 289

                 ....*.
gi 496047307 296 TAMIDK 301
Cdd:PRK10653 290 LKLVTK 295
PRK15479 PRK15479
transcriptional regulator TctD;
660-774 2.98e-17

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 81.69  E-value: 2.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVILLTA 738
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNgFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRG--QTLPVLLLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:PRK15479  81 RSAVADRVKGLNVGADDYLPKPFELEELDARLRALL 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
660-760 4.39e-17

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 77.20  E-value: 4.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmaLSHIPVILLTA 738
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAhGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLRE---WSAVPVIVLSA 77
                         90       100
                 ....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd17620   78 RDEESDKIAALDAGADDYLTKP 99
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
660-760 4.39e-17

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: 77.49  E-value: 4.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdmALSHIPVILLTA 738
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR---QKSTLPVIFLTS 77
                         90       100
                 ....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd19936   78 KDDEIDEVFGLRMGADDYITKP 99
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
70-292 6.07e-17

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: 81.89  E-value: 6.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSNETEPVTPvAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIK 149
Cdd:cd20008   42 DIAGQVNLVENAISRKPDAIVLAPNDTAALVP-AVEAADAGIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAELLK 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 150 KETT----ILEIWGRRGSSSATERHQGFVDAMS-IDPNVKIreLDGYWY---RKNAYEEVlkLDSIE---DVDIVFAHND 218
Cdd:cd20008  121 ASGGgkgkVAIISFQAGSQTLVDREEGFRDYIKeKYPDIEI--VDVQYSdgdIAKALNQT--TDLLTanpDLVGIFGANN 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 219 MMALGAREAIEERdsSLVGHVEFIGVDgllGGGLGVEAVAQGKLDASF----YYPtgGGVAIKVAWQILSGQAYTKKY 292
Cdd:cd20008  197 PSAVGVAQALAEA--GKAGKIVLVGFD---SSPDEVALLKSGVIKALVvqdpYQM--GYEGVKTAVKALKGEEIVEKN 267
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
70-187 6.22e-17

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: 81.86  E-value: 6.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIK 149
Cdd:cd06314   41 DAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALP 120
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 496047307 150 KETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKIRE 187
Cdd:cd06314  121 GGGKVAIITGGLGADNLNERIQGFKDALKGSPGIEIVD 158
PRK10766 PRK10766
two-component system response regulator TorR;
657-774 1.28e-16

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 79.70  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 657 DYTILIVEDDWDIRA----YLQHElsgNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHIP 732
Cdd:PRK10766   2 SYHILVVEDEPVTRArlqgYFEQE---GYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSR---STVG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 496047307 733 VILLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:PRK10766  76 IILVTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
404-603 1.77e-16

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 83.14  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 404 FFTNVSHEIKTPLTLILGPLNKMaQDAPAGAFADDIRIVKKNAERLKRVIDQLLDFRKIENNKMGLRVIKMDLVFLIQEV 483
Cdd:PRK10549 243 FMADISHELRTPLAVLRGELEAI-QDGVRKFTPESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLLEVA 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 484 KSYFNNLAQSKRIDYTF-LHEMDSLFVwvDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPE 562
Cdd:PRK10549 322 GGAFRERFASRGLTLQLsLPDSATVFG--DPDRLMQLFNNLLENSLRYTDSGGSLHISAEQRDKTLRLTFADSAPGVSDE 399
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 496047307 563 NLASVFERFFTSGQSY---APGTGIGLHLTREFVLMHKGSIHVE 603
Cdd:PRK10549 400 QLQKLFERFYRTEGSRnraSGGSGLGLAICLNIVEAHNGRIIAA 443
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
30-303 1.83e-16

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: 81.18  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEA--LNHPEI--ELVVMDAIQDNDTQISQIKGFIKKKVDLLIIssnetEPVTPVAV- 104
Cdd:cd19997    1 VIALSNSYAGNTWRQQMVDAFEEAAkkAKADGLiaDYIVVNADGSATTQISQIQNLILQGVDAIVI-----DAASPTALn 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 105 ----EAYRAGIPTIILDRKINSDEYttYIGADNYE-IGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSI 179
Cdd:cd19997   76 gaiqQACDAGIKVVVFDSGVTEPCA--YILNNDFEdYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 180 DPNVKI-RELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDmMALGAREAIEE--RDSSLV---GHVEFIGVDGLLGGGL 252
Cdd:cd19997  154 YPDLKVvAEVYGNWTQSVAQKAVTGiLPSLPEVDAVITQGG-DGYGAAQAFEAagRPLPIIiggNRGEFLKWWQEEYAKN 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496047307 253 GVEAVAQGKldasfyYPTGGGVAIKVAWQILSGQAYTKKYALSTAMIDKTN 303
Cdd:cd19997  233 GYETVSVST------DPGQGSAAFWVALDILNGKDVPKEMILPVVTITEDD 277
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
383-623 2.43e-16

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 84.13  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 383 QKEELSVANQRIEQVTTQKLQFFTNVSHEIKTPLTLILG--------PLNKMAQDApagafaddIRIVKKNAERLKRVID 454
Cdd:PRK11107 275 QNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGftrqtlktPLTPTQRDY--------LQTIERSANNLLAIIN 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 455 QLLDFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFL--HEMDSLFVWvDTDKMEKILTNLLSNAFKFTp 532
Cdd:PRK11107 347 DILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNidPDVPDNVIG-DPLRLQQIITNLVGNAIKFT- 424
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 533 EQGKITIR--LREEETEVVL---SVEDNGEGIPPENLASVFERFftsGQSYAP------GTGIGLHLTREFVLMHKGSIH 601
Cdd:PRK11107 425 ESGNIDILveLRALSNTKVQlevQIRDTGIGISERQQSQLFQAF---RQADASisrrhgGTGLGLVITQKLVNEMGGDIS 501
                        250       260
                 ....*....|....*....|..
gi 496047307 602 VESEQGERTVFTVQIPKGKSHF 623
Cdd:PRK11107 502 FHSQPNRGSTFWFHLPLDLNPN 523
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
61-264 3.23e-16

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: 79.67  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  61 ELVVMDAIQDNDTQISQIKGFIKKKVDLLII-SSNETEPVTPVAvEAYRAGIPTIILDRKINS-DEYTTYIGADNYEIGR 138
Cdd:cd19967   31 EVTVFDHQNDTAKEAELFDTAIASGAKAIILdPADADASIAAVK-KAKDAGIPVFLIDREINAeGVAVAQIVSDNYQGAV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 139 SIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVK-IRELDGYWYRKNAYEevlKLDSI----EDVDIV 213
Cdd:cd19967  110 LLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQYPELKmVAQQSADWDRTEAFE---KMESIlqanPDIKGV 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496047307 214 FAHNDMMALGAREAIEErdSSLVGHVEFIGVDgllGGGLGVEAVAQGKLDA 264
Cdd:cd19967  187 ICGNDEMALGAIAALKA--AGRAGDVIIVGFD---GSNDVRDAIKEGKISA 232
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
659-773 4.49e-16

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: 74.95  E-value: 4.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLT 737
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEgYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIICT 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496047307 738 ALSDDSQRLYGFegGADEYIQKPFNIEIVKLRIIKL 773
Cdd:cd17554   80 AYSEYKSDFSSW--AADAYVVKSSDLTELKETIKRL 113
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
658-806 5.18e-16

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 78.32  E-value: 5.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELS--GNFNVL-VAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVI 734
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEkyPDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRE--LDPPPPII 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496047307 735 LLTALSDDSqrLYGFEGGADEYIQKPFNIEIVKLRIIKLLeERNRLREVFLKESQSPAGLSIETKGKVESLD 806
Cdd:COG3279   80 FTTAYDEYA--LEAFEVNAVDYLLKPIDEERLAKALEKAK-ERLEAKAAAEASPEEKDRIFVKSGGKLVKIP 148
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-617 5.77e-16

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: 74.36  E-value: 5.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFK-FTPEQGKITIR--------LREEETEVVL--SVEDNGEGIPPENLASVFERFFTSGQSyapGTGI 584
Cdd:cd16918    1 LIQVFLNLVRNAAQaLAGSGGEIILRtrtqrqvtLGHPRHRLALrvSVIDNGPGIPPDLQDTIFYPMVSGREN---GTGL 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 496047307 585 GLHLTREFVLMHKGSIHVESEQGeRTVFTVQIP 617
Cdd:cd16918   78 GLAIAQNIVSQHGGVIECDSQPG-HTVFSVSLP 109
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
814-907 6.37e-16

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: 80.48  E-value: 6.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 814 IALIEENYSDPDfSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQrSGTISEVAYATGFGSPAYFS 893
Cdd:COG2169   90 CRLIEAGAEDRP-SLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQT-GLSVTDAAYAAGFGSLSRFY 167
                         90
                 ....*....|....
gi 496047307 894 KCFKAVYNITPTEF 907
Cdd:COG2169  168 EAFKKLLGMTPSAY 181
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
53-245 8.80e-16

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: 78.43  E-value: 8.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  53 EALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLII--SSNETEpvtpvAVEAYRAGIPTIILDRKINSDEYTtYIG 130
Cdd:cd06290   23 EVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVvgGFGDEE-----LLKLLAEGIPVVLVDRELEGLNLP-VVN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 131 ADNYEIGRsigMYVSSLIKK-ETTILEIWGRRGSSSATERHQGFVDAM-----SIDPNvkiRELDGYWYRKNAYEEVLK- 203
Cdd:cd06290   97 VDNEQGGY---NATNHLIDLgHRRIVHISGPEDHPDAQERYAGYRRALedaglEVDPR---LIVEGDFTEESGYEAMKKl 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 496047307 204 LDSIEDVDIVFAHNDMMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd06290  171 LKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFD 212
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
48-286 9.37e-16

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: 78.62  E-value: 9.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  48 RDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTT 127
Cdd:cd01538   18 RDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLILNADVDY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 128 YIGADNYEIGRsigMYVSSLIKK--ETTILEIWGRRGSSSATERHQGfvdAMS-IDPNV---KIRELDGY----WYRKNA 197
Cdd:cd01538   98 YISFDNEKVGE---LQAQALLDAkpEGNYVLIGGSPTDNNAKLFRDG---QMKvLQPAIdsgKIKVVGDQwvddWLPANA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 198 Y---EEVLKlDSIEDVDIVFAHNDMMALGAREAIEErdSSLVGHVEFIGVDgllGGGLGVEAVAQGKLDASFYYPTG--G 272
Cdd:cd01538  172 QqimENALT-ANGNNVDAVVASNDGTAGGAIAALKA--QGLSGGVPVSGQD---ADLAAIKRILAGTQTMTVYKDIRllA 245
                        250
                 ....*....|....
gi 496047307 273 GVAIKVAWQILSGQ 286
Cdd:cd01538  246 DAAAEVAVALMRGE 259
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
48-292 1.64e-15

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 78.25  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  48 RDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTT 127
Cdd:COG4213   21 GDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYDRLILNSDVDY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 128 YIGADNYEIGRSIGMYVSSLIKKETT--ILEIWGRRGSSSATERHQGfvdAMSI-DPNV---KIRELDGY----WYRKNA 197
Cdd:COG4213  101 YVSFDNVKVGELQGQYLVDGLPLKGKgnIELFGGSPTDNNATLFFEG---AMSVlQPYIdsgKLVVVSGQwtlgWDPETA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 198 YEEVlklDSI-----EDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGGLGVEAVAQGKLDASFYYPTG- 271
Cdd:COG4213  178 QKRM---ENLltangNKVDAVLAPNDGLAGGIIQALKAQG--LAGKVVVTGQD---AELAAVQRILAGTQYMTVYKDTRe 249
                        250       260
                 ....*....|....*....|....
gi 496047307 272 -GGVAIKVAWQILSGQ--AYTKKY 292
Cdd:COG4213  250 lAEAAAELAVALAKGEkpEVNGTY 273
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-617 2.79e-15

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: 72.43  E-value: 2.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFK----FTPEQGKITIRL-REEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSyapGTGIGLHLTR 590
Cdd:cd16920    1 IQQVLINLVRNGIEamseGGCERRELTIRTsPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSE---GLGMGLSICR 77
                         90       100
                 ....*....|....*....|....*..
gi 496047307 591 EFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:cd16920   78 SIIEAHGGRLSVESPAGGGATFQFTLP 104
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
48-245 3.19e-15

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: 76.89  E-value: 3.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  48 RDMEVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTT 127
Cdd:cd19991   18 RDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADVDL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 128 YIGADNYEIGRSIGMYVSSLIKKETTILeIWGRRGSSSATERHQGFVDAMS--IDP-NVKIRE---LDGYWYRKNAY--E 199
Cdd:cd19991   98 YVSFDNEKVGELQAEALVKAKPKGNYVL-LGGSPTDNNAKLFREGQMKVLQplIDSgDIKVVGdqwVDDWDPEEALKimE 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 496047307 200 EVLKLDSIeDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVD 245
Cdd:cd19991  177 NALTANNN-KIDAVIASNDGTAGGAIQALAEQG--LAGKVAVSGQD 219
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-616 3.49e-15

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: 72.10  E-value: 3.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEQ--GKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSgQSYAPGTGIGLHLTREFV 593
Cdd:cd16976    1 IQQVLMNLLQNALDAMGKVenPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTT-KPVGKGTGLGLSISYGIV 79
                         90       100
                 ....*....|....*....|...
gi 496047307 594 LMHKGSIHVESEQGERTVFTVQI 616
Cdd:cd16976   80 EEHGGRLSVANEEGAGARFTFDL 102
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
660-760 3.57e-15

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 71.85  E-value: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdmALSHIPVILLTA 738
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEgFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMVTA 77
                         90       100
                 ....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd17621   78 KDSEIDKVVGLELGADDYVTKP 99
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
659-767 4.09e-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: 72.44  E-value: 4.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHEL-SGNFNVL-VAENGAKALDILLKENVSLVVSDVMMP-EMNGFELCRRVKSdmaLSHIPVIL 735
Cdd:cd17534    2 KILIVEDEAIIALDLKEILeSLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE---KFDIPVIF 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496047307 736 LTALSDDS--QR-----LYGfeggadeYIQKPFNIEIVK 767
Cdd:cd17534   79 LTAYSDEEtlERaketnPYG-------YLVKPFNERELK 110
PRK10604 PRK10604
sensor protein RstB; Provisional
385-617 4.53e-15

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 78.49  E-value: 4.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 385 EELSVA-NQ---RIEQVTTQKLQFFTNVSHEIKTPLTLI---LGPLNKMAQDAPAgAFADDIrivkknaERLKRVIDQLL 457
Cdd:PRK10604 192 ERLGVAfNQmadNINALIASKKQLIDGIAHELRTPLVRLryrLEMSDNLSAAESQ-ALNRDI-------GQLEALIEELL 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 458 DFRKIENNKMGLRVIKMDLVFLIQEVKSYFNNLAQSKRIDYTFLHEmdSLFVWVDTDKMEKILTNLLSNAFKFTpeQGKI 537
Cdd:PRK10604 264 TYARLDRPQNELHLSEPDLPAWLSTHLADIQAVTPEKTVRLDTPHQ--GDYGALDMRLMERVLDNLLNNALRYA--HSRV 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 538 TIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSY---APGTGIGLHLTREFVLMHKGSIHVESEQ--GERTVF 612
Cdd:PRK10604 340 RVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRdraTGGCGLGLAIVHSIALAMGGSVNCDESElgGARFSF 419

                 ....*
gi 496047307 613 TVQIP 617
Cdd:PRK10604 420 SWPVW 424
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
30-286 7.28e-15

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: 75.79  E-value: 7.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEA-LNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYR 108
Cdd:cd06321    1 VIGVTVQDLGNPFFVAMVRGAEEAAaEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 109 AGIPTIILDrkINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRgSSSATERHQGFVDAMSIDPNVKIR-E 187
Cdd:cd06321   81 AGIIVVAVD--VAAEGADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPP-VSAVIDRVNGCKEALAEYPGIKLVdD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 188 LDGYWYRKNAyEEVLK--LDSIEDVDIVFAHNDMMALGAREAIEERDSSlvgHVEFIGVDGLLggglgvEAVAQGKLDAS 265
Cdd:cd06321  158 QNGKGSRAGG-LSVMTrmLTAHPDVDGVFAINDPGAIGALLAAQQAGRD---DIVITSVDGSP------EAVAALKREGS 227
                        250       260
                 ....*....|....*....|....*...
gi 496047307 266 FYYPTG-------GGVAIKVAWQILSGQ 286
Cdd:cd06321  228 PFIATAaqdpydmARKAVELALKILNGQ 255
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
660-811 7.40e-15

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 74.96  E-value: 7.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLTA 738
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTeAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLLTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNRLrevfLKESQ---------------SPAGLSIETKGKVE 803
Cdd:PRK09836  81 LGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAV----IIESQfqvadlmvdlvsrkvTRSGTRITLTSKEF 156

                 ....*...
gi 496047307 804 SLDDLFMR 811
Cdd:PRK09836 157 TLLEFFLR 164
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
660-759 7.88e-15

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: 71.39  E-value: 7.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGNFN---VLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVILL 736
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEPDievVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRR--YPDLKVIVL 78
                         90       100
                 ....*....|....*....|...
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQK 759
Cdd:cd17535   79 TAHDDPEYVLRALKAGAAGYLLK 101
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
362-604 1.05e-14

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 78.19  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 362 INRKVRQNNLLLNERNRLVQQQ-KEELSVANQRI----EQVTTQKL----QFFTNVSHEIKTPLTLI---LGPLNKMAQD 429
Cdd:COG4192  385 IARLLRVFRDQAIEKTQELETEiEERKRIEKNLRqtqdELIQAAKMavvgQTMTSLAHELNQPLNAMsmyLFSAKKALEQ 464
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 430 APAGAFADDIRIVKKNAERLKRVIDQLLDFRKIENNKMGLrvikmdlVFLIQEVKSYFNNLA-QSKRIDYTfLHEMDSLF 508
Cdd:COG4192  465 ENYAQLPTSLDKIEGLIERMDKIIKSLRQFSRKSDTPLQP-------VDLRQVIEQAWELVEsRAKPQQIT-LHIPDDLM 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 509 VWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPpeNLASVFERFFTSGQSyapGTGIGLHL 588
Cdd:COG4192  537 VQGDQVLLEQVLVNLLVNALDAVATQPQISVDLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTTKEV---GLGLGLSI 611
                        250
                 ....*....|....*.
gi 496047307 589 TREFVLMHKGSIHVES 604
Cdd:COG4192  612 CRSIMQQFGGDLYLAS 627
glnL PRK11073
nitrogen regulation protein NR(II);
374-617 1.09e-14

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 76.66  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 374 NERnRLVQQQkeelsvaNQRIEQVTTQKLqfFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFADDIRIVKKNAERLKRVI 453
Cdd:PRK11073 113 NQR-RLSQEQ-------LQHAQQVAARDL--VRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 454 DQLLD-----FRKIEN-NKMGLRV---IKMDLVFLIQEVKSYFNNLAQskridytFLHemdslfvwvDTDKMEKILTNLL 524
Cdd:PRK11073 183 DRLLGpqrpgTHVTESiHKVAERVvqlVSLELPDNVRLIRDYDPSLPE-------LAH---------DPDQIEQVLLNIV 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 525 SNAFK-FTPEQGKITIRLRE--------EETEVV--LSVEDNGEGIPPENLASVFERFfTSGQSyaPGTGIGLHLTREFV 593
Cdd:PRK11073 247 RNALQaLGPEGGTITLRTRTafqltlhgERYRLAarIDIEDNGPGIPPHLQDTLFYPM-VSGRE--GGTGLGLSIARNLI 323
                        250       260
                 ....*....|....*....|....
gi 496047307 594 LMHKGSIHVESEQGeRTVFTVQIP 617
Cdd:PRK11073 324 DQHSGKIEFTSWPG-HTEFSVYLP 346
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
31-245 1.26e-14

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: 74.98  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  31 IGVSQCSMTDIWRQSMIRDMEVEAlNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIIssNETEPVTP-VAVEAYRA 109
Cdd:cd01537    2 IGVTIYSYDDNFMSVIRKAIEQDA-KQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAI--NLVDPAAAgVAEKARGQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 GIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEiwGRRGSSSATERHQGFVDAMSiDPNVKIREL- 188
Cdd:cd01537   79 NVPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLK--GPLGHPDAEARLAGVIKELN-DKGIKTEQLq 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 189 --DGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd01537  156 ldTGDWDTASGKDKMDQwLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYD 215
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
45-231 2.56e-14

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: 74.09  E-value: 2.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  45 SMIRDMEVEALNHpEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEpvtpvaVEAY-RAGIPTIILDRKINsd 123
Cdd:cd06291   16 ELAKYIEKELFKK-GYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLD------IEEYkKLNIPIVSIDRYLS-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 124 EYTTYIGADNYEIGRSIGMYvssLIKKETT-ILEIWGRRGSSSATERHQGFVDAMSiDPNVKIRELDGYWYRKN---AYE 199
Cdd:cd06291   87 EGIPSVSSDNYQGGRLAAEH---LIEKGCKkILHIGGPSNNSPANERYRGFEDALK-EAGIEYEIIEIDENDFSeedAYE 162
                        170       180       190
                 ....*....|....*....|....*....|...
gi 496047307 200 EVLK-LDSIEDVDIVFAHNDMMALGAREAIEER 231
Cdd:cd06291  163 LAKElLEKYPDIDGIFASNDLLAIGVLKALQKL 195
PRK11173 PRK11173
two-component response regulator; Provisional
660-762 2.65e-14

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 73.51  E-value: 2.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQH--ELSGnFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCR--RVKSDMALshipvIL 735
Cdd:PRK11173   6 ILIVEDELVTRNTLKSifEAEG-YDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARelREQANVAL-----MF 79
                         90       100
                 ....*....|....*....|....*..
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:PRK11173  80 LTGRDNEVDKILGLEIGADDYITKPFN 106
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
392-598 3.89e-14

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 75.00  E-value: 3.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 392 QRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFADDIRIvkknaERLKRVIDQLLDFRKIENN-KMGLr 470
Cdd:PRK10755 128 SRLTSTLDQERLFTADVAHELRTPLAGIRLHLELLEKQHHIDVAPLIARL-----DQMMHTVEQLLQLARAGQSfSSGH- 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 471 vikMDLVFLIQEV----KSYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTPEQGKITIRLREEET 546
Cdd:PRK10755 202 ---YQTVKLLEDVilpsQDELSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTITIKLSQEDG 278
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496047307 547 EVVLSVEDNGEGIPPENLASVFERFFTSGQSYApGTGIGLHLTREFVLMHKG 598
Cdd:PRK10755 279 GAVLAVEDEGPGIDESKCGELSKAFVRMDSRYG-GIGLGLSIVSRITQLHHG 329
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
659-791 4.02e-14

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 72.80  E-value: 4.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRA----YLQhelSGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmaLSHIPVI 734
Cdd:PRK10710  12 RILIVEDEPKLGQllidYLQ---AASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR---FSDIPIV 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496047307 735 LLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNRLREVFLKESQSP 791
Cdd:PRK10710  86 MVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESP 142
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
519-624 6.37e-14

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 75.33  E-value: 6.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 519 ILTNLLSNAFKFTPEQ--GKITIRLREEETEVVLSVEDNGEGIPPENLASVFER-FFTSGqsyaPGTGIGLHLTREFVLM 595
Cdd:PRK11086 437 ILGNLIENALEAVGGEegGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKgYSTKG----SNRGVGLYLVKQSVEN 512
                         90       100
                 ....*....|....*....|....*....
gi 496047307 596 HKGSIHVESEQGERTVFTVQIPKGKSHFD 624
Cdd:PRK11086 513 LGGSIAVESEPGVGTQFFVQIPWDGERSN 541
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
58-286 7.62e-14

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: 73.09  E-value: 7.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  58 PEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIG 137
Cdd:cd19995   31 PDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNVAVG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 138 RSIGMYVSSLIKKETT----ILEIWGRRGSSSATERHQGfvdAMS-IDPNVKIREL----DGY---WYRKNA---YEEVL 202
Cdd:cd19995  111 EAQAQSLVDHLKAIGKkgvnIVMINGSPTDNNAGLFKKG---AHEvLDPLGDSGELklvcEYDtpdWDPANAqtaMEQAL 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 203 -KLDSieDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGGLGVEAVAQGKLDASFY--YPTGGGVAIKVA 279
Cdd:cd19995  188 tKLGN--NIDGVLSANDGLAGGAIAALKAQG--LAGKVPVTGQD---ATVAGLQRILAGDQYMTVYkpIKKEAAAAAKVA 260

                 ....*..
gi 496047307 280 WQILSGQ 286
Cdd:cd19995  261 VALLKGE 267
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
660-770 1.02e-13

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: 68.20  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdMALSHIPVILLTA 738
Cdd:cd17616    1 VLLIEDDSATAQSIELMLkSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLR--LAKVKTPILILSG 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRI 770
Cdd:cd17616   79 LADIEDKVKGLGFGADDYMTKPFHKDELVARI 110
PRK10610 PRK10610
chemotaxis protein CheY;
657-776 1.04e-13

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 68.85  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 657 DYTILIVEDDWDIRAYLQHELS--GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVI 734
Cdd:PRK10610   5 ELKFLVVDDFSTMRRIVRNLLKelGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVL 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 496047307 735 LLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEE 776
Cdd:PRK10610  85 MVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
envZ PRK09467
osmolarity sensor protein; Provisional
408-607 1.14e-13

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 74.18  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 408 VSHEIKTPLTLILGPLNKMAQDApaGAFADDIrivKKNAERLKRVIDQLLDFRKiENNKMGLRVIkmDLVFLIQEVKSyf 487
Cdd:PRK09467 236 VSHDLRTPLTRIRLATEMMSEED--GYLAESI---NKDIEECNAIIEQFIDYLR-TGQEMPMEMA--DLNALLGEVIA-- 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 488 nnlAQSKR---IDYTFLHEMDSlfVWVDTDKMEKILTNLLSNAFKFTpeQGKITIRLREEETEVVLSVEDNGEGIPPENL 564
Cdd:PRK09467 306 ---AESGYereIETALQPGPIE--VPMNPIAIKRALANLVVNAARYG--NGWIKVSSGTEGKRAWFQVEDDGPGIPPEQL 378
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 496047307 565 ASVFERfFTSGQSY--APGTGIGLHLTREFVLMHKGSIHV-ESEQG 607
Cdd:PRK09467 379 KHLFQP-FTRGDSArgSSGTGLGLAIVKRIVDQHNGKVELgNSEEG 423
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
62-237 1.94e-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: 71.41  E-value: 1.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  62 LVVMDAIQDNDTQISQIKGFikkKVDLLIISSneTEPVTPVAVEAYRAGIPTIILDRKInSDEYTTYIGADNYEIGRSIG 141
Cdd:cd06278   34 LFNVDDEDDVDDALRQLLQY---RVDGVIVTS--ATLSSELAEECARRGIPVVLFNRVV-EDPGVDSVSCDNRAGGRLAA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 142 MYvssLIKKE-TTILEIWGRRGSSSATERHQGFVDAMS---IDPnvkIRELDGYWYRKNAYEEVLKL-DSIEDVDIVFAH 216
Cdd:cd06278  108 DL---LLAAGhRRIAFLGGPEGTSTSRERERGFRAALAelgLPP---PAVEAGDYSYEGGYEAARRLlAAPDRPDAIFCA 181
                        170       180
                 ....*....|....*....|....*...
gi 496047307 217 NDMMALGAREAIEER-------DSSLVG 237
Cdd:cd06278  182 NDLMALGALDAARQEgglvvpeDISVVG 209
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
60-299 1.95e-13

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: 71.46  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  60 IELVVMDA--IQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIG 137
Cdd:cd06306   30 VKLTVYEAggYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAARVLVDFYDMG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 138 RSIGMY-VSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSiDPNVKIRELDgywYRKNAYEEVLKLdsIEDV-----D 211
Cdd:cd06306  110 YLAGEYlVEHHPGKPVKVAWFPGPAGAGWAEDREKGFKEALA-GSNVEIVATK---YGDTGKAVQLNL--VEDAlqahpD 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 212 I-VFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGGLGVEAVAQGKLDASFYYPT--GGGVAIKVAWQILSGQAY 288
Cdd:cd06306  184 IdYIVGNAVAAEAAVGALREAG--LTGKVKVVSTY---LTPGVYRGIKRGKILAAPSDQPvlQGRIAVDQAVRALEGKPV 258
                        250
                 ....*....|.
gi 496047307 289 TKKYALSTAMI 299
Cdd:cd06306  259 PKHVGPPILVV 269
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
660-771 2.21e-13

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: 67.27  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILL--KENVSLVVSDVMMPEMNGFELCRRVKSDMalsHIPVILL 736
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRcGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFNIEivKLRII 771
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVSIE--DLKNI 110
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
38-230 2.32e-13

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: 71.50  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  38 MTDIWRQSMIRDMEvEALNHPEIELV-VMDAIQDNDTQISQIKGFIKKKVDLLIissneTEPVTPVAV-EAYR----AGI 111
Cdd:cd06316    9 TGSDWSRLQVAGIK-DTFEELGIEVVaVTDANFDPAKQITDLETLIALKPDIII-----SIPVDPVATaAAYKkvadAGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 112 PTIILDRKIN----SDEYTTYIGADNYEIGRSIGMYVSSLIKKETTILEI------WgrrgsssAT-ERHQGFVDAMSID 180
Cdd:cd06316   83 KLVFMDNVPDgleaGKDYVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIyhdadfY-------ATnQRDKAFKDTLKEK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496047307 181 -PNVKIRELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEE 230
Cdd:cd06316  156 yPDIKIVAEQGFADPNDAEEVASAmLTANPDIDGIYVSWDTPALGVISALRA 207
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
660-767 2.82e-13

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: 67.39  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKE-----------NVSLVVSDVMMPEMNGFELCRRVKSDMA 727
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLrISSCRVTAVDSGKRALEFLGLEdeedssnfnepKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 496047307 728 LSHIPVILLTalSDD-SQRLYG-FEGGADEYIQKPFNIEIVK 767
Cdd:cd17581   81 LKEIPVVIMS--SENiPTRISRcLEEGAEDFLLKPVKLADVK 120
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
659-760 3.83e-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: 66.84  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDD----WDIRAYLqhELSGnFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVI 734
Cdd:cd17555    2 TILVIDDDevvrESIAAYL--EDSG-FQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVI 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 496047307 735 LLTA---LSDDSQ--RLygfegGADEYIQKP 760
Cdd:cd17555   77 VVSGagvMSDAVEalRL-----GAWDYLTKP 102
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
31-230 3.94e-13

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: 70.79  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  31 IGVSQCSMTDIWRQSMIRDM--EVEALNhpeIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYR 108
Cdd:cd06305    2 IAVVRNGTSGDWDQQALQGAvaEAEKLG---GTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 109 AGIPTIILDRKINSDEyTTYIGADNYEIGRSIGMYVSSLIKKETTILEIWGrRGSSSATERHQGFVDAMSIDPNVKIRE- 187
Cdd:cd06305   79 AGIPVVTFDTDSQVPG-VNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNV-FGVPPLDKRYDIYKAVLKANPGIKKIVa 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496047307 188 ----------LDGYwyrkNAYEEVLKLDSIEDVDIVFAHNDMMALGAREAIEE 230
Cdd:cd06305  157 elgdvtpntaADAQ----TQVEALLKKYPEGGIDAIWAAWDEPAKGAVQALEE 205
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
660-775 4.59e-13

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 66.37  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILL-- 736
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDeGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE--KYPDLPVIMIsg 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496047307 737 -----TALSddSQRLygfegGADEYIQKPFNIEIVKLRIIKLLE 775
Cdd:cd17550   79 hgtieTAVK--ATKL-----GAYDFIEKPLSLDRLLLTIERALE 115
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-617 5.29e-13

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


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 65.87  E-value: 5.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQS-YAPGTGIGLHLTREFVL 594
Cdd:cd16923    1 LQRVFSNLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSrNTEGAGLGLSIAKAIIE 80
                         90       100
                 ....*....|....*....|...
gi 496047307 595 MHKGSIHVESeQGERTVFTVQIP 617
Cdd:cd16923   81 LHGGSASAEY-DDNHDLFKVRLP 102
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
488-607 6.80e-13

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: 66.50  E-value: 6.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 488 NNLAQSKRIDYTFLHEMDSLFVWVDTDKMEkILTNLLSNAFKFTPEQgkITIRLREEETEVVLSVEDNGEGIPPENLASV 567
Cdd:cd16954   11 NKVYQRKGVSISLDISPELRFPGERNDLME-LLGNLLDNACKWCLEF--VEVTARQTDGGLHLIVDDDGPGVPESQRSKI 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496047307 568 FERfftsGQ---SYAPGTGIGLHLTREFVLMHKGSIHVE-SEQG 607
Cdd:cd16954   88 FQR----GQrldEQRPGQGLGLAIAKEIVEQYGGELSLSdSPLG 127
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
658-759 7.46e-13

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 69.28  E-value: 7.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWD----IRAYL-QHELsgnfNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALshiP 732
Cdd:PRK10701   2 NKIVFVEDDAEvgslIAAYLaKHDI----DVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG---P 74
                         90       100
                 ....*....|....*....|....*..
gi 496047307 733 VILLTALSDDSQRLYGFEGGADEYIQK 759
Cdd:PRK10701  75 IVLLTSLDSDMNHILALEMGACDYILK 101
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
659-761 8.15e-13

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 65.22  E-value: 8.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKE-NVSLVVSDVMMPEMNGFELCRRV-KSDMAlshIPVIL 735
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLkKAGYAVTEAESGAEALEKLQQGkDIDIVVTDIVMPEMDGIELAREArKIDPD---VKILF 77
                         90       100
                 ....*....|....*....|....*.
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPF 761
Cdd:cd18160   78 ISGGAAAAPELLSDAVGDNATLKKPF 103
PRK10337 PRK10337
sensor protein QseC; Provisional
392-596 1.28e-12

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 70.83  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 392 QRIEQVTTQKLQFFTNVSHEIKTPLTL--ILGPLNKMAQDAPAG---AFADdiriVKKNAERLKRVIDQLLDFRKIENnk 466
Cdd:PRK10337 228 ARTHAMMVRERRFTSDAAHELRSPLAAlkVQTEVAQLSDDDPQArkkALLQ----LHAGIDRATRLVDQLLTLSRLDS-- 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 467 mglrvikMDLVFLIQEVKsyFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEKILT-----------NLLSNAFKFTPEQG 535
Cdd:PRK10337 302 -------LDNLQDVAEIP--LEDLLQSAVMDIYHTAQQAGIDVRLTLNAHPVIRTgqplllsllvrNLLDNAIRYSPQGS 372
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496047307 536 KITIRLreeeTEVVLSVEDNGEGIPPENLASVFERFF-TSGQSyAPGTGIGLHLTREFVLMH 596
Cdd:PRK10337 373 VVDVTL----NARNFTVRDNGPGVTPEALARIGERFYrPPGQE-ATGSGLGLSIVRRIAKLH 429
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
516-617 1.49e-12

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


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 65.09  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEQGKITIRLREEETE---------------VVLSVEDNGEGIPPENLASVFERFFTSgQSYAP 580
Cdd:cd16919    1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDadyalnyrdlipgnyVCLEVSDTGSGMPAEVLRRAFEPFFTT-KEVGK 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496047307 581 GTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:cd16919   80 GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
807-906 2.14e-12

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 68.55  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 807 DLFMRKFIALIEENYSDpDFSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGF 886
Cdd:PRK13503 170 DARLNQLLAWLEDHFAE-EVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGF 248
                         90       100
                 ....*....|....*....|
gi 496047307 887 GSPAYFSKCFKAVYNITPTE 906
Cdd:PRK13503 249 GDSNHFSTLFRREFSWSPRD 268
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
658-783 2.36e-12

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 70.26  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVILL 736
Cdd:PRK11361   5 NRILIVDDEDNVRRMLSTAFAlQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHE--TRTPVILM 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERNRLREV 783
Cdd:PRK11361  83 TAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEI 129
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
660-797 2.82e-12

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 67.44  E-value: 2.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLTA 738
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNgFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEernRLREVFLKESQSPAGLSIE 797
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR---RISPMAVEEVIEMQGLSLD 140
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
441-620 2.95e-12

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 69.66  E-value: 2.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 441 IVKKNAERLKRVIDQLLD-FRK-IENNKmglrvikmDLVFL---IQEVKSYFN--NLAQSKRIDYTFlhEMDslfvwvDT 513
Cdd:COG2972  267 AELEDPEEAEEMLEALSKlLRYsLSKGD--------ELVTLeeeLELIKSYLEiqKLRFGDRLEVEI--EID------EE 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 514 DKMEKILTNLLS----NAFKF----TPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQsyapGTGIG 585
Cdd:COG2972  331 LLDLLIPKLILQplveNAIEHgiepKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKGE----GRGIG 406
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 496047307 586 LHLTREFVLMH---KGSIHVESEQGERTVFTVQIPKGK 620
Cdd:COG2972  407 LRNVRERLKLYygeEYGLEIESEPGEGTTVTIRIPLEE 444
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
659-770 3.62e-12

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 63.62  E-value: 3.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHIPVILLT 737
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERgFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR---SDVPIIIIS 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 496047307 738 ALSDD-SQRLYGFEGGADEYIQKPFNIEIVKLRI 770
Cdd:cd17594   78 GDRRDeIDRVVGLELGADDYLAKPFGLRELLARV 111
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
70-238 3.66e-12

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: 67.59  E-value: 3.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISsnetePV---TPVAVEAY-RAGIPTIILDRKInSDEYTTYIGADNYEIGRsigMYVS 145
Cdd:cd06289   40 DPERQRRFLRRMLEQGVDGLILS-----PAagtTAELLRRLkAWGIPVVLALRDV-PGSDLDYVGIDNRLGAQ---LATE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 146 SLIKK-ETTILEIWGRRGSSSATERHQGFVDAMSidpNVKIRELDGYWY-----RKNAYEEVLK-LDSIEDVDIVFAHND 218
Cdd:cd06289  111 HLIALgHRRIAFLGGLSDSSTRRERLAGFRAALA---EAGLPLDESLIVpgpatREAGAEAARElLDAAPPPTAVVCFND 187
                        170       180
                 ....*....|....*....|....*.
gi 496047307 219 MMALGAREAIEE------RDSSLVGH 238
Cdd:cd06289  188 LVALGAMLALRRrglepgRDIAVVGF 213
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
680-760 4.38e-12

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: 63.16  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 680 NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLTALSDDSQRLYGFEGGADEYIQK 759
Cdd:cd17602   22 GFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGLVDRIRAKMAGASGYLTK 101

                 .
gi 496047307 760 P 760
Cdd:cd17602  102 P 102
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-607 4.51e-12

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 63.22  E-value: 4.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTPEQGKITIRLREEEteVVLSVEDNGEGIPPENLASVFERFF---TSGQSYAPGTGIGLHLTREF 592
Cdd:cd16939    1 MARALDNLLRNALRYAHRTVRIALLVSGGR--LTLIVEDDGPGIPAAARERVFEPFVrldPSRDRATGGFGLGLAIVHRV 78
                         90
                 ....*....|....*.
gi 496047307 593 VLMHKGSIHV-ESEQG 607
Cdd:cd16939   79 ALWHGGHVECdDSELG 94
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
660-809 5.51e-12

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 69.13  E-value: 5.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALshIPVILLTA 738
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGaGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTA 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNI-EIVKL--RIIKLLEERNRLRevflkeSQSPAGLSIETKGKVESLDDLF 809
Cdd:PRK10923  84 HSDLDAAVSAYQQGAFDYLPKPFDIdEAVALveRAISHYQEQQQPR------NIQVNGPTTDIIGEAPAMQDVF 151
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
30-279 6.77e-12

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: 67.12  E-value: 6.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTD----IWRQSMirdmeVEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVE 105
Cdd:cd19993    1 VVGVSWSNFQEerwkTDEAAM-----KKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 106 AYRAGIPTIILDRKI-NSDEYttYIGADNYEIGRSIGMYVSSLiKKETTILEIwgrRGSSSATERH----------QGFV 174
Cdd:cd19993   76 AAAEGIPVIAYDRLIeNPIAF--YISFDNVEVGRMQARGVLKA-KPEGNYVFI---KGSPTDPNADflragqmevlQPAI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 175 DAMSIDpNVKIRELDGyWYRKNA---YEEVLKLDSiEDVDIVFAHNDMMALGAREAIEERDssLVGHVEFIGVDgllGGG 251
Cdd:cd19993  150 DSGKIK-IVGEQYTDG-WKPANAqknMEQILTANN-NKVDAVVASNDGTAGGAVAALAAQG--LAGKVPVSGQD---ADK 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 496047307 252 LGVEAVAQGKL------DASFYYPTGGGVAIKVA 279
Cdd:cd19993  222 AALNRIALGTQtvtvwkDARELGKEAAEIAVELA 255
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
520-600 9.88e-12

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: 62.34  E-value: 9.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 520 LTNLLSNAFKFTPEqgKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSY---APGTGIGLHLTREFVLMH 596
Cdd:cd16949    5 LENVLRNALRYSPS--KILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARdreSGGTGLGLAIAERAIEQH 82

                 ....
gi 496047307 597 KGSI 600
Cdd:cd16949   83 GGKI 86
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
59-245 1.12e-11

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: 66.50  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  59 EIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGR 138
Cdd:cd20005   31 KITFEGPDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSDLPLATVATDNYAAGA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 139 SIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSID-PNVKIRELDgywYRKNAyeEVLKLDSIEDV-----DI 212
Cdd:cd20005  111 LAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKyPDIKVVNVQ---YGVGD--HAKAADIAKAIlqanpDL 185
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 496047307 213 --VFAHNDMMALGAREAIEERdsSLVGHVEFIGVD 245
Cdd:cd20005  186 kgIYATNEGAAIGVANALKEM--GKLGKIKVVGFD 218
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-607 1.58e-11

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: 61.70  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 516 MEKILTNLLSNAFKFTpeQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFeRFFTSGQSY--APGTGIGLHLTREFV 593
Cdd:cd16950    1 LKRVLSNLVDNALRYG--GGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELF-QPFYRGDNArgTSGTGLGLAIVQRIS 77
                         90
                 ....*....|....
gi 496047307 594 LMHKGSIHVESEQG 607
Cdd:cd16950   78 DAHGGSLTLANRAG 91
PRK11517 PRK11517
DNA-binding response regulator HprR;
660-762 1.69e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 64.92  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmaLSHIPVILLTA 738
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSeAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRT---AKQTPVICLTA 79
                         90       100
                 ....*....|....*....|....
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:PRK11517  80 RDSVDDRVRGLDSGANDYLVKPFS 103
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
658-762 1.76e-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: 61.84  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILL 736
Cdd:cd17537    1 ATVYVVDDDEAVRDSLAFLLRSVgLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLA--RGSNIPIIFI 78
                         90       100
                 ....*....|....*....|....*.
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPFN 762
Cdd:cd17537   79 TGHGDVPMAVEAMKAGAVDFLEKPFR 104
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
46-237 2.13e-11

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: 65.35  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  46 MIRDMEvEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSnETEPVTPVAVEAYRAGIPTIILDRKINSDEY 125
Cdd:cd19976   17 LVRGIE-DTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIAS-SNISDEAIIKLLKEEKIPVVVLDRYIEDNDS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 126 TtYIGADNYEigrsiGMYVSS--LIKK-ETTILEIWGRRGSSSATERHQGFVDAMSiDPNVKIRELDGYWYRKN---AYE 199
Cdd:cd19976   95 D-SVGVDDYR-----GGYEATkyLIELgHTRIGCIVGPPSTYNEHERIEGYKNALQ-DHNLPIDESWIYSGESSlegGYK 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 496047307 200 EVLKLDSIEDVDIVFAHNDMMALGAREAIEER------DSSLVG 237
Cdd:cd19976  168 AAEELLKSKNPTAIFAGNDLIAMGVYRAALELglkipeDLSVIG 211
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
400-465 2.39e-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: 59.92  E-value: 2.39e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496047307  400 QKLQFFTNVSHEIKTPLTLILGPLnKMAQDAPAGA-FADDIRIVKKNAERLKRVIDQLLDFRKIENN 465
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYL-ELLRDEKLDEeQREYLETILRSAERLLRLINDLLDLSRIEAG 66
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
658-782 2.56e-11

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: 63.82  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHEL--SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMAlshIPVIL 735
Cdd:COG3707    4 LRVLVVDDEPLRRADLREGLreAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APVIL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFNIEIVK----------LRIIKLLEERNRLRE 782
Cdd:COG3707   81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLpalelalarfRELRALRRELAKLRE 137
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
658-774 4.42e-11

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: 60.76  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHELS-GNFNVLV-AENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmaLSHIPVIL 735
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTkAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKI--DPNAKVIM 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd17542   79 CSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
70-237 4.88e-11

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: 64.20  E-value: 4.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVD-LLIISSNETEPVTPVaVEAYRAgIPTIILDRKINSDeYTTYIGADNYEIGRSIGMYVSSLI 148
Cdd:cd06275   40 DPEKQRAYLDMLAEKRVDgLLLMCSEMTDDDAEL-LAALRS-IPVVVLDREIAGD-NADAVLDDSFQGGYLATRHLIELG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 149 KKEttILEIWGRRGSSSATERHQGFVDAMSiDPNVKIRE---LDGYWYRKNAYEEVLKLDSIE-DVDIVFAHNDMMALGA 224
Cdd:cd06275  117 HRR--IGCITGPLEHSVSRERLAGFRRALA-EAGIEVPPswiVEGDFEPEGGYEAMQRLLSQPpRPTAVFACNDMMALGA 193
                        170
                 ....*....|....*....
gi 496047307 225 REAIEER------DSSLVG 237
Cdd:cd06275  194 LRAAQEQglrvpqDISIIG 212
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
659-763 6.28e-11

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 63.28  E-value: 6.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmaLSHIPVILLT 737
Cdd:PRK10529   3 NVLIVEDEQAIRRFLRTALEGDgMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQ---WSAIPVIVLS 79
                         90       100
                 ....*....|....*....|....*.
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNI 763
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSKPFGI 105
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
660-760 6.40e-11

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: 59.98  E-value: 6.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGNFN---VLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVILL 736
Cdd:cd17565    1 FYIVDDDKNIIKILSDIIEDDDLgevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTG--SNGKFIMI 78
                         90       100
                 ....*....|....*....|....
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd17565   79 SQVSDKEMIGKAYQAGIEFFINKP 102
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
61-230 7.81e-11

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: 64.19  E-value: 7.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  61 ELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKI-NSDEYTTYIGADNYEIGRS 139
Cdd:cd19994   31 TVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYDRLImNTDAVDYYVTFDNEKVGEL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 140 IGMYVSS---LIKKETTI-LEIWGrrGSSS----------ATERHQGFVDA---------MSIDpnvKIRELDgyWYRKN 196
Cdd:cd19994  111 QGQYLVDklgLKDGKGPFnIELFA--GSPDdnnaqlffkgAMEVLQPYIDDgtlvvrsgqTTFE---QVATPD--WDTET 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 496047307 197 AYEevlKLDSI--------EDVDIVFAHNDMMALGAREAIEE 230
Cdd:cd19994  184 AQA---RMETLlsayytggKKLDAVLSPNDGIARGVIEALKA 222
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
81-238 7.86e-11

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: 63.72  E-value: 7.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  81 FIKKKVDLLIISSNETEPVTPVAVEAyraGIPTIILDRkINSDEYTTYIGADNYEIGRSIgmyVSSLIKKETT-ILEIWG 159
Cdd:cd06288   52 LLSRRVDGIIYASMHHREVTLPPELT---DIPLVLLNC-FDDDPSLPSVVPDDEQGGYLA---TRHLIEAGHRrIAFIGG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 160 RRGSSSATERHQGFVDAM-----SIDPNvkiRELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEER-- 231
Cdd:cd06288  125 PEDSLATRLRLAGYRAALaeagiPYDPS---LVVHGDWGRESGYEAAKRlLSAPDRPTAIFCGNDRMAMGVYQAAAELgl 201
                        170
                 ....*....|.
gi 496047307 232 ----DSSLVGH 238
Cdd:cd06288  202 rvpeDLSVVGF 212
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
86-245 9.07e-11

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: 63.37  E-value: 9.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  86 VDLLIISSNeTEPVTPVAVEAyRAGIPTIILDRkiNSDEYTTYIGADNYEIGRSIGMYvssLIkkE---TTILEIWGRRG 162
Cdd:cd01574   57 VDGIIVIAP-DEAVLEALRRL-PPGLPVVIVGS--GPSPGVPTVSIDQEEGARLATRH---LL--ElghRRIAHIAGPLD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 163 SSSATERHQGFVDAM---SIDPnVKIRELDgyWYRKNAYEEVLKLDSIEDVDIVFAHNDMMALGAREAIEERDSSLVGHV 239
Cdd:cd01574  128 WVDARARLRGWREALeeaGLPP-PPVVEGD--WSAASGYRAGRRLLDDGPVTAVFAANDQMALGALRALHERGLRVPEDV 204

                 ....*.
gi 496047307 240 EFIGVD 245
Cdd:cd01574  205 SVVGFD 210
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
660-760 1.05e-10

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: 60.10  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELS--GNFNVL-VAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVksdMALSHIPVILL 736
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILEsdPDIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRI---MAERPTPVVMV 79
                         90       100
                 ....*....|....*....|....*..
gi 496047307 737 TALSDDSQRLyGFEG---GADEYIQKP 760
Cdd:cd17541   80 SSLTEEGAEI-TLEAlelGAVDFIAKP 105
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
512-617 1.26e-10

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: 59.09  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 512 DTDKMEKILTNLLSNAFKFTPEQ--GKITIRLREE---ETEVVLSVEDNGEGIPPENLASVFERFFTSGqsyAPGTGIGL 586
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEGRpsDVGEVRIRVEadqDGRIVLIVCDNGKGFPREMRHRATEPYVTTR---PKGTGLGL 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 496047307 587 HLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:cd16944   78 AIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
660-778 1.31e-10

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: 59.52  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalsHIP--VILL 736
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSdEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQER----SLPtsVIVI 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 496047307 737 TA-----LSDDSQRLygfegGADEYIQKPFNIEIVKLRIIKLLEERN 778
Cdd:cd17572   77 TAhgsvdIAVEAMRL-----GAYDFLEKPFDADRLRVTVRNALKHRK 118
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
400-465 1.34e-10

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 57.58  E-value: 1.34e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496047307   400 QKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAGAFADDIRIVKKNAERLKRVIDQLLDFRKIENN 465
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
512-616 1.77e-10

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: 58.63  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 512 DTDKMEKILTNLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSYAPGT--GIGLHLT 589
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGhyGMGLYIA 80
                         90       100
                 ....*....|....*....|....*..
gi 496047307 590 REFVLMHKGSIHVESEQGERTVFTVQI 616
Cdd:cd16975   81 KNLVEKHGGSLIIENSQKGGAEVTVKI 107
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
511-624 1.78e-10

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 64.47  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 511 VDTDKMEKILTNLLSNAFKF---TPEQGK-ITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQSYAPGTGIGL 586
Cdd:PRK15053 428 LDSTEFAAIVGNLLDNAFEAslrSDEGNKiVELFLSDEGDDVVIEVADQGCGVPESLRDKIFEQGVSTRADEPGEHGIGL 507
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 496047307 587 HLTREFVLMHKGSIHVESEQGERTVFTVQIPKGKSHFD 624
Cdd:PRK15053 508 YLIASYVTRCGGVITLEDNDPCGTLFSIFIPKVKPNDS 545
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
660-770 1.79e-10

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: 58.98  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAEN---GAKALDIllkENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVIL 735
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKgYQADVAESlkdGEYYIDI---RNYDLVLVSDKLPDGNGLSIVSRIKEKH--PSIVVIV 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRI 770
Cdd:cd17573   76 LSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
660-782 2.21e-10

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 58.70  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIR---AYLQHELSGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmaLSHIP-VIL 735
Cdd:cd17532    1 ALIVDDEPLAReelRYLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSK---LAKPPlIVF 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 496047307 736 LTALsdDSQRLYGFEGGADEYIQKPFNIEivklRIIKLLeerNRLRE 782
Cdd:cd17532   78 VTAY--DEYAVEAFELNAVDYLLKPFSEE----RLAEAL---AKLRK 115
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
42-215 2.83e-10

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: 62.31  E-value: 2.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  42 WRQSMIRDMEVEALNHP---EIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDR 118
Cdd:cd19998   13 WRQEMINIAKAAAKQPPyadKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 119 KINSDE-YTtyIGADNYEIGRSIGMYVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKI-RELDGYWYRKN 196
Cdd:cd19998   93 VVDEPCaYN--VNTDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEVFKKYPDIKVvAEYYGNWDDGT 170
                        170       180
                 ....*....|....*....|
gi 496047307 197 AYEEVLK-LDSIEDVDIVFA 215
Cdd:cd19998  171 AQKAVADaLAAHPDVDGVWT 190
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
659-764 3.23e-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: 59.93  E-value: 3.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLT 737
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERrGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE--RDPDARIVVLT 83
                         90       100
                 ....*....|....*....|....*..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIE 764
Cdd:COG4567   84 GYASIATAVEAIKLGADDYLAKPADAD 110
PRK10643 PRK10643
two-component system response regulator PmrA;
660-778 4.39e-10

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 60.82  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRV-KSDMALshiPVILLT 737
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTeGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWrQKKYTL---PVLILT 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERN 778
Cdd:PRK10643  80 ARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQ 120
fixJ PRK09390
response regulator FixJ; Provisional
657-775 5.11e-10

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 60.02  E-value: 5.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 657 DYTILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVIL 735
Cdd:PRK09390   3 KGVVHVVDDDEAMRDSLAFLLdSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARG--SPLPVIV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFNIEivklRIIKLLE 775
Cdd:PRK09390  81 MTGHGDVPLAVEAMKLGAVDFIEKPFEDE----RLIGAIE 116
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
660-778 7.68e-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: 60.58  E-value: 7.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  660 ILIVEDDWDIRAYLQHELSG--NFNVL-VAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdMALSHIP-VIL 735
Cdd:TIGR02875   5 IVIADDNKEFCNLLKEYLAAqpDMEVVgVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNE-IELSARPrVIM 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 496047307  736 LTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEERN 778
Cdd:TIGR02875  84 LSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQLAWGTN 126
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
475-617 7.73e-10

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 62.23  E-value: 7.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 475 DLVFLIQEVKSYFNNLAQSKRIDYtflhEMDSLFVWVDTDK-----MekILTNLLSNAFKF---TPEQGKITIRLREEET 546
Cdd:COG3920  360 DLRDYLRELLEPLRDSYGGRGIRI----ELDGPDVELPADAavplgL--ILNELVTNALKHaflSGEGGRIRVSWRREDG 433
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496047307 547 EVVLSVEDNGEGIPPenlasvferfftsGQSYAPGTGIGLHLTREFVLMHKGSIHVESEQGerTVFTVQIP 617
Cdd:COG3920  434 RLRLTVSDNGVGLPE-------------DVDPPARKGLGLRLIRALVRQLGGTLELDRPEG--TRVRITFP 489
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
70-228 1.00e-09

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: 60.56  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYT-TYIGADNYEIGRSIGMYV-SSL 147
Cdd:cd19973   42 DNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDTPTDPIDAAdATFATDNFKAGVLIGEWAkAAL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 148 IKKETTILEIWGRRGSSSATERHQGFVDAMSIDPNVKIRELDGYWYR--------------KNAYEEVLKLDSieDVDIV 213
Cdd:cd19973  122 GAKDAKIATLDLTPGHTVGVLRHQGFLKGFGIDEKDPESNEDEDDSQvvgsadtngdqakgQTAMENLLQKDP--DINLV 199
                        170
                 ....*....|....*
gi 496047307 214 FAHNDMMALGAREAI 228
Cdd:cd19973  200 YTINEPAAAGAYQAL 214
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
659-764 1.11e-09

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: 58.96  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLT 737
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLeSAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAA--RGSPLPVIFLT 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496047307 738 AlsddsqrlYG--------FEGGADEYIQKPFNIE 764
Cdd:COG4566   79 G--------HGdvpmavraMKAGAVDFLEKPFDDQ 105
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
658-711 1.23e-09

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 54.50  E-value: 1.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 496047307   658 YTILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMP 711
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKeGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
660-774 1.67e-09

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 61.20  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdmALS-HIPVILLT 737
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK---ALNpAIPVLIMT 84
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:PRK10365  85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
400-461 1.81e-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: 54.53  E-value: 1.81e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047307 400 QKLQFFTNVSHEIKTPLTLILGPLNKMAQDAPAGA-FADDIRIVKKNAERLKRVIDQLLDFRK 461
Cdd:cd00082    3 AKGEFLANVSHELRTPLTAIRGALELLEEELLDDEeQREYLERIREEAERLLRLINDLLDLSR 65
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
660-774 3.27e-09

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 55.64  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdMALSHIPVILLTA 738
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFnKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMK--VIDENIRVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL 774
Cdd:cd17553   81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
522-617 4.46e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 54.74  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 522 NLLSNAFKFTPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQsyapGTGIGL-HLTREFVLMH--KG 598
Cdd:cd16957   12 NAIRHAFPKRKENNEVRVVVKKDQHKVHVSVSDNGQGIPEERLDLLGKTTVTSEK----GTGTALeNLNRRLIGLFgsEA 87
                         90
                 ....*....|....*....
gi 496047307 599 SIHVESEQGERTVFTVQIP 617
Cdd:cd16957   88 CLHIESEVHGGTEVWFVIP 106
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
48-291 4.96e-09

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: 58.04  E-value: 4.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  48 RDMEVEALNHpEIELVVMDAIQDNDTQISQIKGFIKKKVDLLII--SSNETEPVtpvaVEAYRAGIPTIILDRKINSDEY 125
Cdd:cd06280   19 RGIEDAAEKH-GYQVILANTDEDPEKEKRYLDSLLSKQVDGIILapSAGPSREL----KRLLKHGIPIVLIDREVEGLEL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 126 TTyIGADNYEIGRSIGMYVSSLIKKETTIleIWGRRGSSSATERHQGFVDAMSiDPNVKIRE---LDGYWYRKNAYEEVL 202
Cdd:cd06280   94 DL-VAGDNREGAYKAVKHLIELGHRRIGL--ITGPLEISTTRERLAGYREALA-EAGIPVDEsliFEGDSTIEGGYEAVK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 203 KL-DSIEDVDIVFAHNDMMALGAREAIEER------DSSLVGhveFIGVDGLLGGGLGVEAVAQgkldASFYYptgGGVA 275
Cdd:cd06280  170 ALlDLPPRPTAIFATNNLMAVGALRALRERgleipqDISVVG---FDDSDWFEIVDPPLTVVAQ----PAYEI---GRIA 239
                        250
                 ....*....|....*.
gi 496047307 276 IKVAWQILSGQAYTKK 291
Cdd:cd06280  240 AQLLLERIEGQGEEPR 255
PRK15115 PRK15115
response regulator GlrR; Provisional
660-738 5.83e-09

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 59.47  E-value: 5.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFEL---CRRVKSDMalshiPVIL 735
Cdd:PRK15115   8 LLLVDDDPGLLKLLGMRLtSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLfaeIQKVQPGM-----PVII 82

                 ...
gi 496047307 736 LTA 738
Cdd:PRK15115  83 LTA 85
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
660-761 6.98e-09

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 53.89  E-value: 6.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIR---AYLQHELSgnFNVLVAENGAKALDILlKEN--VSLVVSDVMMP-EMNGFELCRRVKSdmALSHIPV 733
Cdd:cd18161    1 VLVVEDDPDVRrltAEVLEDLG--YTVLEAASGDEALDLL-ESGpdIDLLVTDVIMPgGMNGSQLAEEARR--RRPDLKV 75
                         90       100
                 ....*....|....*....|....*...
gi 496047307 734 ILLTALSDDSQRLYGFEGGADeYIQKPF 761
Cdd:cd18161   76 LLTSGYAENAIEGGDLAPGVD-VLSKPF 102
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
659-760 9.17e-09

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: 54.68  E-value: 9.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdmALSHIPV-ILLT 737
Cdd:cd17596    2 TILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVR---ERWPEVVrIIIS 78
                         90       100
                 ....*....|....*....|....
gi 496047307 738 ALSDDSQRLYGF-EGGADEYIQKP 760
Cdd:cd17596   79 GYTDSEDIIAGInEAGIYQYLTKP 102
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
74-265 9.86e-09

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: 57.35  E-value: 9.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  74 QISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLI--KKE 151
Cdd:cd19969   45 QITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLggKGK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 152 TTILEIwgrRGSSSATERHQGFVDAMSIDPNVK-IRELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIe 229
Cdd:cd19969  125 VAVLTG---PGQPNHEERVEGFKEAFAEYPGIEvVAVGDDNDDPEKAAQNTSAlLQAHPDLVGIFGVDASGGVGAAQAV- 200
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 496047307 230 eRDSSLVGHVEFIGVDGLLGGGLGVEAvaqGKLDAS 265
Cdd:cd19969  201 -REAGKTGKVKIVAFDDDPETLDLIKD---GVIDAS 232
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
519-617 1.03e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; 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 UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 52.94  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 519 ILTNLLSNAFKFTPeQGKITIRLREEETEVVLSVEDNGEGIPPENlasvferfftsgqsYAPGTGIGLHLTREFVLMHKG 598
Cdd:cd16917    4 IVQEALTNALKHAG-ASRVRVTLSYTADELTLTVVDDGVGFDGPA--------------PPGGGGFGLLGMRERAELLGG 68
                         90
                 ....*....|....*....
gi 496047307 599 SIHVESEQGERTVFTVQIP 617
Cdd:cd16917   69 TLTIGSRPGGGTRVTARLP 87
PRK10816 PRK10816
two-component system response regulator PhoP;
660-778 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 496047307 660 ILIVEDDwdirAYLQHELSGNFN-----VLVAENgAKALDILLKENV-SLVVSDVMMPEMNGFELCRRVKSDMAlsHIPV 733
Cdd:PRK10816   3 VLVVEDN----ALLRHHLKVQLQdaghqVDAAED-AKEADYYLNEHLpDIAIVDLGLPDEDGLSLIRRWRSNDV--SLPI 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 496047307 734 ILLTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLeERN 778
Cdd:PRK10816  76 LVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALM-RRN 119
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
680-776 1.10e-08

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 54.08  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 680 NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELcrrvksdmaLSHIPVILLTAL----SDDSQ-----RLygFE 750
Cdd:cd17593   25 DVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEV---------LEALPVEQLETKvivvSGDVQpeakeRV--LE 93
                         90       100
                 ....*....|....*....|....*.
gi 496047307 751 GGADEYIQKPFNIEIVKlriiKLLEE 776
Cdd:cd17593   94 LGALAFLKKPFDPEKLA----QLLEE 115
PLN03029 PLN03029
type-a response regulator protein; Provisional
658-786 1.18e-08

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 56.58  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDIRAYLQHEL-SGNFNVLVAENGAKALDIL-LKEN-------------------VSLVVSDVMMPEMNGF 716
Cdd:PLN03029   9 FHVLAVDDSLIDRKLIEKLLkTSSYQVTTVDSGSKALKFLgLHEDdrsnpdtpsvspnshqeveVNLIITDYCMPGMTGY 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 717 ELCRRVKSDMALSHIPVILLTALSDDSQRLYGFEGGADEYIQKPFNieivklriiklLEERNRLREVFLK 786
Cdd:PLN03029  89 DLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQ-----------LSDLNRLKPHMMK 147
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
811-907 1.18e-08

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 57.35  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 811 RKFIALIEENYSDPDFSIEKGSEKLGLSRVHLYRKVKElSGITPTDFLRNYRLKK-ASAL---LKQRSgtISEVAYATGF 886
Cdd:PRK09685 200 QKVVALIDQSIQEEILRPEWIAGELGISVRSLYRLFAE-QGLVVAQYIRNRRLDRcADDLrpaADDEK--ITSIAYKWGF 276
                         90       100
                 ....*....|....*....|.
gi 496047307 887 GSPAYFSKCFKAVYNITPTEF 907
Cdd:PRK09685 277 SDSSHFSTAFKQRFGVSPGEY 297
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
511-617 1.21e-08

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: 55.28  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 511 VDTDKMEKI---LTNLLSNAF------------KFTPEQGKITIRLREEETEVVLSVEDNGEGIPPE---------NLAS 566
Cdd:cd16916   31 LDKSVLEKLadpLTHLLRNAVdhgieapeerlaAGKPPEGTITLRAEHQGNQVVIEVSDDGRGIDREkirekaierGLIT 110
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 567 -----------VFERFFTSGQSYA------PGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:cd16916  111 adeaatlsddeVLNLIFAPGFSTAeqvtdvSGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
62-237 1.94e-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: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 56.47  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  62 LVVMDAIQDNDTQISQIKGFIKKKVDLLIISSneTEPVTPVAVEAYRAGIPTIILDRKINSDEYTTyIGADNYEIGRSIG 141
Cdd:cd06285   32 VLLADTGDDPERELAALDSLLSRRVDGLIITP--ARDDAPDLQELAARGVPVVLVDRRIGDTALPS-VTVDNELGGRLAT 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 142 MYVSSLikKETTILEIWGRRGSSSATERHQGFVDAM-----SIDPnvkIRELDGYWYRKNAYEEVLKLDSIEDVDI-VFA 215
Cdd:cd06285  109 RHLLEL--GHRRIAVVAGPLNASTGRDRLRGYRRALaeaglPVPD---ERIVPGGFTIEAGREAAYRLLSRPERPTaVFA 183
                        170       180
                 ....*....|....*....|....*...
gi 496047307 216 HNDMMALGAREAIEER------DSSLVG 237
Cdd:cd06285  184 ANDLMAIGVLRAARDLglrvpeDLSVVG 211
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
536-617 1.98e-08

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 56.17  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 536 KITIRLREEETEVVLSVEDNGEGIPPENlasvferfftsgqsyAPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQ 615
Cdd:COG4585  182 RVTVTLEVDDGELTLTVRDDGVGFDPEA---------------APGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRAT 246

                 ..
gi 496047307 616 IP 617
Cdd:COG4585  247 LP 248
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
485-600 2.92e-08

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 57.34  E-value: 2.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 485 SYFNNLAQSKRIDYTFLHEMDSLFVWVDTDKMEkILTNLLSNAFKFTPEQGKITIRLREEETEVVlsVEDNGEGIPPENL 564
Cdd:PRK10815 349 SALNKVYQRKGVNITLDISPEITFVGEKNDFME-VMGNVLDNACKYCLEFVEISARQTDEHLHIV--VEDDGPGIPESKR 425
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496047307 565 ASVFERfftsGQ---SYAPGTGIGLHLTREFVLMHKGSI 600
Cdd:PRK10815 426 ELIFDR----GQradTLRPGQGLGLSVAREITEQYEGKI 460
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
7-150 2.94e-08

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 56.67  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   7 YILLWLSLILCFACSPG-KKEKKyvIGVSqcsMTDI----WRQSmiRDMEVEALNHPEIELVVMDAIQDNDTQISQIKGF 81
Cdd:PRK10355   5 NILLTLCASLLLTSVAAhAKEVK--IGMA---IDDLrlerWQKD--RDIFVKKAESLGAKVFVQSANGNEETQMSQIENM 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496047307  82 IKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRsigMYVSSLIKK 150
Cdd:PRK10355  78 INRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGE---LQAKALVDK 143
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
660-764 3.09e-08

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: 52.80  E-value: 3.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGNFNVLVAE--NGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMAlshIPVILLT 737
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVVGEasDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI---APIVLLT 79
                         90       100
                 ....*....|....*....|....*..
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIE 764
Cdd:cd19932   80 AYSQQDLVERAKEAGAMAYLVKPFSES 106
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
391-600 3.42e-08

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 56.86  E-value: 3.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 391 NQRI---EQVTTQKLQFFTNVSHEIKTPLTLIlgplnkmaQDAPA------GAFADDIRIvKKNAERLKRVIDQLLDF-R 460
Cdd:PRK09470 230 NQMVtalERMMTSQQRLLSDISHELRTPLTRL--------QLATAllrrrqGESKELERI-ETEAQRLDSMINDLLVLsR 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 461 KIENNKMGLRVIKMDLVF--LIQEVKsyFNnlAQSKRIDYTFLHEMDSLFVWVDTDKMEKILTNLLSNAFKFTpeQGKIT 538
Cdd:PRK09470 301 NQQKNHLERETFKANSLWseVLEDAK--FE--AEQMGKSLTVSAPPGPWPINGNPNALASALENIVRNALRYS--HTKIE 374
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 539 IRLREEETEVVLSVEDNGEGIPPENLASVFERFF--------TSGqsyapGTGIGLHLTREFVLMHKGSI 600
Cdd:PRK09470 375 VAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYrvdeardrESG-----GTGLGLAIVENAIQQHRGWV 439
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
659-722 4.84e-08

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: 52.59  E-value: 4.84e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496047307 659 TILIVEDDWDIRAYLQHELSGNFNVLV---AENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRV 722
Cdd:COG2197    3 RVLIVDDHPLVREGLRALLEAEPDIEVvgeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
30-245 4.96e-08

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: 55.35  E-value: 4.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMtDIWRQSMIRDMeVEALNHPEIEL----VVMDAIQDNDTQISQIKGFIKKKVDLLIIS-SNETEPVtpVAV 104
Cdd:cd01391    1 IIGVVTSSL-HQIREQFGIQR-VEAIFHTADKLgasvEIRDSCWHGSVALEQSIEFIRDNIAGVIGPgSSSVAIV--IQN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 105 EAYRAGIPTIILDRKINSD------EYTTYIGADNYEIGRSIGMYVSSLIKKETTILEiwgRRGSSSATERHQGFVDAMS 178
Cdd:cd01391   77 LAQLFDIPQLALDATSQDLsdktlyKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIH---GEGLNSGELRMAGFKELAK 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496047307 179 IDPNVKIRELDGYWYRKNAYEEVL--KLDSIEDVDIVFAHNDMMALGAREAIeeRDSSLVGHVEFIGVD 245
Cdd:cd01391  154 QEGICIVASDKADWNAGEKGFDRAlrKLREGLKARVIVCANDMTARGVLSAM--RRLGLVGDVSVIGSD 220
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
523-617 5.02e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 51.68  E-value: 5.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 523 LLSNAFKFTPEQ----GKITIRLREEETEVVLSVEDNGEGIPPENLAsvferffTSGQSYAPGTGIGLHLTREFVLMHKG 598
Cdd:cd16924    9 LVENAIQHGLSPltdkGVVTISALKEDNHVMIEVEDNGRGIDPKVLN-------ILGKKPKEGNGIGLYNVHQRLILLFG 81
                         90       100
                 ....*....|....*....|..
gi 496047307 599 ---SIHVESEQGERTVFTVQIP 617
Cdd:cd16924   82 edyGIHIASEPDKGTRITFTIP 103
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
62-245 5.10e-08

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: 55.36  E-value: 5.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  62 LVVMDAIQDNDTQISQIKGFIKKKVDLLIISSneTEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIG 141
Cdd:cd06299   32 VILGNSDEDPEREDESLEMLLSQRVDGIIAVP--TGENSEGLQALIAQGLPVVFVDREVEGLGGVPVVTSDNRPGAREAV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 142 MYVSSLikKETTILEIWGRRGSSSATERHQGFVDAMS-----IDPNVkIRELDgywYRK-NAYEEVLK-LDSIEDVDIVF 214
Cdd:cd06299  110 EYLVSL--GHRRIGYISGPLSTSTGRERLAAFRAALTaagipIDEEL-VAFGD---FRQdSGAAAAHRlLSRGDPPTALI 183
                        170       180       190
                 ....*....|....*....|....*....|.
gi 496047307 215 AHNDMMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd06299  184 AGDSLMALGAIQALRELGLRIGDDVSLISFD 214
PRK10336 PRK10336
two-component system response regulator QseB;
660-811 7.52e-08

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 54.13  E-value: 7.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMalSHIPVILLTA 738
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKmGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKG--QREPVLILTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLL-----EERNRLR--EVFLKESQSPAGLSIET---KGKVESLDDL 808
Cdd:PRK10336  81 RDALAERVEGLRLGADDYLCKPFALIEVAARLEALMrrtngQASNELRhgNVMLDPGKRIATLAGEPltlKPKEFALLEL 160

                 ...
gi 496047307 809 FMR 811
Cdd:PRK10336 161 LMR 163
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
660-760 8.67e-08

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 51.95  E-value: 8.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDI-RAY---LQHELSGNFNVLVAENGAKALDIL--LK---ENVSLVVSDVMMPEMNGFELCRRVksdMALS- 729
Cdd:cd17595    3 ILTVDDDPQVlRAVardLRRQYGKDYRVLRADSGAEALDALkeLKlrgEAVALFLVDQRMPEMDGVEFLEKA---MELFp 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 496047307 730 HIPVILLTALSDDSQRLYGF-EGGADEYIQKP 760
Cdd:cd17595   80 EAKRVLLTAYADTDAAIRAInDVQLDYYLLKP 111
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
62-245 9.47e-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: 9.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  62 LVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEpvTPVAVEAYRAGIPTIILDRKINSDEyTTYIGADNYEIGRsig 141
Cdd:cd06270   32 LLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALS--DEELILIAEKIPPLVVINRYIPGLA-DRCVWLDNEQGGR--- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 142 MYVSSLIKK-ETTILEIWGRRGSSSATERHQGFVDAM-----SIDPNVKI----RELDGYWyrknAYEEVLKLDsiEDVD 211
Cdd:cd06270  106 LAAEHLLDLgHRRIACITGPLDIPDARERLAGYRDALaeagiPLDPSLIIegdfTIEGGYA----AAKQLLARG--LPFT 179
                        170       180       190
                 ....*....|....*....|....*....|....
gi 496047307 212 IVFAHNDMMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd06270  180 ALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFD 213
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
548-617 1.24e-07

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


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 55.30  E-value: 1.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  548 VVLSVEDNGEGIPPENLASVFERFFTSGQSYAPGTGIGLHLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:TIGR02938 424 IVVSILDSGPGIPQDLRYKVFEPFFTTKGGSRKHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEFR 493
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
660-760 2.01e-07

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: 50.09  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDIL--LKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKcSYEVTAASDGLQAWDVLedEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
683-770 2.97e-07

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: 49.70  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 683 VLVAENGAKALDILLKENVS--LVVSDVMMPEMNGFELCRRVKSDMALSHIPVIL-LTALSDDSQRLYGFEGGADEYIQK 759
Cdd:cd19933   27 VTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLFGRRERPLIVaLTANTDDSTREKCLSLGMNGVITK 106
                         90
                 ....*....|.
gi 496047307 760 PFNIEIVKLRI 770
Cdd:cd19933  107 PVSLHALGDEL 117
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
660-760 3.14e-07

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 49.42  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELS-GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILLTA 738
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGrAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKK--ARPDLPIIVMSA 78
                         90       100
                 ....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd19928   79 QNTLMTAVKAAERGAFEYLPKP 100
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
82-238 3.31e-07

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 53.19  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  82 IKKKVD-LLIISSNETEPVTPVaVEAYRAgIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYvssLIKK-ETTILEIWG 159
Cdd:PRK10703 112 AQKRVDgLLVMCSEYPEPLLAM-LEEYRH-IPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRY---LIERgHRDIGVIPG 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 160 RRGSSSATERHQGFVDAMSiDPNVKIRE---LDGYWYRKNAYEEVLKLDSIEDVDI-VFAHNDMMALGAREAIEER---- 231
Cdd:PRK10703 187 PLERNTGAGRLAGFMKAME-EANIKVPEewiVQGDFEPESGYEAMQQILSQKHRPTaVFCGGDIMAMGAICAADEMglrv 265

                 ....*....
gi 496047307 232 --DSSLVGH 238
Cdd:PRK10703 266 pqDISVIGY 274
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
28-231 4.16e-07

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: 52.51  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307   28 KYVIGVSQCSMTDIWRQSMIRDMEvEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAY 107
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGIT-KAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  108 RaGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLIKKETtILEIWGRRGSSSATERHQGFVDAMSidpnVKIRE 187
Cdd:pfam00532  80 Y-GIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRP-IAVMAGPASALTARERVQGFMAALA----AAGRE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 496047307  188 LDGYWYR---------KNAYEEVLKLDSieDVDIVFAHNDMMALGAREAIEER 231
Cdd:pfam00532 154 VKIYHVAtgdndipdaALAANAMLVSHP--TIDAIVAMNDEAAMGAVRALLKQ 204
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
107-237 6.39e-07

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: 51.89  E-value: 6.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 107 YRAGIPTIILDRKINSDEYTTYIGADNYEIGRSIGMYVSSLikKETTILEIWGRRGSSSATERHQGFVDAM-----SIDP 181
Cdd:cd06296   75 RSAGIPFVLIDPVGEPDPDLPSVGATNWAGGRLATEHLLDL--GHRRIAVITGPPRSVSGRARLAGYRAALaeagiAVDP 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047307 182 nVKIRELDgyWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEER------DSSLVG 237
Cdd:cd06296  153 -DLVREGD--FTYEAGYRAARElLELPDPPTAVFAGNDEQALGVYRAARALglrvpdDLSVIG 212
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
658-764 6.74e-07

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 48.78  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 658 YTILIVEDDWDI----RAYLQHeLSGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPV 733
Cdd:cd19925    1 INVLIVEDDPMVaeihRAYVEQ-VPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA--AGHDVDV 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 496047307 734 ILLTALSDDSQRLYGFEGGADEYIQKPFNIE 764
Cdd:cd19925   78 IVVTAANDVETVREALRLGVVDYLIKPFTFE 108
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
821-910 7.03e-07

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 52.30  E-value: 7.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 821 YSDPD--FSIEKGSEKLGLSRVHLYRKVKElSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSKCFKA 898
Cdd:PRK15185 216 SSSPSrqWKLTDVADHIFMSTSTLKRKLAE-EGTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKK 294
                         90
                 ....*....|..
gi 496047307 899 VYNITPTEFIES 910
Cdd:PRK15185 295 YFKTTPSTFIKM 306
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
659-764 7.65e-07

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 48.59  E-value: 7.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELS--GnFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmALSHIPVILL 736
Cdd:cd17563    2 SLLLVDDDEVFAERLARALErrG-FEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRA--LQPDARIVVL 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 496047307 737 TALSD-----DSQRLygfegGADEYIQKPFNIE 764
Cdd:cd17563   79 TGYASiatavEAIKL-----GADDYLAKPADAD 106
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
101-265 8.77e-07

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 51.80  E-value: 8.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 101 PVAVEAYRAGIPTIILDRKINSDEYT-------TYIGADNYEIGRSIGMYVSSLIKK---ETTILEiwGRRGSSSATERH 170
Cdd:PRK09701  98 MPVARAWKKGIYLVNLDEKIDMDNLKkaggnveAFVTTDNVAVGAKGASFIIDKLGAeggEVAIIE--GKAGNASGEARR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 171 QGFVDAMSIDPNVKIRELD-GYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIeeRDSSLVGHVEFIGVDGLL 248
Cdd:PRK09701 176 NGATEAFKKASQIKLVASQpADWDRIKALDVATNvLQRNPNIKAIYCANDTMAMGVAQAV--ANAGKTGKVLVVGTDGIP 253
                        170
                 ....*....|....*..
gi 496047307 249 GGGLGVEAvaqGKLDAS 265
Cdd:PRK09701 254 EARKMVEA---GQMTAT 267
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
70-237 1.02e-06

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: 50.99  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQ--IKGFIKKKVD-LLIISSNETEPVTPVAVEAyraGIPTIILDRKINSDEyTTYIGADNYEIGRSIgmyVSS 146
Cdd:cd19977   38 DEDPEKEKkyIEMLRAKQVDgIIIAPTGGNEDLIEKLVKS---GIPVVFVDRYIPGLD-VDTVVVDNFKGAYQA---TEH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 147 LIKK-ETTILEIWGRRGSSSATERHQGFVDAMS-----IDPNVkIRELDgywYRKNAYE---EVLKLDsiEDVDIVFAHN 217
Cdd:cd19977  111 LIELgHKRIAFITYPLELSTRQERLEGYKAALAdhglpVDEEL-IKHVD---RQDDVRKaisELLKLE--KPPDAIFAAN 184
                        170       180
                 ....*....|....*....|....*.
gi 496047307 218 DMMALGAREAIEER------DSSLVG 237
Cdd:cd19977  185 NLITLEVLKAIKELglripdDIALIG 210
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
60-237 1.09e-06

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: 50.96  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  60 IELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNEtepVTPVAVEAYR-AGIPTIILDRKinsDEYTTYIGADNYEIGR 138
Cdd:cd01542   30 YQPLIANTNLDEEREIEYLETLARQKVDGIILFATE---ITDEHRKALKkLKIPVVVLGQE---HEGFSCVYHDDYGAGK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 139 SIGMYVSSLIKKEttILEIW-GRRGSSSATERHQGFVDAMSIDPNVKIRELDGYWYRKNAYEEVLKLDSIEDVDIVFAHN 217
Cdd:cd01542  104 LLGEYLLKKGHKN--IAYIGvDEEDIAVGVARKQGYLDALKEHGIDEVEIVETDFSMESGYEAAKELLKENKPDAIICAT 181
                        170       180
                 ....*....|....*....|....*.
gi 496047307 218 DMMALGAREAIEER------DSSLVG 237
Cdd:cd01542  182 DNIALGAIKALRELgikipeDISVAG 207
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
660-760 1.25e-06

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 47.53  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG-NFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMAlsHIPVILLTA 738
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRmGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLP--QTPVAVITA 78
                         90       100
                 ....*....|....*....|..
gi 496047307 739 LSDDSQRLYGFEGGADEYIQKP 760
Cdd:cd19926   79 YGSLDTAIEALKAGAFDFLTKP 100
pleD PRK09581
response regulator PleD; Reviewed
620-760 1.60e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 51.44  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 620 KSHFDEscVFLSNATESSSGVAHLDISQVQetlNKKYDYTILIVEDDWDIRAYLQHELSGNFNVLVAENGAKALDILLKE 699
Cdd:PRK09581 123 KMVIDE--LRLRASTNAEIGVTALMIMAYA---NKDEDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAET 197
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496047307 700 NVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILLTALSDDSQRLYGFEGGADEYIQKP 760
Cdd:PRK09581 198 NYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLVDEDDDPRLVKALELGVNDYLMRP 258
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
817-911 1.61e-06

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 47.61  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 817 IEENYSDPdFSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSKCF 896
Cdd:PRK10219  14 IDEHIDQP-LNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSRVF 92
                         90
                 ....*....|....*
gi 496047307 897 KAVYNITPTEFIESL 911
Cdd:PRK10219  93 RRQFDRTPSDYRHRL 107
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
519-611 1.63e-06

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 47.99  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 519 ILTNLLSNAFKFTPEqGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTSGQsyapgtgiGLHLTREfvLMHkg 598
Cdd:COG2172   42 AVTNAVRHAYGGDPD-GPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYSTLAEGGR--------GLFLIRR--LMD-- 108
                         90
                 ....*....|...
gi 496047307 599 SIHVESEQGERTV 611
Cdd:COG2172  109 EVEYESDPGGTTV 121
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
660-770 1.90e-06

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: 47.64  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELS--GNFNVLVAENGAKALDILLKENVSLVVSDVMMPE-MNGFELCRRVKSDMALSHIPV-IL 735
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRslGVTRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLISPSTVfIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496047307 736 LTALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRI 770
Cdd:cd17589   81 VTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
659-764 1.93e-06

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: 47.82  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELS--GNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRvksdMALSHIP--VI 734
Cdd:cd17530    2 RVLVLDDDPFQCMMAATILEdlGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRH----LAESHSNaaVI 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496047307 735 LLTALsdDSQRLYGFEGGADEY-------IQKPFNIE 764
Cdd:cd17530   78 LMSGL--DGGILESAETLAGANglnllgtLSKPFSPE 112
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
523-617 2.55e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain.


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 46.66  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 523 LLSNAFKF----TPEQGKITIRLREEETEVVLSVEDNGEGIPPENLASVFERfftsgqsyaPGTGIGLHLTREFVLMHKG 598
Cdd:cd16956    9 IVENAVKHglsgLLDGGRVEITARLDGQHLLLEVEDNGGGMDPDTLARILIR---------SSNGLGLNLVDKRLRQAFG 79
                         90       100
                 ....*....|....*....|..
gi 496047307 599 SIH---VESEQGERTVFTVQIP 617
Cdd:cd16956   80 NDYgldIECAPGEGTRITIRLP 101
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
70-178 3.42e-06

ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members 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 members of the type 1 periplasmic binding protein superfamily. 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: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 49.51  E-value: 3.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSneTEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIGaDNYEIGRSIgmyVSSLIK 149
Cdd:cd06274   40 DPEQERRLVENLIARQVDGLIVAP--STPPDDIYYLCQAAGLPVVFLDRPFSGSDAPSVVS-DNRAGARAL---TEKLLA 113
                         90       100       110
                 ....*....|....*....|....*....|
gi 496047307 150 KET-TILEIWGRRGSSSATERHQGFVDAMS 178
Cdd:cd06274  114 AGPgEIYFLGGRPELPSTAERIRGFRAALA 143
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
807-907 3.44e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 49.90  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 807 DLFMRKFIALIEENYSDPDFSiekgsEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGF 886
Cdd:PRK13501 179 DLIMSALQQSLGAYFDMADFC-----HKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGF 253
                         90       100
                 ....*....|....*....|.
gi 496047307 887 GSPAYFSKCFKAVYNITPTEF 907
Cdd:PRK13501 254 EDSNYFSAVFTREAGMTPRDY 274
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
120-224 3.64e-06

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: 49.48  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 120 INSDEYTTYIGADNYEIGRSIGMYvssLIKK-ETTILEIWGRRGSSSATERHQGFVDAMSiDPNVKIRE---LDGYWYRK 195
Cdd:cd01545   89 GTDDDRSPSVRIDDRAAAREMTRH---LIALgHRRIGFIAGPPDHGASAERLEGFRDALA-EAGLPLDPdlvVQGDFTFE 164
                         90       100       110
                 ....*....|....*....|....*....|
gi 496047307 196 NAYEEVLKLDSIED-VDIVFAHNDMMALGA 224
Cdd:cd01545  165 SGLEAAEALLDLPDrPTAIFASNDEMAAGV 194
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
660-761 3.93e-06

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: 46.45  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSG--NFNVL-VAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:cd17561    4 VLIADDNREFVQLLEEYLNSqpDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIML 83
                         90       100
                 ....*....|....*....|....*
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQKPF 761
Cdd:cd17561   84 TAFGQEDITQRAVELGASYYILKPF 108
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
660-779 5.85e-06

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 49.75  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  660 ILIVEDDWDIRAYLQHELSGnFNVLVAENGAKALDILLKENVSLVVSDVMMP--EMNGFELCRRVKSDMALS-HIPVILL 736
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFAD-YELAVAADRESAIALVRRHEPAVVTLDLGLPpdADGASEGLAALQQILAIApDTKVIVI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 496047307  737 TALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRI-----IKLLEERNR 779
Cdd:TIGR02915  80 TGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVdrafhLYTLETENR 127
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
51-192 8.04e-06

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 49.18  E-value: 8.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  51 EVEALNhpeIELVVMDA--IQDNDTQISQIKGFIKKKVDLLIISSnetepVTPVA----VEAYRAGIPTIILDRKINSDE 124
Cdd:PRK10936  71 EAKRLG---VDLKVLEAggYYNLAKQQQQLEQCVAWGADAILLGA-----VTPDGlnpdLELQAANIPVIALVNGIDSPQ 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496047307 125 YTTYIGADNYEIGRSIGMYVSSLIKKETTILEI-W--GRRGSSSATERHQGFVDAMSidpNVKIRELDGYW 192
Cdd:PRK10936 143 VTTRVGVSWYQMGYQAGRYLAQWHPKGSKPLNVaLlpGPEGAGGSKAVEQGFRAAIA---GSDVRIVDIAY 210
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
832-911 9.55e-06

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 48.52  E-value: 9.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 832 SEKLGLSRVHLYRKVKElSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSKCFKAVYNITPTEFIESL 911
Cdd:PRK15186 204 SDSLYMSCSTLKRKLKQ-ENTSFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEFLAFL 282
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
872-908 1.08e-05

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 43.30  E-value: 1.08e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 496047307  872 QRSGTISEVAYATGFgSPAYFSKCFKAVYNITPTEFI 908
Cdd:pfam00165   6 STNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
532-617 1.20e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 49.02  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 532 PEQGKITIRLREEETEVVLSVEDNGEGIPPENLAS--------------------VFERFFTSGQSYAP------GTGIG 585
Cdd:COG0643  306 PETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAkaiekglitaeeaaalsdeeLLELIFAPGFSTAEevtdlsGRGVG 385
                         90       100       110
                 ....*....|....*....|....*....|..
gi 496047307 586 LHLTREFVLMHKGSIHVESEQGERTVFTVQIP 617
Cdd:COG0643  386 MDVVKTNIEALGGTIEIESEPGKGTTFTLRLP 417
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
70-300 1.35e-05

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: 47.70  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSNETEPV-TPVAVEAYRAGIPTIILDRKINSDEYTT----YIGADNYEIGRSIGMYv 144
Cdd:cd19966   41 DPEKMVEQFKEAIAAKPDGIAIMGHPGDGAyTPLIEAAKKAGIIVTSFNTDLPKLEYGDcglgYVGADLYAAGYTLAKE- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 145 ssLIK----KETTILEIWGRRGSSS-ATERHQGFVDAMsiDP---NVKIRELDgywyrknayEEVLKLDSIEDV--DIVF 214
Cdd:cd19966  120 --LVKrgglKTGDRVFVPGLLPGQPyRVLRTKGVIDAL--KEagiKVDYLEIS---------LEPNKPAEGIPVmtGYLA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 215 AHND---MMALG------AREAIEerDSSL-VGHVEFIGVDgllGGGLGVEAVAQGKLDAsfyyptgggvaikVAWQILS 284
Cdd:cd19966  187 ANPDvkaIVGDGggltanVAKYLK--AAGKkPGEIPVAGFD---LSPATVQAIKSGYVNA-------------TIDQQPY 248
                        250       260
                 ....*....|....*....|....
gi 496047307 285 GQAY--------TKKYALSTAMID 300
Cdd:cd19966  249 LQGYlpvlqiylTKKYGFSGLDID 272
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
103-245 2.64e-05

ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. 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: 380518 [Multi-domain]  Cd Length: 273  Bit Score: 46.86  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 103 AVEAYRAGIPTIILDRKINSDEYTTyIGADNYEIGRSIgmyVSSLIKKETTILEIWGRRGSSSATERHQGFVDAMS---- 178
Cdd:cd06295   79 LRELAQQGLPMVVWGAPEDGQSYCS-VGSDNVKGGALA---TEHLIEIGRRRIAFLGDPPHPEVADRLQGYRDALAeagl 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496047307 179 -IDPN----VKIRELDGYwyrkNAYEEVLKLDSieDVDIVFAHNDMMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd06295  155 eADPSlllsCDFTEESGY----AAMRALLDSGT--AFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYD 220
PRK13560 PRK13560
hypothetical protein; Provisional
386-617 3.05e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 47.74  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 386 ELSVANQRIEQVTTQKLQFFTNVSHEIKTPLTLILGPLNKMAQDApagafaDDIRIVKKNAERLKRVIDQLLDFRKIENN 465
Cdd:PRK13560 590 ERKHAEEKIKAALTEKEVLLKEIHHRVKNNLQIISSLLDLQAEKL------HDEEAKCAFAESQDRICAMALAHEKLYQS 663
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 466 KmglrvikmDLVF--LIQEVKSYFNNLAQSKRIDYTFLH-EMDSLFVWVDTDKMEK---ILTNLLSNAFKFT-PEQ--GK 536
Cdd:PRK13560 664 E--------DLADidFLDYIESLTAHLKNSFAIDFGRIDcKIDADDGCLDIDKAIPcglIISELLSNALKHAfPDGaaGN 735
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 537 ITIRLREEETEVV-LSVEDNGEGIPpenlasvferfftSGQSYAPGTGIGLHLTREFVLMHKGSIHVESEQGERtvFTVQ 615
Cdd:PRK13560 736 IKVEIREQGDGMVnLCVADDGIGLP-------------AGFDFRAAETLGLQLVCALVKQLDGEIALDSRGGAR--FNIR 800

                 ..
gi 496047307 616 IP 617
Cdd:PRK13560 801 FP 802
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
660-739 4.05e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.80  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYL--------QHELSGnfnvlVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVksdMALSHI 731
Cdd:PRK12555   3 IGIVNDSPLAVEALrralardpDHEVVW-----VATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRI---MAERPC 74

                 ....*...
gi 496047307 732 PVILLTAL 739
Cdd:PRK12555  75 PILIVTSL 82
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
67-264 4.39e-05

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: 46.07  E-value: 4.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  67 AIQDNDT--QISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIIL----DRKINSDEYTTYIGADNYEIGRSI 140
Cdd:cd06312   37 GPQNNDIadQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAInsgdDRSKERLGALTYVGQDEYLAGQAA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 141 GMYVSSliKKETTILEIWGRRGSSSATERHQGFVDAMSiDPNVKIRELDGYWYRKNAYEEV---LKLDSieDVDIVFAHN 217
Cdd:cd06312  117 GERALE--AGPKNALCVNHEPGNPGLEARCKGFADAFK-GAGILVELLDVGGDPTEAQEAIkayLQADP--DTDAVLTLG 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 496047307 218 DMMALGAREAIEErdSSLVGHVEFIGVDgllGGGLGVEAVAQGKLDA 264
Cdd:cd06312  192 PVGADPALKAVKE--AGLKGKVKIGTFD---LSPETLEAIKDGKILF 233
PRK10693 PRK10693
two-component system response regulator RssB;
685-782 5.25e-05

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 46.14  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 685 VAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKsdMALSHIPVILLTALS-----DDSQRLygfegGADEYIQK 759
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLR--NRGDQTPVLVISATEnmadiAKALRL-----GVQDVLLK 74
                         90       100
                 ....*....|....*....|...
gi 496047307 760 PfnieivklriIKLLeerNRLRE 782
Cdd:PRK10693  75 P----------VKDL---NRLRE 84
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
69-189 7.64e-05

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: 45.34  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  69 QDND--TQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDrkINSDEY----TTYIGADNYEIGRSIGM 142
Cdd:cd19965   38 QTFDvaEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFN--VDAPGGenarLAFVGQDLYPAGYVLGK 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 496047307 143 YVSSLIK-KETTILEIWGRRGSSSATERHQGFVDAMS-IDPNVKIRELD 189
Cdd:cd19965  116 RIAEKFKpGGGHVLLGISTPGQSALEQRLDGIKQALKeYGRGITYDVID 164
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
69-237 7.83e-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: 7.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  69 QDNDTQISQIKGFIK-KKVDLLII-SSNETEPVTPvavEAYRAGIPTIILDRKINSDEyTTYIGADNYEIGRSIGMYvss 146
Cdd:cd06294   43 NTEEELLEEVKRMVRgRRVDGFILlYSKEDDPLIE---YLKEEGFPFVVIGKPLDDND-VLYVDNDNVQAGYEATEY--- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 147 LIKK-ETTILEIWGRRGSSSATERHQGFVDAMS----IDPNVKIRELD-GYWYRKNAYEEVLKLDsiEDVDIVFAHNDMM 220
Cdd:cd06294  116 LIDKgHKRIAFIGGDKNLVVSIDRLQGYKQALKeaglPLDDDYILLLDfSEEDGYDALQELLSKP--PPPTAIVATDDLL 193
                        170       180
                 ....*....|....*....|...
gi 496047307 221 ALGAREAIEE------RDSSLVG 237
Cdd:cd06294  194 ALGVLRYLQElglrvpEDVSIIS 216
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
128-245 8.81e-05

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: 45.22  E-value: 8.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 128 YIGADNYEIGRSIGMYVSSLIKKEttILEIWGRRGSSSATERHQGFVDAMS---IDPNVKIRELDGYWYR--KNAYEEVL 202
Cdd:cd06284   94 SVSIDNEAAAYDATEYLISLGHRR--IAHINGPLDNVYARERLEGYRRALAeagLPVDEDLIIEGDFSFEagYAAARALL 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496047307 203 KLDsiEDVDIVFAHNDMMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd06284  172 ALP--ERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFD 212
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
659-766 9.45e-05

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: 43.17  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDWDIRAYLQHELSGNFNVLV--AENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPVILL 736
Cdd:cd17575    2 MVLLVDDQAIIGEAVRRALADEEDIDFhyCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVL 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 496047307 737 TALSDDSQRLYGFEGGADEYIQK-PFNIEIV 766
Cdd:cd17575   82 STKEEPEVKSEAFALGANDYLVKlPDKIELV 112
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
536-574 1.47e-04

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 43.58  E-value: 1.47e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 496047307 536 KITIRLREEETEVVlSVEDNGEGIPPENLASVFERFFTS 574
Cdd:cd16926   32 RIDVEIEEGGLKLI-RVTDNGSGISREDLELAFERHATS 69
PRK13856 PRK13856
two-component response regulator VirG; Provisional
660-777 1.60e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 44.42  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGN-FNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDmalSHIPVILLT- 737
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHaFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATK---SDVPIIIISg 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496047307 738 ALSDDSQRLYGFEGGADEYIQKPFNIEIVKLRIIKLLEER 777
Cdd:PRK13856  81 DRLEEADKVVALELGATDFIAKPFGTREFLARIRVALRVR 120
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
660-760 1.61e-04

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: 42.30  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGNFNVLVAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSDMALSHIPvILLTAL 739
Cdd:cd17539    1 VLLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLP-ILAVAD 79
                         90       100
                 ....*....|....*....|..
gi 496047307 740 SDDSQRLY-GFEGGADEYIQKP 760
Cdd:cd17539   80 PGDRGRLIrALEIGVNDYLVRP 101
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
30-245 2.18e-04

ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 44.08  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  30 VIGVSQCSMTDIWRQSMIRDMEVEALNHpEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRa 109
Cdd:cd19975    1 TIGVIIPDISNSFFAEILKGIEDEAREN-GYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMN- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 110 gIPTIILDRKINSDEYTtYIGADNYEIGRSIgmyVSSLIKKETTILEIWGrrGS----SSATERHQGFVDAMSiDPNVKI 185
Cdd:cd19975   79 -IPVVLVSTESEDPDIP-SVKIDDYQAAYDA---TNYLIKKGHRKIAMIS--GPlddpNAGYPRYEGYKKALK-DAGLPI 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496047307 186 RE---LDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd19975  151 KEnliVEGDFSFKSGYQAMKRlLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFD 214
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
760-907 2.32e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 44.32  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 760 PFNIEIVKLRIIKLLEERNRLRevFLKESQSPAglSIETkgkveslddlFMRKFIALIEENYSDPdFSIEKGSEKLGLSR 839
Cdd:PRK13500 172 PFANEMAELLFGQLVMLLNRHR--YTSDSLPPT--SSET----------LLDKLITRLAASLKSP-FALDKFCDEASCSE 236
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 840 VHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSKCFKAVYNITPTEF 907
Cdd:PRK13500 237 RVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQW 304
ftrA PRK09393
transcriptional activator FtrA; Provisional
833-905 2.65e-04

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 44.18  E-value: 2.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047307 833 EKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSKCFKAVYNITPT 905
Cdd:PRK09393 242 ARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPA 314
HATPase_YpdA-like cd16955
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
536-617 2.92e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli YpdA, a HK of the two-component system (TCS) YpdA-YpdB which is involved in a nutrient sensing regulatory network with YehU-YehT. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and some have a GAF sensor domain; some contain a DUF3816 domain; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340431 [Multi-domain]  Cd Length: 102  Bit Score: 40.91  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 536 KITIRLREEeTEVVLSVEDNGEGIPPENLASVFerfftsgQSYAPGTGIGL-HLTREFVLMHKGSIHVESEQGERTVFTV 614
Cdd:cd16955   28 KISVKKQLK-NRLHIAVEDNGIGISPKVIERVE-------QDEMPGNKIGLlNVHQRLKLGYGEGLHIRSRPDPGTLIAF 99

                 ...
gi 496047307 615 QIP 617
Cdd:cd16955  100 YIP 102
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
62-245 2.93e-04

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: 43.81  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  62 LVVMDAIQDNDTQISQIKGFIKKKVDLLIISSNETEpVTPVAVEAYRAGIPTIILDRKINSDEYTTyIGADNYEIGRSIG 141
Cdd:cd06282   32 LLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQ-GSEALELLEEEGVPYVLLFNQTENSSHPF-VSVDNRLASYDVA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 142 MYVSSLikKETTILEIWGR-RGSSSATERHQGFVDAMSiDPNVKIRELDGYWYRKNAYEEVLK--LDSIEDVDIVFAHND 218
Cdd:cd06282  110 EYLIAL--GHRRIAMVAGDfSASDRARLRYQGYRDALK-EAGLKPIPIVEVDFPTNGLEEALTslLSGPNPPTALFCSND 186
                        170       180
                 ....*....|....*....|....*..
gi 496047307 219 MMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd06282  187 LLALSVISALRRLGIRVPDDVSVIGFD 213
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
69-245 3.00e-04

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: 43.70  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  69 QDNDTQISQIKGFIKKKVDLLIIssnetEPvTPVAV---------EAYRAGIPTIILDRKINSDEYTtYIGADNYEIGRS 139
Cdd:cd01541   39 NDVEKEREILESLLDQNVDGLII-----EP-TKSALpnpnldlyeELQKKGIPVVFINSYYPELDAP-SVSLDDEKGGYL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 140 IgmyVSSLIKK-ETTILEIWgRRGSSSATERHQGFVDAMSiDPNVKIRELDGYWY-------RKNAYEEVLKLDSIEDVD 211
Cdd:cd01541  112 A---TKHLIDLgHRRIAGIF-KSDDLQGVERYQGFIKALR-EAGLPIDDDRILWYstedledRFFAEELREFLRRLSRCT 186
                        170       180       190
                 ....*....|....*....|....*....|....
gi 496047307 212 IVFAHNDMMALGAREAIEERDSSLVGHVEFIGVD 245
Cdd:cd01541  187 AIVCYNDEIALRLIQALREAGLRVPEDLSVVGFD 220
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
523-574 3.79e-04

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 44.11  E-value: 3.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 523 LLSNAFKFTPEQG---KITIRLREEETE---VVLSVEDNGEGIPPENLASVFERFFTS 574
Cdd:PRK04184  44 LVDNSLDACEEAGilpDIKIEIKRVDEGkdhYRVTVEDNGPGIPPEEIPKVFGKLLYG 101
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
70-244 4.36e-04

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: 43.39  E-value: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  70 DNDTQISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYI-GADNYEIGRSIGMYVSSLI 148
Cdd:cd06302   41 DAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSARDYFVnQADDEGLGEALVDSLAKEI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 149 KKETTILEIwgrRGSSSATErHQGFVDAMS--IDPNVKIRELDGYWYRKNAYEEVLK--LDSIE---DVDIVFAHNDMMA 221
Cdd:cd06302  121 GGKGKVAIL---SGSLTATN-LNAWIKAMKeyLKSKYPDIELVDTYYTDDDQQKAYTqaQNLIQaypDLKGIIGVSTTAP 196
                        170       180
                 ....*....|....*....|...
gi 496047307 222 LGAREAIEErdSSLVGHVEFIGV 244
Cdd:cd06302  197 PAAAQAVEE--AGKTGKVAVTGI 217
COG1389 COG1389
DNA topoisomerase VI, subunit B [Replication, recombination and repair];
536-574 4.68e-04

DNA topoisomerase VI, subunit B [Replication, recombination and repair];


Pssm-ID: 440999 [Multi-domain]  Cd Length: 530  Bit Score: 43.66  E-value: 4.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 496047307 536 KITIRLREEETEVVLSVEDNGEGIPPENLASVFERFFTS 574
Cdd:COG1389   61 KVSIERVDGKDIYRVTVEDNGPGIPPEQIPKVFGKLLYG 99
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
500-607 5.61e-04

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 41.56  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 500 FLHEMDS--LFVWVDTdKMEKILTNLLSNAFKFTPEQGK--------ITIRLREEETEVVLSVEDNGEGIPPENLASVFE 569
Cdd:cd16929   27 LEIEGDPsiRFPYVPS-HLYYILFELLKNAMRATVESHGddsddlppIKVTVAKGDEDLTIKISDRGGGIPREDLARLFS 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496047307 570 RFFT--------------SGQSYAP--GTGIGLHLTREFVLMHKGSIHVESEQG 607
Cdd:cd16929  106 YMYStapqpslddfsdliSGTQPSPlaGFGYGLPMSRLYAEYFGGDLDLQSMEG 159
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
685-761 5.74e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 43.21  E-value: 5.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496047307 685 VAENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVksdMALSHIPVILLTALSDDSQR--LYGFEGGADEYIQKPF 761
Cdd:PRK00742  34 TAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKI---MRLRPTPVVMVSSLTERGAEitLRALELGAVDFVTKPF 109
lacI PRK09526
lac repressor; Reviewed
154-269 5.75e-04

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 43.06  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 154 ILEIWGRRGSSSATERHQGFVDAMSiDPNVK-IRELDGYWYRKNAYEEVLKL--DSIEDVDIVFAhNDMMALGAREAIEE 230
Cdd:PRK09526 184 IALLAGPESSVSARLRLAGWLEYLT-DYQLQpIAVREGDWSAMSGYQQTLQMlrEGPVPSAILVA-NDQMALGVLRALHE 261
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496047307 231 RDSSLVGHVEFIGVDGLLggglgveavaqgklDASFYYP 269
Cdd:PRK09526 262 SGLRVPGQISVIGYDDTE--------------DSSYFIP 286
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
88-237 7.07e-04

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: 42.64  E-value: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  88 LLIISSNETEPvtpvAVEAYRA-GIPTIILDRKINSDEYTTyIGADNYEIGRsigMYVSSLIKK-ETTILEIWGRRGSSS 165
Cdd:cd06293   59 LIVTPSDDDLS----HLARLRArGTAVVLLDRPAPGPAGCS-VSVDDVQGGA---LAVDHLLELgHRRIAFVSGPLRTRQ 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 166 ATERHQGFVDAMS---IDPNVKIRELD-GYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEER------DSS 234
Cdd:cd06293  131 VAERLAGARAAVAeagLDPDEVVRELSaPDANAELGRAAAAQlLAMPPRPTAVFAANDLLALGLLAGLRRAglrvpdDVS 210

                 ...
gi 496047307 235 LVG 237
Cdd:cd06293  211 VVG 213
PRK15044 PRK15044
transcriptional regulator SirC; Provisional
834-911 7.72e-04

transcriptional regulator SirC; Provisional


Pssm-ID: 185004 [Multi-domain]  Cd Length: 295  Bit Score: 42.71  E-value: 7.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 834 KLGLSRVHLYRKVKElSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSKCFKAVYNITPTEFIESL 911
Cdd:PRK15044 217 KLFMSVSSLKRKLAA-EEVSFSKIYLDARMNQAIKLLRMGAGNISQVATMCGYDTPSYFIAIFKRHFKITPLSFMRTM 293
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
807-907 8.84e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 42.35  E-value: 8.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 807 DLFMRKFIALIEENYSDPdFSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGF 886
Cdd:PRK13502 175 ETLLDKLITALANSLECP-FALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGF 253
                         90       100
                 ....*....|....*....|.
gi 496047307 887 GSPAYFSKCFKAVYNITPTEF 907
Cdd:PRK13502 254 EDSNYFSVVFTRETGMTPSQW 274
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
59-187 1.08e-03

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: 41.78  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  59 EIELVVMDAIqDNDTQISQIKGfIKKKVDLLIISSNETEPVTPvAVEAYRA-GIPTIILDRKINSDEYTTYIGADNYEIG 137
Cdd:cd06307   34 RLRIHFVDSL-DPEALAAALRR-LAAGCDGVALVAPDHPLVRA-AIDELAArGIPVVTLVSDLPGSRRLAYVGIDNRAAG 110
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496047307 138 RSIGMYVS-SLIKKETTILEIWGRRGSSSATERHQGFVDAMSID-PNVKIRE 187
Cdd:cd06307  111 RTAAWLMGrFLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRERfPDLTVLE 162
PRK14084 PRK14084
DNA-binding response regulator;
660-761 1.16e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 41.66  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 660 ILIVEDDWDIRAYLQHELSGNFNVLV---AENGAKALDILLKENVSLVVSDVMMPEMNGFELCRRVKSdmaLSHIPVILL 736
Cdd:PRK14084   3 ALIVDDEPLARNELTYLLNEIGGFEEineAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQK---MKEPPAIIF 79
                         90       100
                 ....*....|....*....|....*
gi 496047307 737 tALSDDSQRLYGFEGGADEYIQKPF 761
Cdd:PRK14084  80 -ATAHDQFAVKAFELNATDYILKPF 103
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
659-770 1.25e-03

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: 39.54  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 659 TILIVEDDW----DIRAYLQ---HELSGnfnvlVAENGAKALDILLKENVSLVVSDVMMPE-MNGFELCRRVKSDMalsH 730
Cdd:cd17540    2 RVLIIEDEPliamDLEQIVEdlgHQVVG-----IARTRDEAVALARRERPDLILADIQLADgSSGIDAVNEILTTH---D 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496047307 731 IPVILLTALSDdsqRLYGFEGGADEY-IQKPFNIEIVKLRI 770
Cdd:cd17540   74 VPVIFVTAYPE---RLLTGERPEPTFlITKPFDPEMVKAAI 111
HATPase_AgrC-ComD-like cd16935
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
485-616 1.52e-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: 39.48  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 485 SYFNNLAQSKRIDYTF-LHEMDSLFVwvDTDKMEKILTNLLSNAF----KFTPEQGKITIRLREEETEVVLSVEDNGEGI 559
Cdd:cd16935    7 SEKLELAREKGIEFTIeIDIPILLPI--SPLDLCIIFGNLLDNAIeacaKIDKENRFIHLKIRQKKGFLIISIENSYEGE 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496047307 560 PPENlasvFERFFTSGQSyaPGTGIGLHLTREFVLMHKGSIHVESEQGertVFTVQI 616
Cdd:cd16935   85 LKKK----NGLFLSTKKD--KNHGIGLKSIREIVKKYNGNLSIEYENG---IFTLSI 132
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
815-909 2.52e-03

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 40.68  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 815 ALIEENYSDpDFSIEKGSEKLGLSRVHLYRKVKElSGITPTDFLRNYRLKKASALLKQRSGTISEVAYATGFGSPAYFSK 894
Cdd:PRK09978 149 TVINNNIAH-EWTLARIASELLMSPSLLKKKLRE-EETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIY 226
                         90
                 ....*....|....*
gi 496047307 895 CFKAVYNITPTEFIE 909
Cdd:PRK09978 227 VFRNYYGMTPTEYQE 241
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
74-177 3.25e-03

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: 40.70  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  74 QISQIKGFIKKKVDLLIISSNETEPVTPVAVEAYRAGIPTIILDRKINSDEYTTYIG-ADNYEIGRSIGMYVSSLI--KK 150
Cdd:cd20000   45 QIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKVVTFDSDVAPEARDLFVNqADADGIGRAQVDMMAELIggEG 124
                         90       100
                 ....*....|....*....|....*...
gi 496047307 151 ETTILeiwgrrgSSSATERHQ-GFVDAM 177
Cdd:cd20000  125 EFAIL-------SATPTATNQnAWIDAM 145
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
36-177 4.73e-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: 39.91  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  36 CSMTDI---WRQSMIRDMEvEALNHPEIELVVMDAIQDNDTQISQIKGFIKKKVDLLIIS-SNETEPVTPVAVEayRAGI 111
Cdd:cd06281    4 CLVSDIsnpLYARIVKAAE-ARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTpGDEDDPELAAALA--RLDI 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496047307 112 PTIILDRKINSDeyTTYIGADNYEIGRSIGMYVSSLIKKEttILEIWGRRGSSSATERHQGFVDAM 177
Cdd:cd06281   81 PVVLIDRDLPGD--IDSVLVDHRSGVRQATEYLLSLGHRR--IALLTGGPDIRPGRERIAGFKAAF 142
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
62-189 6.05e-03

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: 39.46  E-value: 6.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307  62 LVVMDAiqDNDTQ--ISQIKGFIKKKVDLLII-SSNETEPVTPVAVEAyraGIPTIILDRKINSDEYTTyIGADNYEIGR 138
Cdd:cd06283   32 LLICNS--NNDPEkeRDYIESLLSQRVDGLILqPTGNNNDAYLELAQK---GLPVVLVDRQIEPLNWDT-VVTDNYDATY 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496047307 139 SIGMYvssLIKK--ETTILEIWGRRGSSSATERHQGFVDAMS-IDPNVKIRELD 189
Cdd:cd06283  106 EATEH---LKEQgyERIVFVTEPIKGISTRRERLQGFLDALArYNIEGDVYVIE 156
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
168-237 7.87e-03

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: 39.04  E-value: 7.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496047307 168 ERHQGFVDAMSI-DPNVKIRELDGYWYRKNAYEEVLK-LDSIEDVDIVFAHNDMMALGAREAIEER------DSSLVG 237
Cdd:cd01544  135 PRLRAFREYMKEkGLYNEEYIYIGEFSVESGYEAMKElLKEGDLPTAFFVASDPMAIGALRALQEAgikvpeDISIIS 212
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
817-859 8.04e-03

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 35.21  E-value: 8.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 496047307  817 IEENYSDpDFSIEKGSEKLGLSRVHLYRKVKELSGITPTDFLR 859
Cdd:pfam00165   1 LRENLST-NLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
511-611 8.48e-03

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 36.96  E-value: 8.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 511 VDTDKMEKILTNLLSNAFKFTPEqGKITIRLREEETEVVLSV--EDNGEGIPpeNLASVFERFFTSGQsyapGTGIGLHL 588
Cdd:cd16934   21 VRQAEIATAVTELARNLLKHAGG-GQVLLEVVAEGGRVALEIlaVDQGPGIA--DVDEALRDGFSTGG----GLGLGLGG 93
                         90       100
                 ....*....|....*....|...
gi 496047307 589 TREfvLMHKGSIHVESEQGERTV 611
Cdd:cd16934   94 VRR--LADEFDLHSAPGRGTVVV 114
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
166-238 9.29e-03

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: 39.07  E-value: 9.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047307 166 ATERHQGFVDAM-----SIDPNVKIR----ELDGYwyrkNAYEEVLKLDsiEDVDIVFAHNDMMALGAREAIEE------ 230
Cdd:cd20010  135 AHQRRDGYRAALaeaglPVDPALVREgpltEEGGY----QAARRLLALP--PPPTAIVCGSDLLALGAYRALREaglspg 208

                 ....*...
gi 496047307 231 RDSSLVGH 238
Cdd:cd20010  209 KDVSVIGH 216
 
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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