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Conserved domains on  [gi|499349852|ref|WP_011039145|]
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PAS domain-containing hybrid sensor histidine kinase/response regulator [Xanthomonas campestris]

Protein Classification

PAS domain-containing hybrid sensor histidine kinase/response regulator( domain architecture ID 11586209)

PAS domain-containing hybrid sensor histidine kinase/response regulator with an N-terminal domain related to SLC5 solute-binding domains, part of a two-component regulatory system, receives the signal from the sensor partner in a two-component system through its receiver (REC) domain and functions as a protein kinase that phosphorylates a target protein in response to various signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SLC5sbd cd10322
Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding ...
6-509 3.49e-66

Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding domain; This family represents the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporter family or solute sodium symporter family) that co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. Family members include: the human glucose (SGLT1, 2, 4, 5), chiro-inositol (SGLT5), myo-inositol (SMIT), choline (CHT), iodide (NIS), multivitamin (SMVT), and monocarboxylate (SMCT) cotransporters, as well as Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. Vibrio parahaemolyticus Na(+)/galactose cotransporter (vSGLT) has 13 transmembrane helices (TMs): TM-1, an inverted topology repeat: TMs1-5 and TMs6-10, and TMs 11-12 (TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). One member of this family, human SGLT3, has been characterized as a glucose sensor and not a transporter. Members of this family are important in human physiology and disease.


:

Pssm-ID: 271357 [Multi-domain]  Cd Length: 454  Bit Score: 230.90  E-value: 3.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    6 ILLLVSLGYAALLFGVAWWGDHR------PLYPERPWLRPAVYSLALAVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLL 79
Cdd:cd10322     1 IDLIIVVVYLALLLGIGLYASKKvkssedFFLAGRSLGPWLLAGTLAATWISAGSFVGVAGLAYTYGLSAIWYILGAALG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   80 LLFGWRIIerlALIARAENTVSIADFISSRYGrSRRLAALVAVIALVGIVPYLALQYKAVAMSLEVLTGhssagrgIFAD 159
Cdd:cd10322    81 ALLLALFL---APRLRRLGKTTIPETILERYY-SKGLRLLVAIIIIIALIPYLALQLIGGGYILSTLLG-------IPYT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  160 PALYVALLMALFATLFGTRqvdatehhHGMMLAIALESVIKLVAIVAVGVFAWLWLGDHQL-HIADSARTLFQHTPSVG- 237
Cdd:cd10322   150 VAVIIAAVIVILYTVFGGM--------RAVAWTDVIQGIVMLIGVLVAAIFILSKVGGGGFsALAAALPALLLALGPGGg 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  238 -----FISQTLLSFLAVVCLPRQFHVAVVECSDVgDIRRARWLFGAYLVIISAMVVPIASAGVALFGQDSSVvdDAVVLA 312
Cdd:cd10322   222 lgwstILSLILLTGLGVLALPQVFQRILAAKDEK-TARRAFLLAGLLLLLIGFLVALIGLAARALFPDLENP--DLALPT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  313 LPLSQGNTVLALVAYVGGFSAATGMVIVASIALATMVSNDLVMPVLLRRRSSAdaratvasRVLWIRRVAILLLALIAYG 392
Cdd:cd10322   299 LINSLLPPGLAGLVLAGLLAAAMSTADSLLLAASTLFTRDIYKPLINPKASDK--------KLLRVSRIAVVVVGVLALL 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  393 YHRSVANdtTLAAYGLMAFAAVAQFAPGVIGGLYWRGASRKGVETGMVLGFMTWIYTLLLPAAtragwlqpewlvdGPFG 472
Cdd:cd10322   371 LALLPPS--ILLLLSLAAGLLAAALFPPLLGGLFWKRATKAGAIAGIIVGLIVTLVWLLLPLA-------------SPLG 435
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 499349852  473 IgwlqpqqlfgmsgwdplaHGTFWSLLINTGTMMVVS 509
Cdd:cd10322   436 I------------------DPIIPALLVSLIVFVVVS 454
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
676-1002 2.23e-59

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 207.45  E-value: 2.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  676 MLYVGRPVADLIRYNAERGELGEGDIEDQIDRRIRHMRAGSPHVFERTRSDGKVIEMRGQALPGGGYVTSYNDITDYKRA 755
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  756 ERALLDANENLEQRVADRSREAELAQQSKTRFLAAISHDVLQPLNAARLFASALRESHqnNEEQRHLAERVDASLRAAEE 835
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL--DEEQREYLETILRSADRLLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  836 LLDGLLDVSRLDAGGLRPTVEDFDASALMHELAAQYAPVAGSRGLRLQVH--ARALWVRSDRRLLRRVMQNFLANALRYT 913
Cdd:COG0642   160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDlpDDLPTVRGDPDRLRQVLLNLLSNAIKYT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  914 RQG-RIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQPFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQ 992
Cdd:COG0642   240 PEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPF--FRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGK 317
                         330
                  ....*....|
gi 499349852  993 GSMFSILLPR 1002
Cdd:COG0642   318 GTTFTVTLPL 327
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1024-1142 2.14e-19

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: 85.29  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1024 SLAGLRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVDP-I 1101
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAgPPDLILLDINMPG-MDGLELLRRIRALPRLPdI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499349852 1102 AGALLTADGRDELKQLARQRG-YRLLTKPVKPASLRAFLSAY 1142
Cdd:COG0784    81 PIIALTAYADEEDRERALEAGaDDYLTKPVDPEELLEALRRL 122
PAS super family cl43642
PAS domain [Signal transduction mechanisms];
552-759 3.01e-12

PAS domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2202:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.13  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  552 AERVVGERHAHRAFLDQAQLLERELQPTAVADRAWvQFTERLLAASIGAASARLVLTSLLRGSGMELGEVVAVLD----- 626
Cdd:COG2202    48 AEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW-RGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDiterk 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  627 EAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRynaergELGEGDIEDQID 706
Cdd:COG2202   127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEEL-LGKSLLDLLH------PEDRERLLELLR 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499349852  707 RRIRHMRAGSPHVFERTRSDGKVIEMRGQALP------GGGYVTSYNDITDYKRAERAL 759
Cdd:COG2202   200 RLLEGGRESYELELRLKDGDGRWVWVEASAVPlrdggeVIGVLGIVRDITERKRAEEAL 258
 
Name Accession Description Interval E-value
SLC5sbd cd10322
Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding ...
6-509 3.49e-66

Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding domain; This family represents the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporter family or solute sodium symporter family) that co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. Family members include: the human glucose (SGLT1, 2, 4, 5), chiro-inositol (SGLT5), myo-inositol (SMIT), choline (CHT), iodide (NIS), multivitamin (SMVT), and monocarboxylate (SMCT) cotransporters, as well as Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. Vibrio parahaemolyticus Na(+)/galactose cotransporter (vSGLT) has 13 transmembrane helices (TMs): TM-1, an inverted topology repeat: TMs1-5 and TMs6-10, and TMs 11-12 (TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). One member of this family, human SGLT3, has been characterized as a glucose sensor and not a transporter. Members of this family are important in human physiology and disease.


Pssm-ID: 271357 [Multi-domain]  Cd Length: 454  Bit Score: 230.90  E-value: 3.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    6 ILLLVSLGYAALLFGVAWWGDHR------PLYPERPWLRPAVYSLALAVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLL 79
Cdd:cd10322     1 IDLIIVVVYLALLLGIGLYASKKvkssedFFLAGRSLGPWLLAGTLAATWISAGSFVGVAGLAYTYGLSAIWYILGAALG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   80 LLFGWRIIerlALIARAENTVSIADFISSRYGrSRRLAALVAVIALVGIVPYLALQYKAVAMSLEVLTGhssagrgIFAD 159
Cdd:cd10322    81 ALLLALFL---APRLRRLGKTTIPETILERYY-SKGLRLLVAIIIIIALIPYLALQLIGGGYILSTLLG-------IPYT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  160 PALYVALLMALFATLFGTRqvdatehhHGMMLAIALESVIKLVAIVAVGVFAWLWLGDHQL-HIADSARTLFQHTPSVG- 237
Cdd:cd10322   150 VAVIIAAVIVILYTVFGGM--------RAVAWTDVIQGIVMLIGVLVAAIFILSKVGGGGFsALAAALPALLLALGPGGg 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  238 -----FISQTLLSFLAVVCLPRQFHVAVVECSDVgDIRRARWLFGAYLVIISAMVVPIASAGVALFGQDSSVvdDAVVLA 312
Cdd:cd10322   222 lgwstILSLILLTGLGVLALPQVFQRILAAKDEK-TARRAFLLAGLLLLLIGFLVALIGLAARALFPDLENP--DLALPT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  313 LPLSQGNTVLALVAYVGGFSAATGMVIVASIALATMVSNDLVMPVLLRRRSSAdaratvasRVLWIRRVAILLLALIAYG 392
Cdd:cd10322   299 LINSLLPPGLAGLVLAGLLAAAMSTADSLLLAASTLFTRDIYKPLINPKASDK--------KLLRVSRIAVVVVGVLALL 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  393 YHRSVANdtTLAAYGLMAFAAVAQFAPGVIGGLYWRGASRKGVETGMVLGFMTWIYTLLLPAAtragwlqpewlvdGPFG 472
Cdd:cd10322   371 LALLPPS--ILLLLSLAAGLLAAALFPPLLGGLFWKRATKAGAIAGIIVGLIVTLVWLLLPLA-------------SPLG 435
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 499349852  473 IgwlqpqqlfgmsgwdplaHGTFWSLLINTGTMMVVS 509
Cdd:cd10322   436 I------------------DPIIPALLVSLIVFVVVS 454
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
676-1002 2.23e-59

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 207.45  E-value: 2.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  676 MLYVGRPVADLIRYNAERGELGEGDIEDQIDRRIRHMRAGSPHVFERTRSDGKVIEMRGQALPGGGYVTSYNDITDYKRA 755
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  756 ERALLDANENLEQRVADRSREAELAQQSKTRFLAAISHDVLQPLNAARLFASALRESHqnNEEQRHLAERVDASLRAAEE 835
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL--DEEQREYLETILRSADRLLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  836 LLDGLLDVSRLDAGGLRPTVEDFDASALMHELAAQYAPVAGSRGLRLQVH--ARALWVRSDRRLLRRVMQNFLANALRYT 913
Cdd:COG0642   160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDlpDDLPTVRGDPDRLRQVLLNLLSNAIKYT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  914 RQG-RIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQPFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQ 992
Cdd:COG0642   240 PEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPF--FRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGK 317
                         330
                  ....*....|
gi 499349852  993 GSMFSILLPR 1002
Cdd:COG0642   318 GTTFTVTLPL 327
PAS_7 pfam12860
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
643-757 5.01e-51

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 432837 [Multi-domain]  Cd Length: 115  Bit Score: 175.03  E-value: 5.01e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   643 LENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLYVGRPVADLIRYNAERGELGEGDIEDQIDRRIRHMRAGSPHVFER 722
Cdd:pfam12860    1 LENMSQGLSVFDADLRLVAWNRRYRELLDLPEDLVQVGVPFEEIIRYNAERGEYGPGDVEAHVRRRLAAARAGSPHYFER 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 499349852   723 TRSDGKVIEMRGQALPGGGYVTSYNDITDYKRAER 757
Cdd:pfam12860   81 ERPDGRVIEIRGNPLPDGGFVTTFTDITERRRAEE 115
PutP COG0591
Na+/proline symporter [Amino acid transport and metabolism];
4-522 4.33e-39

Na+/proline symporter [Amino acid transport and metabolism];


Pssm-ID: 440356 [Multi-domain]  Cd Length: 476  Bit Score: 152.66  E-value: 4.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    4 SWILLLVSLGYAALLFGVAWWGDHR--------------PlyperPWLrpaVYSLALAVYCSSWTFYGAVGSAVRNGIGY 69
Cdd:COG0591     2 STLDLIIIILYLLLLLGIGLYASRRtksledyflagrslG-----WWV---LALSLGATWLSAWTFLGVPGLAYAYGLSA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   70 LPIYLGPLLLLLFGWRIIerlALIARAENTVSIADFISSRYGRSRRLaaLVAVIALVGIVPYLALQYKAVAMSLEVLTGH 149
Cdd:COG0591    74 LWYALGYALGALLLALFF---APRLRRLGALTIPEFLEKRFGRGLRL--LAAIIILLFLLGYLAAQLVALGKLLEALFGI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  150 SSagrgifaDPALYVALLMALFATLFGtrqvdatehhhGMmLAIA----LESVIKLVAIVAVGVFAWLWLGD-HQLHIAD 224
Cdd:COG0591   149 PY-------WLGILIGALIVLLYTVLG-----------GL-RAVAwtdvLQGILMLVGLILLLIVALSALGGfGELFAAL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  225 SARTLFQHTPSVG------FISQTLLSFLAVVCLPrQFHVAVVECSDVGDIRRARWLFGAYLVIISAMVVPIASAGVALF 298
Cdd:COG0591   210 PAPGLLSLFPGLGftgwlaFLGLFLAIGLGYFGQP-HIVQRFLAAKSEKEARKAALIGGLLYLLFYLLAALIGLLARALF 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  299 GQDSSVVDDAVVLALPLSQGNTVLALVAYVGGFSAAtgMVIVAS--IALATMVSNDLVMPVLLRRRSSAdaratvasRVL 376
Cdd:COG0591   289 PDLPLADPDLALPLLILELLPPGLAGLLLAAILAAA--MSTADSqlLAASSVFTRDIYKPFIKPKASDK--------QLL 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  377 WIRRVAILLLALIAYGYhrSVANDTTLAAYGLMAFAAVAQ-FAPGVIGGLYWRGASRKGVETGMVLGFMTWIYTLLLPAa 455
Cdd:COG0591   359 RVSRLAVLVVGLLALLL--ALLFPSSILDLVLLAWGGLGAaLLPPLLLGLFWKRATKAGALAGMIAGLVVVLLWKLLGG- 435
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499349852  456 tragwlqpewlvdGPFGIGWLqpqqlfgmsgwdplaHGTFWSLLINTGTMMVVSARWRPGVDERLRA 522
Cdd:COG0591   436 -------------PLGPFGWL---------------YPILPGLLVSLLVFVVVSLLTKPPSEEVLEE 474
PRK15347 PRK15347
two component system sensor kinase;
754-1141 4.03e-35

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 145.17  E-value: 4.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  754 RAERALLDA-NE---NLEQRVADRSRE-------AELAQQSKTRFLAAISHDVLQPLNAArLFASALRESHQNNEEQRHL 822
Cdd:PRK15347  357 KAYNQLLDTlNEqydTLENKVAERTQAlaeakqrAEQANKRKSEHLTTISHEIRTPLNGV-LGALELLQNTPLTAEQMDL 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  823 AERVDASLRAAEELLDGLLDVSRLDAGGLRPTVEDFDASAL----MHELAAQyapvAGSRGLRLQVHARA---LWVRSDR 895
Cdd:PRK15347  436 ADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLldqaMLTIQGP----AQSKSLTLRTFVGAhvpLYLHLDS 511
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  896 RLLRRVMQNFLANALRYTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQpfDWGEQGLGLGLSICQR 975
Cdd:PRK15347  512 LRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPF--YQA--DTHSQGTGLGLTIASS 587
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  976 ISRLLDHDLSARSQVGQGSMFSILLPRVDAVP--------AAPV---PVLA---VRPQASGDS----------LAG---- 1027
Cdd:PRK15347  588 LAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPpeplkgelSAPLalhRQLSawgITCQPGHQNpalldpelayLPGrlyd 667
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1028 -----------------------LRVLCVDN---DREILDGMRALLGRwqvEVITASTVDQALELARE-RPDVMLVDYhl 1080
Cdd:PRK15347  668 llqqiiqgapnepvinlplqpwqLQILLVDDvetNRDIIGMMLVELGQ---QVTTAASGTEALELGRQhRFDLVLMDI-- 742
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499349852 1081 hdRLDGLDTLDALQ-----AAAVDP----IAgalLTADGRDELKQLARQRGYR-LLTKPVKPASLRAFLSA 1141
Cdd:PRK15347  743 --RMPGLDGLETTQlwrddPNNLDPdcmiVA---LTANAAPEEIHRCKKAGMNhYLTKPVTLAQLARALEL 808
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
894-1001 1.26e-28

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 110.82  E-value: 1.26e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    894 DRRLLRRVMQNFLANALRYT-RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEqGLGLGLSI 972
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIG-GTGLGLSI 80
                            90       100
                    ....*....|....*....|....*....
gi 499349852    973 CQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
898-1000 3.30e-26

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: 103.84  E-value: 3.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRQ-GRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQPFDWGEQGLGLGLSICQRI 976
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPgGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERF--YRGDKSREGGGTGLGLAIVRRI 78
                          90       100
                  ....*....|....*....|....
gi 499349852  977 SRLLDHDLSARSQVGQGSMFSILL 1000
Cdd:cd00075    79 VEAHGGRITVESEPGGGTTFTVTL 102
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1024-1142 2.14e-19

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: 85.29  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1024 SLAGLRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVDP-I 1101
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAgPPDLILLDINMPG-MDGLELLRRIRALPRLPdI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499349852 1102 AGALLTADGRDELKQLARQRG-YRLLTKPVKPASLRAFLSAY 1142
Cdd:COG0784    81 PIIALTAYADEEDRERALEAGaDDYLTKPVDPEELLEALRRL 122
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1031-1129 2.39e-16

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: 75.34  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1031 LCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVDpIAGALLTAD 1109
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREeRPDLVLLDLMMPG-MDGLELLRKLRELPPD-IPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 499349852 1110 GRDELKQLARQRG-YRLLTKP 1129
Cdd:cd00156    79 ADEEDAVRALELGaDDYLVKP 99
PAS COG2202
PAS domain [Signal transduction mechanisms];
552-759 3.01e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.13  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  552 AERVVGERHAHRAFLDQAQLLERELQPTAVADRAWvQFTERLLAASIGAASARLVLTSLLRGSGMELGEVVAVLD----- 626
Cdd:COG2202    48 AEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW-RGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDiterk 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  627 EAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRynaergELGEGDIEDQID 706
Cdd:COG2202   127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEEL-LGKSLLDLLH------PEDRERLLELLR 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499349852  707 RRIRHMRAGSPHVFERTRSDGKVIEMRGQALP------GGGYVTSYNDITDYKRAERAL 759
Cdd:COG2202   200 RLLEGGRESYELELRLKDGDGRWVWVEASAVPlrdggeVIGVLGIVRDITERKRAEEAL 258
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1030-1137 4.84e-10

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: 57.93  E-value: 4.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  1030 VLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLhDRLDGLDTLDALQAAAVD-PIagALLT 1107
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEeRPDLILLDINM-PGMDGLELLKRIRRRDPTtPV--IILT 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 499349852  1108 ADGRDELKQLARQRG-YRLLTKPVKPASLRA 1137
Cdd:pfam00072   78 AHGDEDDAVEALEAGaDDFLSKPFDPDELLA 108
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
637-759 1.26e-09

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 57.30  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   637 EILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGY-PDGMLyvGRPVADLIRynaergelgEGDIEdQIDRRIRHMRAG 715
Cdd:TIGR00229    3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYsAEELI--GRNVLELIP---------EEDRE-EVRERIERRLEG 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 499349852   716 SPHV----FERTRSDGKVI--EMRGQALP--GG--GYVTSYNDITDYKRAERAL 759
Cdd:TIGR00229   71 EPEPvseeRRVRRKDGSEIwvEVSVSPIRtnGGelGVVGIVRDITERKEAEEAL 124
sss TIGR00813
transporter, SSS family; The Solute:Sodium Symporter (SSS) Family (TC 2.A.21) Members of the ...
45-442 2.08e-09

transporter, SSS family; The Solute:Sodium Symporter (SSS) Family (TC 2.A.21) Members of the SSS family catalyze solute:Na+ symport. The solutes transported may be sugars, amino acids, nucleosides, inositols, vitamins, urea or anions, depending on the system. Members of the SSS family have been identified in bacteria, archaea and animals, and all functionally well characterized members catalyze solute uptake via Na+ symport. Proteins of the SSS generally share a core of 13 TMSs, but different members of the family may have different numbers of TMSs. A 13 TMS topology with a periplasmic N-terminus and a cytoplasmic C-terminus has been experimentally determined for the proline:Na+ symporter, PutP, of E. coli. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273282 [Multi-domain]  Cd Length: 407  Bit Score: 61.16  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    45 ALAVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLLLLFGWRIIerlALIARAENTVSIADFISSRYGrSRRLAALVAVIA 124
Cdd:TIGR00813   14 LFASYISASQFLGLPGAIYAYGFAIGFYELGALVLLIILGWLF---VPIFINNGAYTMPEYLEKRFG-KRILRGLSVLSL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   125 LVGIVPYLALQYKAVAMSLEVLTGHSsagrgifadpaLYVALLMALFATLF-----GTRQVDATEHHHGMMLaIALESVI 199
Cdd:TIGR00813   90 ILYIFLYMSVDLFSGALLIELITGLD-----------LYLSLLLLGAITILytvfgGLKAVVWTDTIQAVIM-ILGTFIL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   200 KLVAIVAVGVFAWLWLGDHQLHIADSARTLFQHTPSVGFISQTLLSFLAVvclpRQFHVAV------------VECSDVG 267
Cdd:TIGR00813  158 PVFAFSEVGGLGTFVEKASQAAPTNPSPDDLYDFFRDPSTSDLPWGAGVF----GLPHVALwywtnqvivqrcLAAKSAK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   268 DIRRARWLFGAYLVIISAMVVPIASAGVALF--------GQDSSVVDDAVVLALPLSQGNTVLAL---VAYVGGFSAATG 336
Cdd:TIGR00813  234 HAKKGCLISGVLKLLPMFGAVLPGLIARALYtdidpalaGAVNQNSDQAYPLLVQELMPPGLAGLflaAILAAVMSTLSS 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   337 MVIVASialaTMVSNDLVMPvllRRRSSADARATVASRVLWIRRVAILLLALIAYGYHRSVandttlaaYGLMAFA---A 413
Cdd:TIGR00813  314 QLNSAS----TVFTMDLYKK---IIRPNASGEKKIVMRGRIAVLVAAVIAGFVAAAQGGQV--------LQYVQEAfggL 378
                          410       420
                   ....*....|....*....|....*....
gi 499349852   414 VAQFAPGVIGGLYWRGASRKGVETGMVLG 442
Cdd:TIGR00813  379 GAPFLPVFLLGIFWKRMNAKGALAGMIAG 407
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1028-1080 1.84e-07

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: 48.72  E-value: 1.84e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 499349852   1028 LRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHL 1080
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEeKPDLILLDIMM 54
SSF pfam00474
Sodium:solute symporter family; This family includes Swiss:P33413 which is not in the Prosite ...
47-442 3.11e-07

Sodium:solute symporter family; This family includes Swiss:P33413 which is not in the Prosite entry. Membership of this family is supported by a significant blast score.


Pssm-ID: 109527 [Multi-domain]  Cd Length: 406  Bit Score: 54.27  E-value: 3.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    47 AVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLLLLF-GWRIIERLaliaRAENTVSIADFISSRYGRSRRLAALVAVIAL 125
Cdd:pfam00474   19 ASYMSAASFVGLAGAGAASGLAGGLYAIGALVGVWLlLWLFAPRL----RNLGAYTMPDYLRKRFGGKRILVYLSALSLL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   126 VGIVPYLALQYKAVAMSLEVLTGHSsagrgiFADPALYVALLMALFATLFGTRQVDATEHHHGMMLAIALeSVIKLVAIV 205
Cdd:pfam00474   95 LYFFTYMSVQIVGGARLIELALGLN------YYTAVLLLGALTAIYTFFGGFLAVSWTDTIQAVLMLFGT-IILMIIVFH 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   206 AVGVFAWLWlgDHQLHIADSARTLFQHTPSVGFIS-QTLLSFLAVVCL---PRQfhVAVVEC---SDVGDIRRARWLFGA 278
Cdd:pfam00474  168 EVGGYSSAV--EKYMTADPNGVDLYTPDGLHILRDpLTGLSLWPGLVLgttGLP--HILQRClaaKDAKCIRCGVLILTP 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   279 YLVIISAMVVPIASAGVALFGqdssVVDDAVVLALPLSQGNTVLALVAYVGGFSA--------ATGMVIVASIALATmvS 350
Cdd:pfam00474  244 MFIIVMPGMISRGLFAIALAG----ANPRACGTVVGCSNIAYPTLAVKLGPPGLAgimlavmlAAIMSTLTSQLLSS--S 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   351 NDLVMPVLLRRRSSADARATVASRVLWIRRVAILLLALIAYgyhrSVANDTTLAAYGLMAFA-AVAQFAPGVIGGLYWRG 429
Cdd:pfam00474  318 SAFTHDLYKNIRRKASATEKELVGRSRIIVLVVISLAILLA----VQPAQMGIAFLVQLAFAgLGSAFLPVILLAIFWKR 393
                          410
                   ....*....|...
gi 499349852   430 ASRKGVETGMVLG 442
Cdd:pfam00474  394 VNEQGALWGMIIG 406
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
637-687 5.26e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.39  E-value: 5.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 499349852    637 EILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLI 687
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEEL-IGKSLLELI 50
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1029-1139 3.14e-04

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 43.64  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARERPDVMLVDYhLHDRLDGLDTLDALQAAAVDPIagALLTA 1108
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDV-MMPKKNGIDTLKELRQTHQTPV--IMLTA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499349852 1109 DGRDelkqLARQRGYRL-----LTKPVKP----ASLRAFL 1139
Cdd:PRK10955   80 RGSE----LDRVLGLELgaddyLPKPFNDrelvARIRAIL 115
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
637-696 2.59e-03

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 37.53  E-value: 2.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   637 EILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLYVGRPVADLIRYNAERGEL 696
Cdd:pfam13188    1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALEL 60
 
Name Accession Description Interval E-value
SLC5sbd cd10322
Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding ...
6-509 3.49e-66

Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding domain; This family represents the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporter family or solute sodium symporter family) that co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. Family members include: the human glucose (SGLT1, 2, 4, 5), chiro-inositol (SGLT5), myo-inositol (SMIT), choline (CHT), iodide (NIS), multivitamin (SMVT), and monocarboxylate (SMCT) cotransporters, as well as Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. Vibrio parahaemolyticus Na(+)/galactose cotransporter (vSGLT) has 13 transmembrane helices (TMs): TM-1, an inverted topology repeat: TMs1-5 and TMs6-10, and TMs 11-12 (TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). One member of this family, human SGLT3, has been characterized as a glucose sensor and not a transporter. Members of this family are important in human physiology and disease.


Pssm-ID: 271357 [Multi-domain]  Cd Length: 454  Bit Score: 230.90  E-value: 3.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    6 ILLLVSLGYAALLFGVAWWGDHR------PLYPERPWLRPAVYSLALAVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLL 79
Cdd:cd10322     1 IDLIIVVVYLALLLGIGLYASKKvkssedFFLAGRSLGPWLLAGTLAATWISAGSFVGVAGLAYTYGLSAIWYILGAALG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   80 LLFGWRIIerlALIARAENTVSIADFISSRYGrSRRLAALVAVIALVGIVPYLALQYKAVAMSLEVLTGhssagrgIFAD 159
Cdd:cd10322    81 ALLLALFL---APRLRRLGKTTIPETILERYY-SKGLRLLVAIIIIIALIPYLALQLIGGGYILSTLLG-------IPYT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  160 PALYVALLMALFATLFGTRqvdatehhHGMMLAIALESVIKLVAIVAVGVFAWLWLGDHQL-HIADSARTLFQHTPSVG- 237
Cdd:cd10322   150 VAVIIAAVIVILYTVFGGM--------RAVAWTDVIQGIVMLIGVLVAAIFILSKVGGGGFsALAAALPALLLALGPGGg 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  238 -----FISQTLLSFLAVVCLPRQFHVAVVECSDVgDIRRARWLFGAYLVIISAMVVPIASAGVALFGQDSSVvdDAVVLA 312
Cdd:cd10322   222 lgwstILSLILLTGLGVLALPQVFQRILAAKDEK-TARRAFLLAGLLLLLIGFLVALIGLAARALFPDLENP--DLALPT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  313 LPLSQGNTVLALVAYVGGFSAATGMVIVASIALATMVSNDLVMPVLLRRRSSAdaratvasRVLWIRRVAILLLALIAYG 392
Cdd:cd10322   299 LINSLLPPGLAGLVLAGLLAAAMSTADSLLLAASTLFTRDIYKPLINPKASDK--------KLLRVSRIAVVVVGVLALL 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  393 YHRSVANdtTLAAYGLMAFAAVAQFAPGVIGGLYWRGASRKGVETGMVLGFMTWIYTLLLPAAtragwlqpewlvdGPFG 472
Cdd:cd10322   371 LALLPPS--ILLLLSLAAGLLAAALFPPLLGGLFWKRATKAGAIAGIIVGLIVTLVWLLLPLA-------------SPLG 435
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 499349852  473 IgwlqpqqlfgmsgwdplaHGTFWSLLINTGTMMVVS 509
Cdd:cd10322   436 I------------------DPIIPALLVSLIVFVVVS 454
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
676-1002 2.23e-59

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 207.45  E-value: 2.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  676 MLYVGRPVADLIRYNAERGELGEGDIEDQIDRRIRHMRAGSPHVFERTRSDGKVIEMRGQALPGGGYVTSYNDITDYKRA 755
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  756 ERALLDANENLEQRVADRSREAELAQQSKTRFLAAISHDVLQPLNAARLFASALRESHqnNEEQRHLAERVDASLRAAEE 835
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL--DEEQREYLETILRSADRLLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  836 LLDGLLDVSRLDAGGLRPTVEDFDASALMHELAAQYAPVAGSRGLRLQVH--ARALWVRSDRRLLRRVMQNFLANALRYT 913
Cdd:COG0642   160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDlpDDLPTVRGDPDRLRQVLLNLLSNAIKYT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  914 RQG-RIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQPFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQ 992
Cdd:COG0642   240 PEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPF--FRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGK 317
                         330
                  ....*....|
gi 499349852  993 GSMFSILLPR 1002
Cdd:COG0642   318 GTTFTVTLPL 327
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
769-1005 5.33e-59

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 202.83  E-value: 5.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  769 RVADRSREAELAQQSKTRFLAAISHDVLQPLNAARLFASALRESHQ-NNEEQRHLAERVDASLRAAEELLDGLLDVSRLD 847
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDlSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  848 AGGLRPTVEDFDASALMHELAAQYAPVAGSRGLRLQVH--ARALWVRSDRRLLRRVMQNFLANALRYTRQG-RIVLGMRG 924
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDlpPELPLVYADPELLEQVLANLLDNAIKYSPPGgTITISARR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  925 RGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQPFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLPRVD 1004
Cdd:COG2205   161 EGDGVRISVSDNGPGIPEEELERIFERF--YRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238

                  .
gi 499349852 1005 A 1005
Cdd:COG2205   239 S 239
PAS_7 pfam12860
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
643-757 5.01e-51

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 432837 [Multi-domain]  Cd Length: 115  Bit Score: 175.03  E-value: 5.01e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   643 LENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLYVGRPVADLIRYNAERGELGEGDIEDQIDRRIRHMRAGSPHVFER 722
Cdd:pfam12860    1 LENMSQGLSVFDADLRLVAWNRRYRELLDLPEDLVQVGVPFEEIIRYNAERGEYGPGDVEAHVRRRLAAARAGSPHYFER 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 499349852   723 TRSDGKVIEMRGQALPGGGYVTSYNDITDYKRAER 757
Cdd:pfam12860   81 ERPDGRVIEIRGNPLPDGGFVTTFTDITERRRAEE 115
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
622-1005 2.69e-48

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 177.44  E-value: 2.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  622 VAVLDEAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLYVGRPVADLIRYNAERGELGEGDI 701
Cdd:COG5002     2 LLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  702 EDQIDRRIRHMRAGSPHVFERTRSDGKVIEMRGQALPGGGYVTSYNDITDYKRAERALLDANENLEQRVADRS-REAELA 780
Cdd:COG5002    82 ALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDiTELERL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  781 QQSKTRFLAAISHDVLQPLNAARLFASALRES-HQNNEEQRHLAERVDASLRAAEELLDGLLDVSRLDAGGLRPTVEDFD 859
Cdd:COG5002   162 EQMRREFVANVSHELRTPLTSIRGYLELLLDGaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  860 ASALMHELAAQYAPVAGSRGLRLQVHARA--LWVRSDRRLLRRVMQNFLANALRYTRQG-RIVLGMRGRGAQVELQVWDT 936
Cdd:COG5002   242 LAELLEEVVEELRPLAEEKGIELELDLPEdpLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSLREEDDQVRISVRDT 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499349852  937 GPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLPRVDA 1005
Cdd:COG5002   322 GIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
516-1005 4.80e-44

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 168.04  E-value: 4.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  516 VDERLRAAPFLDPYSQRPAVAGEWPGHVHVADLQALAERVVGERHAHRAFLDQAQLLERELQPTAVADRAWVQFTERLLA 595
Cdd:COG4251    14 LLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  596 ASIGAASARLVLTSLLRGSGMELGEVVAVLDEAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDG 675
Cdd:COG4251    94 LALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  676 MLYVGRPVADLIRYNAERGELGEGDIEDQIDRRIRHMRAGSPHVFERTRSDGKVIEMRGQALPGGGYVTSYNDITDYKRA 755
Cdd:COG4251   174 ALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLE 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  756 ERALLDANENLEQRVADRSREAELAQQSKTRFLAAISHDVLQPLNAARLFASALRESH--QNNEEQRHLAERVDASLRAA 833
Cdd:COG4251   254 LLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDYgdKLDEEGREYLERIRDAAERM 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  834 EELLDGLLDVSRLDAGGLRPtvEDFDASALMHELAAQYAPVAGSRGLRLQVhARALWVRSDRRLLRRVMQNFLANALRYT 913
Cdd:COG4251   334 QALIDDLLAYSRVGRQELEF--EPVDLNELLEEVLEDLEPRIEERGAEIEV-GPLPTVRGDPTLLRQVFQNLISNAIKYS 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  914 R---QGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDwgEQGLGLGLSICQRISRLLDHDLSARSQV 990
Cdd:COG4251   411 RpgePPRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDE--YEGTGIGLAIVKKIVERHGGRIWVESEP 488
                         490
                  ....*....|....*
gi 499349852  991 GQGSMFSILLPRVDA 1005
Cdd:COG4251   489 GEGATFYFTLPKAPA 503
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
617-1007 1.23e-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: 164.75  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  617 ELGEVVAV-------LDEAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLiry 689
Cdd:COG5000    63 EIGELARAfnrmtdqLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEEL-IGKPLEEL--- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  690 naergeLGEGDIEDQIDRRIRHmraGSPHVFERTRSDGKVIEMRGQALPGGGYVTSYNDITDYKRAER--ALldanenle 767
Cdd:COG5000   139 ------LPELDLAELLREALER---GWQEEIELTRDGRRTLLVRASPLRDDGYVIVFDDITELLRAERlaAW-------- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  768 QRVAdrsreaelaqqsktrflAAISHDVLQPLNAARLFASALRE--SHQNNEEQRHLAERVDASLRAAEEL---LDGLLD 842
Cdd:COG5000   202 GELA-----------------RRIAHEIKNPLTPIQLSAERLRRklADKLEEDREDLERALDTIIRQVDRLkriVDEFLD 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  843 VSRLDAgglrPTVEDFDASALMHELAAQYAPVAGSRG--LRLQVHARALWVRSDRRLLRRVMQNFLANALRYT-RQGRIV 919
Cdd:COG5000   265 FARLPE----PQLEPVDLNELLREVLALYEPALKEKDirLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIeEGGEIE 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  920 LGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEF---RryqqpfdwgEQGLGLGLSICQRIsrLLDHD--LSARSQVGQGS 994
Cdd:COG5000   341 VSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFfttK---------PKGTGLGLAIVKKI--VEEHGgtIELESRPGGGT 409
                         410
                  ....*....|...
gi 499349852  995 MFSILLPRVDAVP 1007
Cdd:COG5000   410 TFTIRLPLAEEAE 422
PutP COG0591
Na+/proline symporter [Amino acid transport and metabolism];
4-522 4.33e-39

Na+/proline symporter [Amino acid transport and metabolism];


Pssm-ID: 440356 [Multi-domain]  Cd Length: 476  Bit Score: 152.66  E-value: 4.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    4 SWILLLVSLGYAALLFGVAWWGDHR--------------PlyperPWLrpaVYSLALAVYCSSWTFYGAVGSAVRNGIGY 69
Cdd:COG0591     2 STLDLIIIILYLLLLLGIGLYASRRtksledyflagrslG-----WWV---LALSLGATWLSAWTFLGVPGLAYAYGLSA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   70 LPIYLGPLLLLLFGWRIIerlALIARAENTVSIADFISSRYGRSRRLaaLVAVIALVGIVPYLALQYKAVAMSLEVLTGH 149
Cdd:COG0591    74 LWYALGYALGALLLALFF---APRLRRLGALTIPEFLEKRFGRGLRL--LAAIIILLFLLGYLAAQLVALGKLLEALFGI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  150 SSagrgifaDPALYVALLMALFATLFGtrqvdatehhhGMmLAIA----LESVIKLVAIVAVGVFAWLWLGD-HQLHIAD 224
Cdd:COG0591   149 PY-------WLGILIGALIVLLYTVLG-----------GL-RAVAwtdvLQGILMLVGLILLLIVALSALGGfGELFAAL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  225 SARTLFQHTPSVG------FISQTLLSFLAVVCLPrQFHVAVVECSDVGDIRRARWLFGAYLVIISAMVVPIASAGVALF 298
Cdd:COG0591   210 PAPGLLSLFPGLGftgwlaFLGLFLAIGLGYFGQP-HIVQRFLAAKSEKEARKAALIGGLLYLLFYLLAALIGLLARALF 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  299 GQDSSVVDDAVVLALPLSQGNTVLALVAYVGGFSAAtgMVIVAS--IALATMVSNDLVMPVLLRRRSSAdaratvasRVL 376
Cdd:COG0591   289 PDLPLADPDLALPLLILELLPPGLAGLLLAAILAAA--MSTADSqlLAASSVFTRDIYKPFIKPKASDK--------QLL 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  377 WIRRVAILLLALIAYGYhrSVANDTTLAAYGLMAFAAVAQ-FAPGVIGGLYWRGASRKGVETGMVLGFMTWIYTLLLPAa 455
Cdd:COG0591   359 RVSRLAVLVVGLLALLL--ALLFPSSILDLVLLAWGGLGAaLLPPLLLGLFWKRATKAGALAGMIAGLVVVLLWKLLGG- 435
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499349852  456 tragwlqpewlvdGPFGIGWLqpqqlfgmsgwdplaHGTFWSLLINTGTMMVVSARWRPGVDERLRA 522
Cdd:COG0591   436 -------------PLGPFGWL---------------YPILPGLLVSLLVFVVVSLLTKPPSEEVLEE 474
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
631-1009 6.62e-38

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 146.14  E-value: 6.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  631 ELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRYNAErgelgegdIEDQIDRRIR 710
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEEL-LGRPLAELFPEDSP--------LRELLERALA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  711 HMRAGSPHVFERTRSDGKVIEMRGQALP------GGGYVTSYNDITDYKRAERalldanenleqrvadrsREAELAQQSK 784
Cdd:COG3852    72 EGQPVTEREVTLRRKDGEERPVDVSVSPlrdaegEGGVLLVLRDITERKRLER-----------------ELRRAEKLAA 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  785 TRFLAA-ISHDVLQPLNAARLFASALRESHQNNEEQRHLAERVDASLRAAeELLDGLLDVSRldagGLRPTVEDFDasal 863
Cdd:COG3852   135 VGELAAgLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLN-NLVDRLLSFSR----PRPPEREPVN---- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  864 MHELAAQYAPVAGS---RGLRLQVH-ARALW-VRSDRRLLRRVMQNFLANAL-------------RYTRQGRIvlGMRGR 925
Cdd:COG3852   206 LHEVLERVLELLRAeapKNIRIVRDyDPSLPeVLGDPDQLIQVLLNLVRNAAeampeggtitirtRVERQVTL--GGLRP 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  926 GAQVELQVWDTGPGIPEHHMRQIFEEF---RryqqpfdwgEQGLGLGLSICQRISRllDHD--LSARSQVGQGSMFSILL 1000
Cdd:COG3852   284 RLYVRIEVIDNGPGIPEEILDRIFEPFfttK---------EKGTGLGLAIVQKIVE--QHGgtIEVESEPGKGTTFRIYL 352

                  ....*....
gi 499349852 1001 PRVDAVPAA 1009
Cdd:COG3852   353 PLEQAEEEP 361
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
680-1003 1.37e-35

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 139.55  E-value: 1.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  680 GRPVADLIRYNAERGELGEGDIEDQIDRRIRHMRAGSPHVFERTRSDGKVIEMRGQALPGGGYVTSYNDITDYKRAERAL 759
Cdd:COG4191    33 LALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELEEL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  760 LDANENLEQRVADRSR-EAELAQQSKT----RFLAAISHDVLQPLNAARLFASALRESHQNNEEQRHLAERVDASLRAAE 834
Cdd:COG4191   113 ERDITELERAEEELRElQEQLVQSEKLaalgELAAGIAHEINNPLAAILGNAELLRRRLEDEPDPEELREALERILEGAE 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  835 ---ELLDGLLDVSRLDAGGLRPtvedFDASALMHELAAQYAPVAGSRG--LRLQVHARALWVRSDRRLLRRVMQNFLAN- 908
Cdd:COG4191   193 raaEIVRSLRAFSRRDEEEREP----VDLNELIDEALELLRPRLKARGieVELDLPPDLPPVLGDPGQLEQVLLNLLINa 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  909 --ALRYTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEefrryqqPF----DWGEqGLGLGLSICQRISRLLDH 982
Cdd:COG4191   269 idAMEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFE-------PFfttkPVGK-GTGLGLSISYGIVEKHGG 340
                         330       340
                  ....*....|....*....|.
gi 499349852  983 DLSARSQVGQGSMFSILLPRV 1003
Cdd:COG4191   341 RIEVESEPGGGTTFTITLPLA 361
PRK15347 PRK15347
two component system sensor kinase;
754-1141 4.03e-35

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 145.17  E-value: 4.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  754 RAERALLDA-NE---NLEQRVADRSRE-------AELAQQSKTRFLAAISHDVLQPLNAArLFASALRESHQNNEEQRHL 822
Cdd:PRK15347  357 KAYNQLLDTlNEqydTLENKVAERTQAlaeakqrAEQANKRKSEHLTTISHEIRTPLNGV-LGALELLQNTPLTAEQMDL 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  823 AERVDASLRAAEELLDGLLDVSRLDAGGLRPTVEDFDASAL----MHELAAQyapvAGSRGLRLQVHARA---LWVRSDR 895
Cdd:PRK15347  436 ADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLldqaMLTIQGP----AQSKSLTLRTFVGAhvpLYLHLDS 511
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  896 RLLRRVMQNFLANALRYTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQpfDWGEQGLGLGLSICQR 975
Cdd:PRK15347  512 LRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPF--YQA--DTHSQGTGLGLTIASS 587
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  976 ISRLLDHDLSARSQVGQGSMFSILLPRVDAVP--------AAPV---PVLA---VRPQASGDS----------LAG---- 1027
Cdd:PRK15347  588 LAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPpeplkgelSAPLalhRQLSawgITCQPGHQNpalldpelayLPGrlyd 667
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1028 -----------------------LRVLCVDN---DREILDGMRALLGRwqvEVITASTVDQALELARE-RPDVMLVDYhl 1080
Cdd:PRK15347  668 llqqiiqgapnepvinlplqpwqLQILLVDDvetNRDIIGMMLVELGQ---QVTTAASGTEALELGRQhRFDLVLMDI-- 742
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499349852 1081 hdRLDGLDTLDALQ-----AAAVDP----IAgalLTADGRDELKQLARQRGYR-LLTKPVKPASLRAFLSA 1141
Cdd:PRK15347  743 --RMPGLDGLETTQlwrddPNNLDPdcmiVA---LTANAAPEEIHRCKKAGMNhYLTKPVTLAQLARALEL 808
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
894-1001 1.26e-28

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 110.82  E-value: 1.26e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    894 DRRLLRRVMQNFLANALRYT-RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEqGLGLGLSI 972
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIG-GTGLGLSI 80
                            90       100
                    ....*....|....*....|....*....
gi 499349852    973 CQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
898-1000 3.30e-26

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: 103.84  E-value: 3.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRQ-GRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQPFDWGEQGLGLGLSICQRI 976
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPgGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERF--YRGDKSREGGGTGLGLAIVRRI 78
                          90       100
                  ....*....|....*....|....
gi 499349852  977 SRLLDHDLSARSQVGQGSMFSILL 1000
Cdd:cd00075    79 VEAHGGRITVESEPGGGTTFTVTL 102
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
898-1001 7.28e-26

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: 102.96  E-value: 7.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRQGRIVL-----GMRGRGAQVELQVWDTGPGIPEHHMRQIFEEF--------RRYQqpfdwgeq 964
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLrvsleEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFsqadssttRKYG-------- 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499349852  965 GLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16922    73 GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
617-1002 1.82e-25

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 112.75  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  617 ELGEVVAVLDEAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRYNAE---- 692
Cdd:PRK11360  242 ELGEISQAINNLAQALRETRSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHEL-VGKPYSELFPPNTPfasp 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  693 -RGELGEGdiEDQIDRRIRHmragspHVFERTR----SDGKVIEMRGQALpggGYVTSYNDITDYKRAERalldanenle 767
Cdd:PRK11360  321 lLDTLEHG--TEHVDLEISF------PGRDRTIelsvSTSLLHNTHGEMI---GALVIFSDLTERKRLQR---------- 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  768 qRVADRSREAELAqqsktRFLAAISHDVLQPLNAARLFASALRESHQNNEEQRHLAErVDASLRAAEELLDGLLDVSRLD 847
Cdd:PRK11360  380 -RVARQERLAALG-----ELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSV-VLREVDRLNKVIDQLLEFSRPR 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  848 agglRPTVEDFDASALMHELAAQYAPVAGSRGLRLQVH-ARAL-WVRSDRRLLRRVMQNFLANALR-YTRQGRIVLGMRG 924
Cdd:PRK11360  453 ----ESQWQPVSLNALVEEVLQLFQTAGVQARVDFETElDNELpPIWADPELLKQVLLNILINAVQaISARGKIRIRTWQ 528
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499349852  925 RGA-QVELQVWDTGPGIPEHHMRQIFEEFrryqqpFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLPR 1002
Cdd:PRK11360  529 YSDgQVAVSIEDNGCGIDPELLKKIFDPF------FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
766-1087 3.71e-24

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 109.99  E-value: 3.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  766 LEQRVAdrSREAELAQQSKTRFLAAISHDVLQPLNAArLFASALRESHQNNEEQRHLAERVDASLRAAEELLDGLLDVSR 845
Cdd:PRK11466  428 IEHRQA--RAEAEKASQAKSAFLAAMSHEIRTPLYGI-LGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSA 504
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  846 LDAGGLRPTVED--FDASALMHELAAQYAPVAGSRGLRLQV-HARAL--WVRSDRRLLRRVMQNFLANALRYTRQGRIVL 920
Cdd:PRK11466  505 IEAGGKNVSVSDepFEPRPLLESTLQLMSGRVKGRPIRLATdIADDLptALMGDPRRIRQVITNLLSNALRFTDEGSIVL 584
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  921 GMRGRGAQVELQVWDTGPGIPEHHMRQIFEEF-----RRyqqpfdwgeQGLGLGLSICQRISRLLDHDLSARSQVGQGSM 995
Cdd:PRK11466  585 RSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFvqvsgKR---------GGTGLGLTISSRLAQAMGGELSATSTPEVGSC 655
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  996 FSILLPRVDAVPAAPVPVlavrpqASGDSLAGLRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALE-LARERP-DV 1073
Cdd:PRK11466  656 FCLRLPLRVATAPVPKTV------NQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALEtLQNSEPfAA 729
                         330
                  ....*....|....
gi 499349852 1074 MLVDYHLHDrLDGL 1087
Cdd:PRK11466  730 ALVDFDLPD-YDGI 742
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
630-1001 4.72e-24

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: 107.37  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  630 QELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRYNAERgelgegdiedQIDRRI 709
Cdd:COG5809   134 EALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEEL-IGKSILELIHSDDQE----------NVAAFI 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  710 RHMRAGSPHV---FERTRSDGKVIEMRGQALP------GGGYVTSYNDITDYKRAERALldanenleqRVADR-SREAEL 779
Cdd:COG5809   203 SQLLKDGGIAqgeVRFWTKDGRWRLLEASGAPikkngeVDGIVIIFRDITERKKLEELL---------RKSEKlSVVGEL 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  780 AqqsktrflAAISHDVLQPLNAARLFASALREShqNNEEQRHLAERVDASLRAAEELLDGLLDVSRLDAG-----GLRPT 854
Cdd:COG5809   274 A--------AGIAHEIRNPLTSLKGFIQLLKDT--IDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIkyepkDLNTL 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  855 VED----FDASALMH------ELAAQYAPVAGsrglrlqvharalwvrsDRRLLRRVMQNFLANALRYT-RQGRIVLGMR 923
Cdd:COG5809   344 IEEviplLQPQALLKnvqielELEDDIPDILG-----------------DENQLKQVFINLLKNAIEAMpEGGNITIETK 406
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499349852  924 G-RGAQVELQVWDTGPGIPEHHMRQIFEEFrryqqpFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:COG5809   407 AeDDDKVVISVTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLP 479
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
748-1145 7.84e-24

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 108.49  E-value: 7.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  748 DITDYKRAERALldanenleqrvadrsreaELAQQSKTRFLAAISHDVLQPLNAARLFASALRESHQNNEEQRHLaERVD 827
Cdd:PRK11091  265 DITERKRYQDAL------------------EKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYL-KTIH 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  828 ASlraAEEL---LDGLLDVSRLDAGGLRPTVEDFDASALMHELAAQYAPVAGSRGLRLQVHARA---LWVRSDRRLLRRV 901
Cdd:PRK11091  326 VS---AITLgniFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLplpHKVITDGTRLRQI 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  902 MQNFLANALRYTRQGRIVLGM-RGRGAQVELQVWDTGPGIPEHHMRQIFEEFrrYQQPFDWGEQ---GLGLGLSICQRIS 977
Cdd:PRK11091  403 LWNLISNAVKFTQQGGVTVRVrYEEGDMLTFEVEDSGIGIPEDELDKIFAMY--YQVKDSHGGKpatGTGIGLAVSKRLA 480
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  978 RLLDHDLSARSQVGQGSMFSILLPrvdavpaAPVPVLAVRPQASGDS--LAGLRVLCVDnDREiLDGM--RALLGRWQVE 1053
Cdd:PRK11091  481 QAMGGDITVTSEEGKGSCFTLTIH-------APAVAEEVEDAFDEDDmpLPALNILLVE-DIE-LNVIvaRSVLEKLGNS 551
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1054 VITASTVDQALELAR-ERPDVMLVDYHLHDrLDGLDtldalqaaavdpIAGALLTADGRDELKQL--------ARQRGYR 1124
Cdd:PRK11091  552 VDVAMTGKEALEMFDpDEYDLVLLDIQLPD-MTGLD------------IARELRERYPREDLPPLvaltanvlKDKKEYL 618
                         410       420
                  ....*....|....*....|....*..
gi 499349852 1125 ------LLTKPVKPASLRAFLSAYHDT 1145
Cdd:PRK11091  619 dagmddVLSKPLSVPALTAMIKKFWDT 645
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
894-1001 1.75e-23

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 96.28  E-value: 1.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   894 DRRLLRRVMQNFLANALRYTRQ-GRIVLGMRgRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPfdwGEQGLGLGLSI 972
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKaGEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKR---GGGGTGLGLSI 77
                           90       100
                   ....*....|....*....|....*....
gi 499349852   973 CQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:pfam02518   78 VRKLVELLGGTITVESEPGGGTTVTLTLP 106
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
790-1002 1.95e-23

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 105.31  E-value: 1.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  790 AISHDVLQPLNAARLFASALRESHQNNEEQRHLAERVDASLRAaEELLDGLLDVSRLDAGGLRPTVEDFDASALMHELAA 869
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARL-QQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  870 QYAPVAGSRGLRLQVHARALWVRSDRRLLRRVMQNFLANALRYT-RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQI 948
Cdd:PRK11100  341 AREAQAAAKGITLRLRPDDARVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVDGEQVALSVEDQGPGIPDYALPRI 420
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499349852  949 FEEFRRYQQPfDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLPR 1002
Cdd:PRK11100  421 FERFYSLPRP-ANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
PRK09303 PRK09303
histidine kinase;
763-1001 9.28e-23

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 101.95  E-value: 9.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  763 NENLEQRVadrsreaelaqQSKTRFLAAISHDVLQPLNAARLFASALrESHQNNEE-------QRHLAERVDASLRAAEE 835
Cdd:PRK09303  141 NETLLEQL-----------KFKDRVLAMLAHDLRTPLTAASLALETL-ELGQIDEDtelkpalIEQLQDQARRQLEEIER 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  836 LLDGLLDVSRLDAGGLRPTVEDFDASALMHELAAQYAPVAGSRGLRLQ---------VHAralwvrsDRRLLRRVMQNFL 906
Cdd:PRK09303  209 LITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQtdipsdlpsVYA-------DQERIRQVLLNLL 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  907 ANALRYTR-QGRIVLGMRGRGAQ-VELQVWDTGPGIPEHHMRQIFEEFRRYQQpfDWGEQGLGLGLSICQRISRLLDHDL 984
Cdd:PRK09303  282 DNAIKYTPeGGTITLSMLHRTTQkVQVSICDTGPGIPEEEQERIFEDRVRLPR--DEGTEGYGIGLSVCRRIVRVHYGQI 359
                         250
                  ....*....|....*..
gi 499349852  985 SARSQVGQGSMFSILLP 1001
Cdd:PRK09303  360 WVDSEPGQGSCFHFTLP 376
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
742-1143 1.29e-22

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 105.20  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  742 YVTSYNDITDYKRAERAL-LDANENLEQRVAdrsreaelaqqsKTRFLAAISHDVLQPLNAARLFASALRESHQNNEEQR 820
Cdd:PRK09959  681 YICGWQDITETRDLIHALeVERNKAINATVA------------KSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRV 748
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  821 HLAERVDASLRAAEELLDGLLDVSRLDAGGLRPTVEDFDASALMHELAAQYAPVAGSRGLRLQVHAR---ALWVRSDRRL 897
Cdd:PRK09959  749 EAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfpdHYLVKIDPQA 828
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRQGRI-----VLGMRGRGAQVELQVWDTGPGIPEHHMRQIfeeFRRYQQPFDWGEQ-GLGLGLS 971
Cdd:PRK09959  829 FKQVLSNLLSNALKFTTEGAVkittsLGHIDDNHAVIKMTIMDSGSGLSQEEQQQL---FKRYSQTSAGRQQtGSGLGLM 905
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  972 ICQRISRLLDHDLSARSQVGQGSMFSILLPRVDAVPAAPVPVLAVRPQASGDSLAglrVLCVDN---DREILDGMRALLG 1048
Cdd:PRK09959  906 ICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLS---ILIADDhptNRLLLKRQLNLLG 982
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1049 rwqVEVITASTVDQAL-ELARERPDVMLVDYHLHDrLDGLDTLDALQAAAVD-PIAGalLTADGRDELKQLARQRGYRL- 1125
Cdd:PRK09959  983 ---YDVDEATDGVQALhKVSMQHYDLLITDVNMPN-MDGFELTRKLREQNSSlPIWG--LTANAQANEREKGLSCGMNLc 1056
                         410
                  ....*....|....*...
gi 499349852 1126 LTKPVKPASLRAFLSAYH 1143
Cdd:PRK09959 1057 LFKPLTLDVLKTHLSQLH 1074
PRK10490 PRK10490
sensor protein KdpD; Provisional
758-1007 1.37e-20

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 98.18  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  758 ALLDAN--ENLEQ-RVADRSREAELAQQSKTRFLAAISHDVLQPLNAarLFASA----LRESHQNNEEQRHlAERVDASL 830
Cdd:PRK10490  635 TLLIANalERLTLtASEEQARLASEREQLRNALLAALSHDLRTPLTV--LFGQAeiltLDLASEGSPHARQ-ASEIRQQV 711
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  831 RAAEELLDGLLDVSRLDAGGLR-----PTVEDFDASALmhelaAQYAPVAGSRGLRLQVHARALWVRSDRRLLRRVMQNF 905
Cdd:PRK10490  712 LNTTRLVNNLLDMARIQSGGFNlrkewLTLEEVVGSAL-----QMLEPGLSGHPINLSLPEPLTLIHVDGPLFERVLINL 786
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  906 LANALRYT-RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRyqqpfdwGEQ-----GLGLGLSICQRISRL 979
Cdd:PRK10490  787 LENAVKYAgAQAEIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFAR-------GNKesaipGVGLGLAICRAIVEV 859
                         250       260
                  ....*....|....*....|....*...
gi 499349852  980 LDHDLSARSQVGQGSMFSILLPrVDAVP 1007
Cdd:PRK10490  860 HGGTIWAENRPEGGACFRVTLP-LETPP 886
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
766-1147 6.13e-20

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 96.20  E-value: 6.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  766 LEQRVADRSREAELAQQSKTRFLAAISHDVLQPL-----NAArlfasaLRESHQNNEEqrhlAERVDASLRAAEELL--- 837
Cdd:PRK10841  429 MEESLQEMAQAAEQASQSKSMFLATVSHELRTPLygiigNLD------LLQTKELPKG----VDRLVTAMNNSSSLLlki 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  838 -DGLLDVSRLDAGGLRPTVEDFDASALMHELAAQYAPvagsrglrLQVHAR-ALW----------VRSDRRLLRRVMQNF 905
Cdd:PRK10841  499 iSDILDFSKIESEQLKIEPREFSPREVINHITANYLP--------LVVKKRlGLYcfiepdvpvaLNGDPMRLQQVISNL 570
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  906 LANALRYTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRY----QQPFdwgeQGLGLGLSICQRISRLLD 981
Cdd:PRK10841  571 LSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVgtgvQRNF----QGTGLGLAICEKLINMMD 646
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  982 HDLSARSQVGQGSMFSILLP--RVDAVPAAPVP-------VLAVRPQASGDSL------AGLRVL-----CVDND----- 1036
Cdd:PRK10841  647 GDISVDSEPGMGSQFTIRIPlyGAQYPQKKGVEglqgkrcWLAVRNASLEQFLetllqrSGIQVQryegqEPTPEdvlit 726
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1037 ------------------------REILDG-----------MRALLGR-WQVEVITASTVDQALELARERPD-----VML 1075
Cdd:PRK10841  727 ddpvqkkwqgravitfcrrhigipLEIAPGewvhstatpheLPALLARiYRIELESDDSANALPSTDKAVSDnddmmILV 806
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1076 VDYH------LHDRL-----------DGLDTLDALQAAAVDPIagalLT------ADGRdELKQLARQRGYRL------- 1125
Cdd:PRK10841  807 VDDHpinrrlLADQLgslgyqcktanDGVDALNVLSKNHIDIV----LTdvnmpnMDGY-RLTQRLRQLGLTLpvigvta 881
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 499349852 1126 ------------------LTKPVKPASLRAFLSAYHDTMR 1147
Cdd:PRK10841  882 nalaeekqrcleagmdscLSKPVTLDVLKQTLTVYAERVR 921
PRK10604 PRK10604
sensor protein RstB; Provisional
783-1010 8.87e-20

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 93.51  E-value: 8.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  783 SKTRFLAAISHDVLQPLnaARLfASALRESHQNNEEQRHLAERvdaSLRAAEELLDGLLDVSRLDAGGLRPTVEDFDASA 862
Cdd:PRK10604  211 SKKQLIDGIAHELRTPL--VRL-RYRLEMSDNLSAAESQALNR---DIGQLEALIEELLTYARLDRPQNELHLSEPDLPA 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  863 LMHELAAQYAPVAGSRGLRLQVHARALWVRSDRRLLRRVMQNFLANALRYTRQgRIVLGMRGRGAQVELQVWDTGPGIPE 942
Cdd:PRK10604  285 WLSTHLADIQAVTPEKTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRYAHS-RVRVSLLLDGNQACLIVEDDGPGIPP 363
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499349852  943 HHMRQIFEEFRRYQQPFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLPRVDAVPAAP 1010
Cdd:PRK10604  364 EERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPVWHNLPQFT 431
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
631-1001 1.49e-19

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 93.64  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  631 ELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDgMLYVGRPVADLIRY-NAERgelgegdiedqIDRRI 709
Cdd:COG5805   151 ILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPR-EELIGKNLLELLHPcDKEE-----------FKERI 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  710 RH-MRAGSPHVFERTR--SDGKVI--EMRGQALPGG-----GYVTSYNDITDYKRAERaLLDANENLeqRVAdrsreAEL 779
Cdd:COG5805   219 ESiTEVWQEFIIEREIitKDGRIRyfEAVIVPLIDTdgsvkGILVILRDITEKKEAEE-LMARSEKL--SIA-----GQL 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  780 AqqsktrflAAISHDVLQPLNAARLFASALREshqNNEEQRHLAERVDASLRAAEELLDGLLDVSRLDAGGLRPT----- 854
Cdd:COG5805   291 A--------AGIAHEIRNPLTSIKGFLQLLQP---GIEDKEEYFDIMLSELDRIESIISEFLALAKPQAVNKEKEninel 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  855 VED----FDASALMHELAaqyapvagsrgLRLQVHARALWVRSDRRLLRRVMQNFLANALRYTRQ-GRIVLGMRGRGAQV 929
Cdd:COG5805   360 IQDvvtlLETEAILHNIQ-----------IRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNgGTITIHTEEEDNSV 428
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499349852  930 ELQVWDTGPGIPEHHMRQIFEEFrryqqpFDWGEQGLGLGLSICQRIsrLLDH--DLSARSQVGQGSMFSILLP 1001
Cdd:COG5805   429 IIRVIDEGIGIPEERLKKLGEPF------FTTKEKGTGLGLMVSYKI--IENHngTIDIDSKVGKGTTFTITLP 494
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1024-1142 2.14e-19

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: 85.29  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1024 SLAGLRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVDP-I 1101
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAgPPDLILLDINMPG-MDGLELLRRIRALPRLPdI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499349852 1102 AGALLTADGRDELKQLARQRG-YRLLTKPVKPASLRAFLSAY 1142
Cdd:COG0784    81 PIIALTAYADEEDRERALEAGaDDYLTKPVDPEELLEALRRL 122
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
775-1143 4.46e-19

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 93.38  E-value: 4.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  775 REAELAQQSKTRFLAAISHDVLQPLNAARLFASALRESHQNNEEQRHLA--ERvdaslrAAEELL----DgLLDVSRLDA 848
Cdd:PRK11107  284 KRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQtiER------SANNLLaiinD-ILDFSKLEA 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  849 G---------GLRPTVEDfdasaLMHELAaqyaPVAGSRGLRLQVHaralwVRSD----------RrlLRRVMQNFLANA 909
Cdd:PRK11107  357 GklvlenipfSLRETLDE-----VVTLLA----HSAHEKGLELTLN-----IDPDvpdnvigdplR--LQQIITNLVGNA 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  910 LRYTRQGRIVLGMRGRGA---QVEL--QVWDTGPGIPEHHMRQIFEEF--------RRYqqpfdwGeqGLGLGLSICQRI 976
Cdd:PRK11107  421 IKFTESGNIDILVELRALsntKVQLevQIRDTGIGISERQQSQLFQAFrqadasisRRH------G--GTGLGLVITQKL 492
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  977 SRLLDHDLSARSQVGQGSMFSILLPrVDAVPAAPVPVLAVrpqasgDSLAGLRVLCVDND---REILdgmRALLGRWQVE 1053
Cdd:PRK11107  493 VNEMGGDISFHSQPNRGSTFWFHLP-LDLNPNPIIDGLPT------DCLAGKRLLYVEPNsaaAQAT---LDILSETPLE 562
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1054 VITASTVDQaleLARERPDVMLVDYHLHDRLDGLDTLDALQAAAvdPIAGALLTA------DGRDELKqlarQRGYR-LL 1126
Cdd:PRK11107  563 VTYSPTLSQ---LPEAHYDILLLGLPVTFREPLTMLHERLAKAK--SMTDFLILAlpcheqVLAEQLK----QDGADaCL 633
                         410
                  ....*....|....*...
gi 499349852 1127 TKPV-KPASLRAFLSAYH 1143
Cdd:PRK11107  634 SKPLsHTRLLPALLEPCH 651
SLC5sbd_PutP cd11475
Na(+)/proline cotransporter PutP and related proteins; solute binding domain; Escherichia coli ...
37-453 4.83e-19

Na(+)/proline cotransporter PutP and related proteins; solute binding domain; Escherichia coli PutP catalyzes the Na+-coupled uptake of proline with a stoichiometry of 1:1. The putP gene is part of the put operon; this operon in addition encodes a proline dehydrogenase, allowing the use of proline as a source of nitrogen and/or carbon. This subfamily also includes the Bacillus subtilis Na+/proline cotransporter (OpuE) which has an osmoprotective instead of catabolic role. Expression of the opuE gene is under osmotic control and different sigma factors contribute to its regulation; it is also a putative CcpA-activated gene. This subfamily belongs to the solute carrier 5 (SLC5) transporter family.


Pssm-ID: 271369  Cd Length: 464  Bit Score: 91.80  E-value: 4.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   37 LRPAVYSL-ALAVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLLLLFGWRII-ERLALIARAENTVSIADFISSRYG-RS 113
Cdd:cd11475    35 LGPWVTALsAGASDMSGWLLLGLPGAAYASGLSAIWIAIGLILGAYLNWLFVaKRLRRYTEKNDSITLPDYLENRFRdKS 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  114 RRLAALVAVIALVGIVPYLALQYKAVAMSLEVLTGHSSAGrgifadpALYVALLMALFATLFGtrqvdatehhhGMMLAI 193
Cdd:cd11475   115 KLLRILSALIILIFFTIYAAAQLVAGGKLFESLFGIDYST-------GLLIGAVVVVAYTFLG-----------GFLAVS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  194 ---ALESVIKLVAIVAVGVFAWLWLG------DHQLHIADSARTLFQHTP---SVGFISQTLLSFLAVVCLPrqfHVAV- 260
Cdd:cd11475   177 wtdFFQGLLMLLALVLVPIVALAALGglsglvAALAAIDPGLLSPFGGDLgagGLLAIISLLAWGLGYFGQP---HILVr 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  261 -VECSDVGDIRRARWLFGAYLVIISAMVVPIASAGVALFGQDSSVVDDAVVLALPLSQGNTVLALVAYVGGFSA----AT 335
Cdd:cd11475   254 fMAIRSPKEIKKARRIAMVWMILFLLGAVLVGLLGRALFPDGLLGDPETVFPVLAQELFPPWLAGILLAAILAAimstAD 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  336 GMVIVASIALatmvSNDLVMPVLLRRRSSAdaratvasRVLWIRRVAILLLALIAYGYhrSVANDTTLAAYGLMAFAAV- 414
Cdd:cd11475   334 SQLLVCSSAL----TEDLYKAFLRKEASDK--------ELVWVSRLAVLVIALIALLI--ALNPPSSVFSLVSFAWAGLg 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 499349852  415 AQFAPGVIGGLYWRGASRKGVETGMVLGFMT---WIYTLLLP 453
Cdd:cd11475   400 AAFGPLLLLSLYWKRTTRQGALAGMIAGAVTvvvWKLLGLGI 441
SLC5sbd_u4 cd11480
Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain; SLC5 ...
102-509 2.51e-18

Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain; SLC5 (also called the sodium/glucose cotransporter family or solute sodium symporter family) is a family of proteins that co-transports Na+ with sugars, amino acids, inorganic ions or vitamins. Prokaryotic members of this family include Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. One member of the SLC5 family, human SGLT3, has been characterized as a glucose sensor and not a transporter. This subfamily belongs to the solute carrier 5 (SLC5) transporter family.


Pssm-ID: 271374  Cd Length: 488  Bit Score: 89.49  E-value: 2.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  102 IADFISSRYGrSRRLAALVAVIALVGIVPYLALQYKAVAMSLEVLTGHSSAGrGIFAdpalyVALLMALFATLfgtrqvd 181
Cdd:cd11480    98 VPDFLGARLG-SRPVRLVAAVSTLVISFFYLVAQMVGAGLLLSLLLGIPYEV-GVVV-----VGALMIVYVVL------- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  182 atehhhGMMLAIALESVIK---------LVAIVAVGVFAWLWLGDHQLHIADSA-----------RTLFQHTPSVGFISQ 241
Cdd:cd11480   164 ------GGMRATTWVQIIQyvlllgaflVPAILVLARFGGNPLGAGPGLLGLAAaaasgageaylAPGLLLTDPLDVISL 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  242 TLLSFLAVVCLPrqfHVaVVECSDVGDIRRARWLFGAYLVIIS---AMVVPIASAGVALFGQDSSVVD---------DAV 309
Cdd:cd11480   238 TLALMLGTAGLP---HV-LMRFYTVPDARAARKSVVWALGFIGlfyLLAPALGFGARALVGPDVIGAPiageldgggDMA 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  310 VLALP--LSQGNTVLALVAYVG---GFSAATGMVIVASIALATmvsnDLvMPVLLRRRSSADARATVAsrvlwirRVAIL 384
Cdd:cd11480   314 VLLLPeiAGLGDLLLALVAAGAfaaILATVAGLLLAAASALAH----DL-YAGVIRPGASERREVRVA-------RIAAV 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  385 LLALIA-----YGYHRSVANDTTLAayglMAFAAVAqFAPGVIGGLYWRGASRKGVETGMVLGFmtwIYTLLLPAATRAG 459
Cdd:cd11480   382 VVGVIAillalLFPPQNVAFLVALA----FAIAASA-FFPVLVLGIFWRRFTTRGAIAGMLVGL---LVSLVLIVLSPAV 453
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 499349852  460 WlqPEWLVDGPFGIgwlqpqqlfgmsgwdPLAHGTFWSLLINTGTMMVVS 509
Cdd:cd11480   454 S--GAPPGHDFAGF---------------PLTNPGLVSVPLGFLVAIVVS 486
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
593-1005 1.49e-16

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 82.97  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  593 LLAASIGAASARLVLTSLLRGSGMELGEVVAVLDEAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGY 672
Cdd:COG3290    40 LLFLLFVIILLLLLLILLLILLLLLLLLLAALLLKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLINDAARRLLGL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  673 PdgmlYVGRPVADLIRynaERGELGEGDIEDQIDRRIRHMRAgsphvfERTRSDGKVIemrgqalpggGYVTSYNDITDY 752
Cdd:COG3290   120 D----AIGRPIDEVLA---EVLETGERDEEILLNGRVLVVNR------VPIRDDGRVV----------GAVATFRDRTEL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  753 KRAERALLDANENLEQrvadrsreaelaqqsktrfLAAISHDVLQPLNAARLFAsalreshQNNEEQRhlaervdaslra 832
Cdd:COG3290   177 ERLEEELEGVKELAEA-------------------LRAQRHDFRNHLHTISGLL-------QLGEYDE------------ 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  833 AEELLDGLLDVSRLDAGGLRPTVEDFDASALMHELAAQyapvAGSRGLRLQVHARALWVRS--DRRLLRRVMQNFLANAL 910
Cdd:COG3290   219 ALEYIDEISEELQELIDSLLSRIGNPVLAALLLGKAAR----ARERGIDLTIDIDSDLPDLplSDTDLVTILGNLLDNAI 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  911 RYTRQ-----GRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEfrryqqpfdwG-----EQGLGLGLSICQRISRLL 980
Cdd:COG3290   295 EAVEKlpeeeRRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFER----------GfstklGEGRGLGLALVKQIVEKY 364
                         410       420
                  ....*....|....*....|....*
gi 499349852  981 DHDLSARSQVGQGSMFSILLPRVDA 1005
Cdd:COG3290   365 GGTIEVESEEGEGTVFTVRLPKEGE 389
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1031-1129 2.39e-16

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: 75.34  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1031 LCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVDpIAGALLTAD 1109
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREeRPDLVLLDLMMPG-MDGLELLRKLRELPPD-IPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 499349852 1110 GRDELKQLARQRG-YRLLTKP 1129
Cdd:cd00156    79 ADEEDAVRALELGaDDYLVKP 99
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
887-1000 4.57e-15

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


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 72.93  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  887 RALWVRSDRRLLRRVMQNFLANALRYTRQGRIvLGM--RGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQ 964
Cdd:cd16947    10 RPIYANANTEALQRILKNLISNAIKYGSDGKF-LGMtlREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQ 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499349852  965 GLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILL 1000
Cdd:cd16947    89 GNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
820-1135 4.60e-15

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 80.11  E-value: 4.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  820 RHLAERVDASLRAaEELLDGLLDVSRLDAGGLRPtvedFDASALMHELAAQYApVAGSRGLRLQVH--ARALWVRSDRRL 897
Cdd:PRK13837  487 RYIDEIISAGARA-RLIIDQILAFGRKGERNTKP----FDLSELVTEIAPLLR-VSLPPGVELDFDqdQEPAVVEGNPAE 560
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALR----------------YTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrryqqpFDW 961
Cdd:PRK13837  561 LQQVLMNLCSNAAQamdgagrvdislsrakLRAPKVLSHGVLPPGRYVLLRVSDTGAGIDEAVLPHIFEPF------FTT 634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  962 GEQGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLPRVDAVPAAPVPVLAVRPQASGdslAGLRVLCVDNDREILD 1041
Cdd:PRK13837  635 RAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQAFFGPGPLPRG---RGETVLLVEPDDATLE 711
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1042 ---GMRALLGRWQVEVITASTVDQALELARERPDVMLVDYHLhdrLDGLDTLDALQAAAVDPIAgALLTADGRDELKQLA 1118
Cdd:PRK13837  712 ryeEKLAALGYEPVGFSTLAAAIAWISKGPERFDLVLVDDRL---LDEEQAAAALHAAAPTLPI-ILGGNSKTMALSPDL 787
                         330
                  ....*....|....*..
gi 499349852 1119 RQRGYRLLTKPVKPASL 1135
Cdd:PRK13837  788 LASVAEILAKPISSRTL 804
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1028-1141 8.37e-15

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: 74.82  E-value: 8.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1028 LRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVD---PIag 1103
Cdd:COG3437     7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEaPPDLILLDVRMPG-MDGFELLRLLRADPSTrdiPV-- 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499349852 1104 ALLTADGRDELKQLARQRG-YRLLTKPVKPASLRAFLSA 1141
Cdd:COG3437    84 IFLTALADPEDRERALEAGaDDYLTKPFDPEELLARVRN 122
PRK10337 PRK10337
sensor protein QseC; Provisional
757-987 8.84e-15

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 78.15  E-value: 8.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  757 RALLDANENLEQRVAD---RSReaelaqqsktRFLAAISHDVLQPLNAARLFASALRESHQNNEEQRHLAERVDASLRAA 833
Cdd:PRK10337  217 RPLVEALNQLFARTHAmmvRER----------RFTSDAAHELRSPLAALKVQTEVAQLSDDDPQARKKALLQLHAGIDRA 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  834 EELLDGLLDVSRLDAGGLRPTVEDFDASALMHE-LAAQYAPV-AGSRGLRLQVHARALWVRSDRRLLRRVMQNFLANALR 911
Cdd:PRK10337  287 TRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSaVMDIYHTAqQAGIDVRLTLNAHPVIRTGQPLLLSLLVRNLLDNAIR 366
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499349852  912 YTRQGRIV-LGMRGRgaqvELQVWDTGPGIPEHHMRQIFEEFRRyqqPFDWGEQGLGLGLSICQRISRLldHDLSAR 987
Cdd:PRK10337  367 YSPQGSVVdVTLNAR----NFTVRDNGPGVTPEALARIGERFYR---PPGQEATGSGLGLSIVRRIAKL--HGMNVS 434
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1028-1141 1.55e-14

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: 73.45  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1028 LRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVD-PIagAL 1105
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEeRPDLILLDLMLPG-MDGLEVCRRLRARPSDiPI--IM 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499349852 1106 LTADGRDELKQLARQRG---YrlLTKPVKPASLRAFLSA 1141
Cdd:COG0745    79 LTARDDEEDRVRGLEAGaddY--LTKPFDPEELLARIRA 115
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1029-1137 2.25e-14

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: 76.54  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVITASTVDQALE-LARERPDVMLVDYHLHDrLDGLDTLDALQAAAVDPIAgALLT 1107
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALAlLREEPPDLVLLDLRMPG-MDGLELLRELRALDPDLPV-ILLT 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 499349852 1108 ADGRDELKQLARQRG-YRLLTKPVKPASLRA 1137
Cdd:COG2204    82 GYGDVETAVEAIKAGaFDYLTKPFDLEELLA 112
ActP COG4147
Na+(or H+)/acetate symporter ActP [Energy production and conversion];
101-509 3.51e-14

Na+(or H+)/acetate symporter ActP [Energy production and conversion];


Pssm-ID: 443318  Cd Length: 526  Bit Score: 76.73  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  101 SIADFISSRYgRSRRLAALVAVIALVGIVPYLALQYKAVAMSLEVLTGhSSAGRGIFAdpalyVALLMALFATLfgtrqv 180
Cdd:COG4147   111 TVPDFLGDRF-YSRPARLVAAISTLVVSFFYLIAQMVGAGVLISLLLG-VDYEVAVVI-----VGVLMIVYVVL------ 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  181 datehhhGMMLAI----ALESVIKLVAIVAVGVFAWLWLGDHQLHIADSARTLFQH-----------TPSVGFISQTLLS 245
Cdd:COG4147   178 -------GGMKGTtwvqIIKAVLLIFAYTVPAVLVLAQFGFNPLPLLAKAAEVHDLgaaylepgglvKSPLDFISLGLAL 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  246 FLAVVCLP----RQFHVAvvecsdvgDIRRARWLFGAYLVIISA---MVVPIASAGVALFGQDSSVVD-----------D 307
Cdd:COG4147   251 MLGTAGLPhilmRFFTVP--------DAKEARKSVGWALGFIGLfylTAPALGFGARALVGPLPEWFDtgligaadgggN 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  308 AVVLALP--LSQGNTVLALVAyVGGFsaATGMVIVAS--IALATMVSNDLVMPVLlrrrssaDARATVASRvLWIRRVAI 383
Cdd:COG4147   323 MAVLALAeiAGGGNWLLGLVA-AGAF--ATILAVVAGllLAIASAISHDLYANVI-------KGKATEKEE-LRVARIAA 391
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  384 LLLALIAyGYHRSVANDTTLAAYGLMAFA-AVAQFAPGVIGGLYWRGASRKGVETGMVLGFMTWIYTLLLpaatragwlq 462
Cdd:COG4147   392 VVIGVVA-ILLGINAPPQNVAFLVALAFAlAASANFPVLLLSIFWKRFNTRGAVAGMLVGLISALVLIVL---------- 460
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 499349852  463 pewlvdGPFGIGWLQPQQLFgmsgwdPLAHGTFWSLLINTGTMMVVS 509
Cdd:COG4147   461 ------SPFVWVLGVDAALF------PLENPGLVSMPLGFLVAIVVS 495
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
885-1000 2.71e-13

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: 67.43  E-value: 2.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  885 HARALWVRSDRRLLRRVMQNFLANALRYTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRyqqPFDWGEQ 964
Cdd:cd16940     1 SAADIQVQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYR---SDGQNYG 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499349852  965 GLGLGLSICQRISRLldHDLSARSQVGQGSMFSILL 1000
Cdd:cd16940    78 GSGLGLSIVKRIVEL--HGGQIFLGNAQGGGLEAWV 111
SLC5sbd_CHT cd11474
Na(+)- and Cl(-)-dependent choline cotransporter CHT and related proteins; solute-binding ...
95-448 3.53e-13

Na(+)- and Cl(-)-dependent choline cotransporter CHT and related proteins; solute-binding domain; Na+/choline co-transport by CHT is Cl- dependent. Human CHT (also called CHT1) is encoded by the SLC5A7 gene, and is expressed in the central nervous system. hCHT1-mediated choline uptake may be the rate-limiting step in acetylcholine synthesis, and essential for cholinergic transmission. Changes in this choline uptake in cortical neurons may contribute to Alzheimer's dementia. This subfamily belongs to the solute carrier 5 (SLC5) transporter family.


Pssm-ID: 271368 [Multi-domain]  Cd Length: 464  Bit Score: 73.33  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   95 RAENTVSIADFISSRYGRsrRLAALVAVIALVGIVPYLALQYKAVAMSLEVLTGHSSAgRGIFadpalyVALLMALFATL 174
Cdd:cd11474    92 RRMGLLTLGDFFRQRYGR--RVEVLLSIPAVLSYLGWVAAQLVALGLVLSVILGLPVE-TGIL------ISAAIVLAYTL 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  175 FGtrqvdatehhhGMMlAIALESVIKLVAIVA--VGVFAWLWLGDHQLHIADSARTL-FQHTPSVGfISQTLLSFLAVVC 251
Cdd:cd11474   163 FG-----------GMW-SVAYTDVVQLIVIFVglLVLVPFVLTNPGGVDIASAAAAGkLRFFPWLG-TKSDWLIWIDAWL 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  252 L------PRQ-FHVAVVECSDVgdiRRARW--LFGAYLVIISAMV-VPIASAGVALFGQDSSVVD-DAVVLALPLS-QGN 319
Cdd:cd11474   230 TlglgsiPQQdVFQRVLSAKSE---KTAQRlsLLAGVGYLLFAIPpLLIGLAAASIDPSLTQYGLeEDAQLILPLLlQYL 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  320 TVLAL-VAYVGGFSAATGMVIVASI-ALATMVSNDLVMPVLLRRRSSadaratvaSRVLWIRRVAILLLALIAYgyhrSV 397
Cdd:cd11474   307 TPLWVqVLFLGALLSAVMSTADSALlAPSSVFSENIYKPPFRPKASD--------RELLWVMRISVVVFGAIAT----LM 374
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499349852  398 ANdTTLAAYGLMAFAA----VAQFAPgVIGGLYWRGASRKGVETGMVLGFMTWIY 448
Cdd:cd11474   375 AL-TVESIYGLVELASdlvlVGLFVP-LLAGLYWKRANTYGALAAIIVGLVLRLL 427
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1002 5.68e-13

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: 65.91  E-value: 5.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRQgRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSICQRIS 977
Cdd:cd16939     1 MARALDNLLRNALRYAHR-TVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVA 79
                          90       100
                  ....*....|....*....|....*.
gi 499349852  978 RLLDHDLSA-RSQVGqGSMFSILLPR 1002
Cdd:cd16939    80 LWHGGHVECdDSELG-GACFRLTWPR 104
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1028-1137 6.80e-13

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: 68.01  E-value: 6.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1028 LRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQA-AAVDPIAGAL 1105
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEhRPDLILLDLEMPD-MDGLELCRRLRAdPRTADIPIIF 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499349852 1106 LTADGRDELKQLARQRG---YrlLTKPVKPASLRA 1137
Cdd:COG3706    81 LTALDDEEDRARALEAGaddY--LTKPFDPEELLA 113
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1001 6.84e-13

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 65.81  E-value: 6.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRQG---RIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGeqGLGLGLSICQ 974
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRrppRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSREEYE--GTGVGLAIVR 78
                          90       100
                  ....*....|....*....|....*..
gi 499349852  975 RISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16921    79 KIIERHGGRIWLESEPGEGTTFYFTLP 105
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1025-1142 7.17e-13

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 66.92  E-value: 7.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1025 LAGLRVLCVDNDREILDGMRALLGR---WQVeVITASTVDQALE-LARERPDVMLVDYHLHDRlDGLDTLDALQAAAVDP 1100
Cdd:COG4565     1 MKMIRVLIVEDDPMVAELLRRYLERlpgFEV-VGVASSGEEALAlLAEHRPDLILLDIYLPDG-DGLELLRELRARGPDV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 499349852 1101 IAgALLTADGRDELKQLARQRG-YRLLTKPVKPASLRAFLSAY 1142
Cdd:COG4565    79 DV-IVITAARDPETVREALRAGvVDYLIKPFTFERLREALERY 120
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
787-1004 1.31e-12

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 70.77  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  787 FLAAISHDVLQPLNAARLFASALRESHqnNEEQRHLAERVDASLRAAEELLDgLLDVSRLDAGGLRPTV---ED-----F 858
Cdd:PRK10755  140 FTADVAHELRTPLAGIRLHLELLEKQH--HIDVAPLIARLDQMMHTVEQLLQ-LARAGQSFSSGHYQTVkllEDvilpsQ 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  859 DASALMHELAAQYapvagsrgLRLQVHARALWVRSDRRLLRRVMQNFLANALRYTRQG-RIVLGMRGRGAQVELQVWDTG 937
Cdd:PRK10755  217 DELSEMLEQRQQT--------LLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGsTITIKLSQEDGGAVLAVEDEG 288
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499349852  938 PGIPEHHMRQIFEEFRRyqqpFDWGEQGLGLGLSICQRISRLldHD----LSARSQvGQGSMFSILLPRVD 1004
Cdd:PRK10755  289 PGIDESKCGELSKAFVR----MDSRYGGIGLGLSIVSRITQL--HHgqffLQNRQE-RSGTRAWVWLPKAQ 352
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
783-849 2.12e-12

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 63.00  E-value: 2.12e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499349852   783 SKTRFLAAISHDVLQPLNAARLFASALREShQNNEEQRHLAERVDASLRAAEELLDGLLDVSRLDAG 849
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDE-KLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
SLC5sbd_PanF cd10327
Na(+)/pantothenate cotransporters: PanF of Escherichia coli and related proteins; solute ...
47-448 2.69e-12

Na(+)/pantothenate cotransporters: PanF of Escherichia coli and related proteins; solute binding domain; PanF catalyzes the Na+-coupled uptake of extracellular pantothenate for coenzyme A biosynthesis in cells. This subfamily belongs to the solute carrier 5 (SLC5) transporter family.


Pssm-ID: 212037  Cd Length: 472  Bit Score: 70.31  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   47 AVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLLLLFGWRII-ERLALIARAENTVSIADFISSRYgRSRRLAALVAVIAL 125
Cdd:cd10327    52 ATYTSASSFIGGPGAAYKIGLGWVLLAMIQVPTGFLTLGVLgKKFAIIARKINAVTIIDYLRARY-NSKALVVLSSLALI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  126 VGIVPYLALQYKAVAMSLEVLTGHSSA-GRGIFAdpalyvaLLMALFATLFGTRQVDATEHHHGMMLAIAleSVIKLVAI 204
Cdd:cd10327   131 VFFIAAMVAQFIGGARLLEAVTGLSYVtGLLIFG-------LTVILYTTIGGFRAVALTDAIQGIVMIIG--TVLLLVGV 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  205 VAVG-----VFAWLWLGDHQLHIADSARTLfqhtpSVGFI-SQTLLSFLAVVCLPRqfhvAVVEC---SDVGDIRRARWL 275
Cdd:cd10327   202 LAAGggmeaIMATLAEIDPNLLTPFGPGFL-----SPPYIlSFWVLVGFGVIGLPQ----TAVRCmgyKDSKSMHRAMII 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  276 FGAYLVIISAMVVPIASAGVALFGQDSSVvdDAVVLALPLSQGNTVLALVAYVGGFSAA----TGMVIVASialATMVsN 351
Cdd:cd10327   273 GTVVVGFLMLGMHLAGVLGRAVLPDLEVP--DKVIPTLALKVLPPWLAGLFLAGPLAAImstvDSQLILAS---SAIV-K 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  352 DLVMPVLLRRRSSADaratvaSRVLWIRRVAILLLALIAYgyhrsvandttLAAY---------GLMAFAA--VAQFAPg 420
Cdd:cd10327   347 DLYLNYKNKEKKTSE------KKVKRISLIITIILGLLVF-----------LLAInppdlivwlNLFAFGGleAAFFWP- 408
                         410       420
                  ....*....|....*....|....*...
gi 499349852  421 VIGGLYWRGASRKGVETGMVLGFMTWIY 448
Cdd:cd10327   409 LVLGLYWKRANATGALASMVVGLVSYIL 436
PAS COG2202
PAS domain [Signal transduction mechanisms];
552-759 3.01e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.13  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  552 AERVVGERHAHRAFLDQAQLLERELQPTAVADRAWvQFTERLLAASIGAASARLVLTSLLRGSGMELGEVVAVLD----- 626
Cdd:COG2202    48 AEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW-RGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDiterk 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  627 EAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRynaergELGEGDIEDQID 706
Cdd:COG2202   127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEEL-LGKSLLDLLH------PEDRERLLELLR 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499349852  707 RRIRHMRAGSPHVFERTRSDGKVIEMRGQALP------GGGYVTSYNDITDYKRAERAL 759
Cdd:COG2202   200 RLLEGGRESYELELRLKDGDGRWVWVEASAVPlrdggeVIGVLGIVRDITERKRAEEAL 258
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
781-845 3.36e-12

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: 62.62  E-value: 3.36e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499349852  781 QQSKTRFLAAISHDVLQPLNAARLFASALRESHQNNEEQRHLAERVDASLRAAEELLDGLLDVSR 845
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
PAS COG2202
PAS domain [Signal transduction mechanisms];
627-847 3.39e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.13  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  627 EAGQELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIrynaergelGEGDIEDQID 706
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEEL-LGKTLRDLL---------PPEDDDEFLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  707 RRIRHMRAGSPHVFE--RTRSDGKVIEMRGQALP-----GG--GYVTSYNDITDYKRAERALLDANENLEQrVADRSREA 777
Cdd:COG2202    71 LLRAALAGGGVWRGElrNRRKDGSLFWVELSISPvrdedGEitGFVGIARDITERKRAEEALRESEERLRL-LVENAPDG 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  778 ELAQQSKTRFLAAISHdvlqplnAARLFASALRESHQNNEEQRHLAERVDASLRAAEELLDGLLDVSRLD 847
Cdd:COG2202   150 IFVLDLDGRILYVNPA-------AEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELE 212
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
894-986 3.80e-12

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: 64.02  E-value: 3.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  894 DRRLLRRVMQNFLANALRYTRQ-GRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSI 972
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTgGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAI 80
                          90
                  ....*....|....
gi 499349852  973 CQRISRLLDHDLSA 986
Cdd:cd16946    81 CHNIALAHGGTISA 94
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
783-849 3.93e-12

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 62.20  E-value: 3.93e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499349852    783 SKTRFLAAISHDVLQPLNAARLFASALRESHQnNEEQRHLAERVDASLRAAEELLDGLLDVSRLDAG 849
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTEL-SEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
787-1002 9.28e-12

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 69.03  E-value: 9.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  787 FLAAISHDVLQPL-NAARLFASALRESHQNNEEQRHLAERVDASLRAAEELLDgLLDVSRLDAGGLRPTVEDFDASALMH 865
Cdd:PRK09835  265 FSADIAHEIRTPItNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSD-MLFLAQADNNQLIPEKKMLDLADEVG 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  866 ELAAQYAPVAGSRGLRLQVHARALWVRSDRRLLRRVMQNFLANALRYTRQG-RIVLGMRGRGAQVELQVWDTGPGIPEHH 944
Cdd:PRK09835  344 KVFDFFEAWAEERGVELRFVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGeAITVRCQEVDHQVQLVVENPGTPIAPEH 423
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499349852  945 MRQIFEEFRRYQQPFDWGEQGLGLGLSICQRISRLLDHDLSARSQVgQGSMFSILLPR 1002
Cdd:PRK09835  424 LPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLPR 480
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
895-1002 9.76e-12

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: 62.44  E-value: 9.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  895 RRLLRRVMQNFLANALR-YTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPfdwgEQGLGLGLSIC 973
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQaMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPV----GEGTGLGLSLS 76
                          90       100
                  ....*....|....*....|....*....
gi 499349852  974 QRISRLLDHDLSARSQVGQGSMFSILLPR 1002
Cdd:cd16943    77 YRIIQKHGGTIRVASVPGGGTRFTIILPI 105
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1001 1.27e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 62.34  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRQgRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSICQRIS 977
Cdd:cd16949     1 LARALENVLRNALRYSPS-KILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAI 79
                          90       100
                  ....*....|....*....|....
gi 499349852  978 RLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16949    80 EQHGGKIKASNRKPGGLRVRIWLP 103
envZ PRK09467
osmolarity sensor protein; Provisional
782-976 1.68e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 67.63  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  782 QSKTRFLAAISHDVLQPLNAARLfASALReshqnNEEQRHLAERVDASLRAAEELLDGLLDVSRLDAgglRPTVEDFDAS 861
Cdd:PRK09467  227 DDRTLLMAGVSHDLRTPLTRIRL-ATEMM-----SEEDGYLAESINKDIEECNAIIEQFIDYLRTGQ---EMPMEMADLN 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  862 ALMHELAAQYAPVAGSRGLRLQVHARALWVRsdRRLLRRVMQNFLANALRYTRqGRIVLGMRGRGAQVELQVWDTGPGIP 941
Cdd:PRK09467  298 ALLGEVIAAESGYEREIETALQPGPIEVPMN--PIAIKRALANLVVNAARYGN-GWIKVSSGTEGKRAWFQVEDDGPGIP 374
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 499349852  942 EHHMRQIFeefrryqQPFDWGEQ-----GLGLGLSICQRI 976
Cdd:PRK09467  375 PEQLKHLF-------QPFTRGDSargssGTGLGLAIVKRI 407
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1001 3.03e-11

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: 61.45  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRQGRIVlgmRGRGAQVE----LQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSIC 973
Cdd:cd16952     1 LRSAFSNLVSNAVKYTPPSDTI---TVRWSQEEsgarLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIV 77
                          90       100
                  ....*....|....*....|....*...
gi 499349852  974 QRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16952    78 KHVMSRHDARLLIASELGKGSRFTCLFP 105
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1029-1129 3.32e-11

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: 60.94  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQ--VEVITASTVDQALELARE-RPDVMLVDYHLhDRLDGLDTLDALQaaAVDPIAG-A 1104
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEhKPDLVITDINM-PGMDGLELLEAIR--ELDPDTKiI 77
                          90       100
                  ....*....|....*....|....*.
gi 499349852 1105 LLTADGRDELKQLARQRG-YRLLTKP 1129
Cdd:COG4753    78 ILSGYSDFEYAQEAIKLGaDDYLLKP 103
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
893-1001 3.65e-11

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: 61.15  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  893 SDRRLLRRVMQNFLANALRYTRQ-GRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEF-----RRYQQpfdwgeQGL 966
Cdd:cd16948     1 TDAKWLSFIIGQIVSNALKYSKQgGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGftgenGRNFQ------EST 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499349852  967 GLGLSICQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16948    75 GMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
900-1001 8.02e-11

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: 60.20  E-value: 8.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  900 RVMQNFLANALRYTRQG---RIVLGMrGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSICQRI 976
Cdd:cd16925     7 RVVLNLLSNAFKFTPDGgriRCILEK-FRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLSIVKEF 85
                          90       100
                  ....*....|....*....|....*
gi 499349852  977 SRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16925    86 VELHGGTVTVSDAPGGGALFQVELP 110
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
894-979 9.88e-11

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 59.78  E-value: 9.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  894 DRRLLRRVMQNFLANALRYTRQGRIV-LGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDwGEQGLGLGLSI 972
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEGGLIaLQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHS-GQKSTGLGLAF 79

                  ....*..
gi 499349852  973 CQRISRL 979
Cdd:cd16945    80 VQEVAQL 86
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
766-1005 1.58e-10

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 62.71  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  766 LEQRVADRSREAELAQQSKTRFLAAIS----------HD-VLQPLNAARLFASALRESHQNNeeqrhlAERVDASLRAAE 834
Cdd:COG4585    25 VLLRARRAERAAELERELAARAEEAREeerrriarelHDgVGQSLSAIKLQLEAARRLLDAD------PEAAREELEEIR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  835 ELLDGLLDVSRLDAGGLRPTV-EDFDASALMHELAAQyapVAGSRGLRLQVHARALWVR---SDRRLLRRVMQNFLANAL 910
Cdd:COG4585    99 ELAREALAELRRLVRGLRPPAlDDLGLAAALEELAER---LLRAAGIRVELDVDGDPDRlppEVELALYRIVQEALTNAL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  911 RYTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQifeefrryqqpfdwgeQGLGLgLSICQRIsRLLDHDLSARSQV 990
Cdd:COG4585   176 KHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAAPG----------------GGLGL-RGMRERA-EALGGTLTIGSAP 237
                         250
                  ....*....|....*
gi 499349852  991 GQGSMFSILLPRVDA 1005
Cdd:COG4585   238 GGGTRVRATLPLAAA 252
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
781-976 1.77e-10

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 64.65  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  781 QQSKTRFLAAISHDVLQPLNAARLFASALREShqnneeQRHLAERVDASLRAAEELLDGLLD----VSRLDAGGLRPTVE 856
Cdd:PRK10549  237 EQMRRDFMADISHELRTPLAVLRGELEAIQDG------VRKFTPESVASLQAEVGTLTKLVDdlhqLSLSDEGALAYRKT 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  857 DFDASALMHELAAQYAPVAGSRGLRLQVH----ARalwVRSDRRLLRRVMQNFLANALRYT-RQGRIVLGMRGRGAQVEL 931
Cdd:PRK10549  311 PVDLVPLLEVAGGAFRERFASRGLTLQLSlpdsAT---VFGDPDRLMQLFNNLLENSLRYTdSGGSLHISAEQRDKTLRL 387
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 499349852  932 QVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSICQRI 976
Cdd:PRK10549  388 TFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNI 432
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
769-1001 2.06e-10

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 64.42  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  769 RVADRSR---EAELAQQSKTRFL----AAISHDVLQPLNAARLFASALRESHQNNEEQRHLAE----RVDASLRAAEELL 837
Cdd:PRK10364  215 RRYLRSRqllQDEMKRKEKLVALghlaAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQvmakEADRLNRVVSELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  838 dGLLDVSRLDaggLRPTvedfDASALMHELAAQYAPVAGSRGLRLQVHAR----ALWVRSDRrlLRRVMQNFLANALRYT 913
Cdd:PRK10364  295 -ELVKPTHLA---LQAV----DLNDLINHSLQLVSQDANSREIQLRFTANdtlpEIQADPDR--LTQVLLNLYLNAIQAI 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  914 -RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrryqqpFDWGEQGLGLGLSICQRISRLLDHDLSARSQVGQ 992
Cdd:PRK10364  365 gQHGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPY------FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGK 438

                  ....*....
gi 499349852  993 GSMFSILLP 1001
Cdd:PRK10364  439 GATFTLWLP 447
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1030-1137 4.84e-10

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: 57.93  E-value: 4.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  1030 VLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLhDRLDGLDTLDALQAAAVD-PIagALLT 1107
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEeRPDLILLDINM-PGMDGLELLKRIRRRDPTtPV--IILT 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 499349852  1108 ADGRDELKQLARQRG-YRLLTKPVKPASLRA 1137
Cdd:pfam00072   78 AHGDEDDAVEALEAGaDDFLSKPFDPDELLA 108
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1030-1137 9.49e-10

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: 57.08  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1030 VLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDAL--QAAAVDPIAGAlL 1106
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRfRPDVILSDIGMPG-MDGYELARRLreLPWLANTPAIA-L 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499349852 1107 TADGRDELKQLARQRGYRL-LTKPVKPASLRA 1137
Cdd:cd17580    79 TGYGQPEDRERALEAGFDAhLVKPVDPDELIE 110
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
787-1001 9.50e-10

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 62.34  E-value: 9.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  787 FLAAISHDVLQPLNAARLF---------ASALRE-SHQNNEEQrhlaervdasLRAAEELLDGLLDVSRLDAGglrPTV- 855
Cdd:PRK11006  207 FFANVSHELRTPLTVLQGYlemmqdqplEGALREkALHTMREQ----------TQRMEGLVKQLLTLSKIEAA---PTId 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  856 --EDFDASALMH--ELAAQyAPVAGSRGLRLQVHArALWVRSDRRLLRRVMQNFLANALRYTRQG-RIVLGMRGRGAQVE 930
Cdd:PRK11006  274 lnEKVDVPMMLRvlEREAQ-TLSQGKHTITFEVDN-SLKVFGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQRVPQGAE 351
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499349852  931 LQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSICQRisRLLDHD--LSARSQVGQGSMFSILLP 1001
Cdd:PRK11006  352 FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKH--ALSHHDsrLEIESEVGKGTRFSFVLP 422
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1030-1137 1.19e-09

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: 56.87  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1030 VLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARERP---DVMLVDYHLHDrLDGLDTLDALQAAAVDPIagALL 1106
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKdefDLVITDVHMPD-MDGFEFLELIRLEMDLPV--IMM 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499349852 1107 TADGRDELKQLARQRGY-RLLTKPVKPASLRA 1137
Cdd:cd17584    78 SADGSTSTVMKGLAHGAcDYLLKPVSIEDLKN 109
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
637-759 1.26e-09

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 57.30  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   637 EILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGY-PDGMLyvGRPVADLIRynaergelgEGDIEdQIDRRIRHMRAG 715
Cdd:TIGR00229    3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYsAEELI--GRNVLELIP---------EEDRE-EVRERIERRLEG 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 499349852   716 SPHV----FERTRSDGKVI--EMRGQALP--GG--GYVTSYNDITDYKRAERAL 759
Cdd:TIGR00229   71 EPEPvseeRRVRRKDGSEIwvEVSVSPIRtnGGelGVVGIVRDITERKEAEEAL 124
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1001 1.65e-09

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: 56.30  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYTRqGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFeefrryqQPFDWGEQ-----GLGLGLSI 972
Cdd:cd16950     1 LKRVLSNLVDNALRYGG-GWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELF-------QPFYRGDNargtsGTGLGLAI 72
                          90       100
                  ....*....|....*....|....*....
gi 499349852  973 CQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16950    73 VQRISDAHGGSLTLANRAGGGLCARIELP 101
sss TIGR00813
transporter, SSS family; The Solute:Sodium Symporter (SSS) Family (TC 2.A.21) Members of the ...
45-442 2.08e-09

transporter, SSS family; The Solute:Sodium Symporter (SSS) Family (TC 2.A.21) Members of the SSS family catalyze solute:Na+ symport. The solutes transported may be sugars, amino acids, nucleosides, inositols, vitamins, urea or anions, depending on the system. Members of the SSS family have been identified in bacteria, archaea and animals, and all functionally well characterized members catalyze solute uptake via Na+ symport. Proteins of the SSS generally share a core of 13 TMSs, but different members of the family may have different numbers of TMSs. A 13 TMS topology with a periplasmic N-terminus and a cytoplasmic C-terminus has been experimentally determined for the proline:Na+ symporter, PutP, of E. coli. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273282 [Multi-domain]  Cd Length: 407  Bit Score: 61.16  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    45 ALAVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLLLLFGWRIIerlALIARAENTVSIADFISSRYGrSRRLAALVAVIA 124
Cdd:TIGR00813   14 LFASYISASQFLGLPGAIYAYGFAIGFYELGALVLLIILGWLF---VPIFINNGAYTMPEYLEKRFG-KRILRGLSVLSL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   125 LVGIVPYLALQYKAVAMSLEVLTGHSsagrgifadpaLYVALLMALFATLF-----GTRQVDATEHHHGMMLaIALESVI 199
Cdd:TIGR00813   90 ILYIFLYMSVDLFSGALLIELITGLD-----------LYLSLLLLGAITILytvfgGLKAVVWTDTIQAVIM-ILGTFIL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   200 KLVAIVAVGVFAWLWLGDHQLHIADSARTLFQHTPSVGFISQTLLSFLAVvclpRQFHVAV------------VECSDVG 267
Cdd:TIGR00813  158 PVFAFSEVGGLGTFVEKASQAAPTNPSPDDLYDFFRDPSTSDLPWGAGVF----GLPHVALwywtnqvivqrcLAAKSAK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   268 DIRRARWLFGAYLVIISAMVVPIASAGVALF--------GQDSSVVDDAVVLALPLSQGNTVLAL---VAYVGGFSAATG 336
Cdd:TIGR00813  234 HAKKGCLISGVLKLLPMFGAVLPGLIARALYtdidpalaGAVNQNSDQAYPLLVQELMPPGLAGLflaAILAAVMSTLSS 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   337 MVIVASialaTMVSNDLVMPvllRRRSSADARATVASRVLWIRRVAILLLALIAYGYHRSVandttlaaYGLMAFA---A 413
Cdd:TIGR00813  314 QLNSAS----TVFTMDLYKK---IIRPNASGEKKIVMRGRIAVLVAAVIAGFVAAAQGGQV--------LQYVQEAfggL 378
                          410       420
                   ....*....|....*....|....*....
gi 499349852   414 VAQFAPGVIGGLYWRGASRKGVETGMVLG 442
Cdd:TIGR00813  379 GAPFLPVFLLGIFWKRMNAKGALAGMIAG 407
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1000 2.94e-09

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: 55.54  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYT---RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQqpfDWGEqGLGLGLSICQ 974
Cdd:cd16976     1 IQQVLMNLLQNALDAMgkvENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTK---PVGK-GTGLGLSISY 76
                          90       100
                  ....*....|....*....|....*.
gi 499349852  975 RISRLLDHDLSARSQVGQGSMFSILL 1000
Cdd:cd16976    77 GIVEEHGGRLSVANEEGAGARFTFDL 102
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1001 1.20e-08

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 53.94  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALR----YTRQGRIVL--GMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrryqqpFDWGEQGLGLGLS 971
Cdd:cd16920     1 IQQVLINLVRNGIEamseGGCERRELTirTSPADDRAVTISVKDTGPGIAEEVAGQLFDPF------YTTKSEGLGMGLS 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 499349852  972 ICQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16920    75 ICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
775-1001 1.45e-08

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 59.18  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  775 REAELAQQSKTRFLAAISHDVLQPLNAARLFASALRESHQNNEEQRHLAERVDASlRAAEELLDGLLDVSRLDAGGLRPT 854
Cdd:PRK10618  441 REYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQS-DVLVRLVDNIQLLNMLETQDWKPE 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  855 VEDFDASALMHELAAQYAPVAGSRGLRLQVH----ARALWvRSDRRLLRRVMQNFLANALRYTRQGRIVLGM---RGRGA 927
Cdd:PRK10618  520 QELFSLQDLIDEVLPEVLPAIKRKGLQLLIHnhlkAEQLR-IGDRDALRKILLLLLNYAITTTAYGKITLEVdqdESSPD 598
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  928 QVELQVWDTGPGIPEHHMRQIfeefrRYqqPF------DWGEQGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:PRK10618  599 RLTIRILDTGAGVSIKELDNL-----HF--PFlnqtqgDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLK 671
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1029-1142 1.62e-08

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: 55.31  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELAR-ERPDVMLVDYHLHDRlDGLDTLDALQaAAVDPIAGALLT 1107
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEqAPPDYAVLDLRLGDG-SGLDLIEALR-ERDPDARIVVLT 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499349852 1108 ADGRDELKQLARQRGYR-LLTKPVKPASLRAFLSAY 1142
Cdd:COG4567    84 GYASIATAVEAIKLGADdYLAKPADADDLLAALERA 119
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1029-1135 2.14e-08

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: 53.71  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDND---REILDGMRALLGRWqvEVITASTVDQALELAR-ERPDVMLVDYHLHDrLDGLDTLDALQA-AAVDPIAG 1103
Cdd:cd17552     3 RILVIDDEediREVVQACLEKLAGW--EVLTASSGQEGLEKAAtEQPDAILLDVMMPD-MDGLATLKKLQAnPETQSIPV 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 499349852 1104 ALLTADGRDELKQLARQRGYR-LLTKPVKPASL 1135
Cdd:cd17552    80 ILLTAKAQPSDRQRFASLGVAgVIAKPFDPLTL 112
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1001 2.29e-08

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: 52.77  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYT-RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGeqGLGLGLSICQRI 976
Cdd:cd16923     1 LQRVFSNLLSNAIKYSpENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNTE--GAGLGLSIAKAI 78
                          90       100
                  ....*....|....*....|....*
gi 499349852  977 SRLLDHDLSARSQvGQGSMFSILLP 1001
Cdd:cd16923    79 IELHGGSASAEYD-DNHDLFKVRLP 102
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1027-1139 3.31e-08

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: 54.96  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1027 GLRVLCVDNDREILDGMRALLGRWQVEVIT-ASTVDQALELARE-RPDVMLVDYHLHDRlDGLDTLDALQAAAVDPIagA 1104
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRElKPDLVIVDIDMPDR-DGLEAARQISEERPAPV--I 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499349852 1105 LLTADGRDELKQLARQRG-YRLLTKPVKPASLRAFL 1139
Cdd:COG3707    80 LLTAYSDPELIERALEAGvSAYLVKPLDPEDLLPAL 115
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
630-762 4.00e-08

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 57.09  E-value: 4.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  630 QELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRYNAERGELGEGdiEDQIDRRI 709
Cdd:COG3829     4 LELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEV-IGKNVTELIPNSPLLEVLKTG--KPVTGVIQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499349852  710 RHMRAGSPHVFERT--RSDGKVIemrgqalpggGYVTSYNDITDYKRAERALLDA 762
Cdd:COG3829    81 KTGGKGKTVIVTAIpiFEDGEVI----------GAVETFRDITELKRLERKLREE 125
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
898-1001 7.46e-08

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 51.80  E-value: 7.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  898 LRRVMQNFLANALRYT--RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSICQR 975
Cdd:cd16953     1 LGQVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISRQ 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 499349852  976 ISRLLDHDLSA--RSQVGQ--GSMFSILLP 1001
Cdd:cd16953    81 IIEAHGGISVAenHNQPGQviGARFTVQLP 110
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1030-1137 1.34e-07

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: 50.93  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1030 VLCV-DND--REIldgMRALLGRWQVEVITASTVDQALELARERP-DVMLVDYHLHDrLDGLDTLDALQAAAVD----PI 1101
Cdd:cd17546     1 VLVVdDNPvnRKV---LKKLLEKLGYEVDVAENGQEALELLKEEPfDLVLMDLQMPV-MDGLEATRRIRELEGGgrrtPI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499349852 1102 AGalLTADGRDELKQLARQRGY-RLLTKPVKPASLRA 1137
Cdd:cd17546    77 IA--LTANALEEDREKCLEAGMdDYLSKPVKLDQLKE 111
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1028-1080 1.84e-07

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: 48.72  E-value: 1.84e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 499349852   1028 LRVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARE-RPDVMLVDYHL 1080
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEeKPDLILLDIMM 54
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
780-972 2.19e-07

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 54.94  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  780 AQQsktRFLAAISHDVLQPLNAARLfASAL--RESHQNNEeqrhlAERVDASLRAAEELLDGLLDVSR--LDAGGLRptv 855
Cdd:PRK09470  242 SQQ---RLLSDISHELRTPLTRLQL-ATALlrRRQGESKE-----LERIETEAQRLDSMINDLLVLSRnqQKNHLER--- 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  856 EDFDASALMHELAAQYAPVAGSRGLRLQV--HARALWVRSDRRLLRRVMQNFLANALRYTRQgRIVLGMRGRGAQVELQV 933
Cdd:PRK09470  310 ETFKANSLWSEVLEDAKFEAEQMGKSLTVsaPPGPWPINGNPNALASALENIVRNALRYSHT-KIEVAFSVDKDGLTITV 388
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 499349852  934 WDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQGLGLGLSI 972
Cdd:PRK09470  389 DDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAI 427
SSF pfam00474
Sodium:solute symporter family; This family includes Swiss:P33413 which is not in the Prosite ...
47-442 3.11e-07

Sodium:solute symporter family; This family includes Swiss:P33413 which is not in the Prosite entry. Membership of this family is supported by a significant blast score.


Pssm-ID: 109527 [Multi-domain]  Cd Length: 406  Bit Score: 54.27  E-value: 3.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852    47 AVYCSSWTFYGAVGSAVRNGIGYLPIYLGPLLLLLF-GWRIIERLaliaRAENTVSIADFISSRYGRSRRLAALVAVIAL 125
Cdd:pfam00474   19 ASYMSAASFVGLAGAGAASGLAGGLYAIGALVGVWLlLWLFAPRL----RNLGAYTMPDYLRKRFGGKRILVYLSALSLL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   126 VGIVPYLALQYKAVAMSLEVLTGHSsagrgiFADPALYVALLMALFATLFGTRQVDATEHHHGMMLAIALeSVIKLVAIV 205
Cdd:pfam00474   95 LYFFTYMSVQIVGGARLIELALGLN------YYTAVLLLGALTAIYTFFGGFLAVSWTDTIQAVLMLFGT-IILMIIVFH 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   206 AVGVFAWLWlgDHQLHIADSARTLFQHTPSVGFIS-QTLLSFLAVVCL---PRQfhVAVVEC---SDVGDIRRARWLFGA 278
Cdd:pfam00474  168 EVGGYSSAV--EKYMTADPNGVDLYTPDGLHILRDpLTGLSLWPGLVLgttGLP--HILQRClaaKDAKCIRCGVLILTP 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   279 YLVIISAMVVPIASAGVALFGqdssVVDDAVVLALPLSQGNTVLALVAYVGGFSA--------ATGMVIVASIALATmvS 350
Cdd:pfam00474  244 MFIIVMPGMISRGLFAIALAG----ANPRACGTVVGCSNIAYPTLAVKLGPPGLAgimlavmlAAIMSTLTSQLLSS--S 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   351 NDLVMPVLLRRRSSADARATVASRVLWIRRVAILLLALIAYgyhrSVANDTTLAAYGLMAFA-AVAQFAPGVIGGLYWRG 429
Cdd:pfam00474  318 SAFTHDLYKNIRRKASATEKELVGRSRIIVLVVISLAILLA----VQPAQMGIAFLVQLAFAgLGSAFLPVILLAIFWKR 393
                          410
                   ....*....|...
gi 499349852   430 ASRKGVETGMVLG 442
Cdd:pfam00474  394 VNEQGALWGMIIG 406
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
762-995 3.46e-07

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 54.31  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  762 ANENLEQRVADRSR--------EAELAQQSKTRFLAA----ISHDVLQPLNAAR--LFASALRESHQNNEEQRHLAERVD 827
Cdd:COG4192   399 KTQELETEIEERKRieknlrqtQDELIQAAKMAVVGQtmtsLAHELNQPLNAMSmyLFSAKKALEQENYAQLPTSLDKIE 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  828 ASLRAAEELLDGLLDVSRLDAGGLRPTvedfdasaLMHELAAQYAPVAGSRGLRLQVHARA---LWVRSDRRLLRRVMQN 904
Cdd:COG4192   479 GLIERMDKIIKSLRQFSRKSDTPLQPV--------DLRQVIEQAWELVESRAKPQQITLHIpddLMVQGDQVLLEQVLVN 550
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  905 FLANALR-YTRQGRIVLGMRGRGAQVELQVWDTGPGipehhmrqiFEEFRRYQQPF-DWGEQGLGLGLSICQRISRLLDH 982
Cdd:COG4192   551 LLVNALDaVATQPQISVDLLSNAENLRVAISDNGNG---------WPLVDKLFTPFtTTKEVGLGLGLSICRSIMQQFGG 621
                         250
                  ....*....|...
gi 499349852  983 DLSARSQVGQGSM 995
Cdd:COG4192   622 DLYLASTLERGAM 634
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1029-1137 3.48e-07

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: 50.10  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVI-TASTVDQALELARE-RPDVMLVDYHLHDRLDGLDTldALQAAAVDPIAGALL 1106
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEEnKPDLILMDINLKGDMDGIEA--AREIREKFDIPVIFL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499349852 1107 TADGRDELKQLARQ---RGYrlLTKPVKPASLRA 1137
Cdd:cd17534    80 TAYSDEETLERAKEtnpYGY--LVKPFNERELKA 111
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1029-1137 4.30e-07

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: 49.71  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVITASTVDQALE-LARERPDVMLVDYhlhdRLDGLDTLDAL-QAAAVDP-IAGAL 1105
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEiLKQEPVDVVISDQ----RMPGMDGAELLkRVRERYPdTVRIL 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499349852 1106 LTadGRDELKQLAR--QRG--YRLLTKPVKPASLRA 1137
Cdd:cd17569    78 LT--GYADLDAAIEaiNEGeiYRFLTKPWDDEELKE 111
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1029-1137 6.41e-07

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: 49.36  E-value: 6.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQ-VEVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVD---PIag 1103
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCREnPPDLILLDYMMPG-MDGLEFIRRLRALPGLedvPI-- 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499349852 1104 ALLTADGRDELKQLARQRGYR-LLTKPVKPASLRA 1137
Cdd:cd17551    79 VMITADTDREVRLRALEAGATdFLTKPFDPVELLA 113
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
863-1000 1.33e-06

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: 48.78  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  863 LMHELAAQYAPVAGSRGLRLQVH----ARALWVRSDrrlLRRVMQNFLANALRYTrQGRIVLGMRGRGAQVELQVWDTGP 938
Cdd:cd16954     2 LLDSLCSALNKVYQRKGVSISLDispeLRFPGERND---LMELLGNLLDNACKWC-LEFVEVTARQTDGGLHLIVDDDGP 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499349852  939 GIPEHHMRQIFEEFRRyqqpFDWGEQGLGLGLSICQRISRLLDHDLSA-RSQVGqGSMFSILL 1000
Cdd:cd16954    78 GVPESQRSKIFQRGQR----LDEQRPGQGLGLAIAKEIVEQYGGELSLsDSPLG-GARFEVVF 135
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
911-1001 2.53e-06

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 47.40  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  911 RYTRQGRIvLGMRGRGAqVELQVWDTGPGIPEHHMRQIFEefrryqqPFDWG-EQGLGLGLSICQRISRLLDHDLSARSQ 989
Cdd:cd16918    28 RTQRQVTL-GHPRHRLA-LRVSVIDNGPGIPPDLQDTIFY-------PMVSGrENGTGLGLAIAQNIVSQHGGVIECDSQ 98
                          90
                  ....*....|..
gi 499349852  990 VGQgSMFSILLP 1001
Cdd:cd16918    99 PGH-TVFSVSLP 109
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
916-1001 3.13e-06

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: 46.90  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  916 GRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEefRRYQQPfdwGEQGLGLGLSICQRISRLLDHDLSARSQVGQGSM 995
Cdd:cd16915    24 KQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFE--RGVSTK---GQGERGIGLALVRQSVERLGGSITVESEPGGGTT 98

                  ....*.
gi 499349852  996 FSILLP 1001
Cdd:cd16915    99 FSIRIP 104
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
894-1002 8.25e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 49.63  E-value: 8.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  894 DRRLLRRVMQNFLANALRY-----TRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRyqqpfdwGEQGLGL 968
Cdd:COG2972   333 DLLIPKLILQPLVENAIEHgiepkEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSS-------KGEGRGI 405
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499349852  969 GLS-ICQRIsRLL---DHDLSARSQVGQGSMFSILLPR 1002
Cdd:COG2972   406 GLRnVRERL-KLYygeEYGLEIESEPGEGTTVTIRIPL 442
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
637-738 1.52e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 45.10  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   637 EILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRYNAERGELgegdieDQIDRRIRHMRAGS 716
Cdd:pfam00989    1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEV-IGKSLLDLIPEEDDAEVA------ELLRQALLQGEESR 73
                           90       100
                   ....*....|....*....|..
gi 499349852   717 PHVFERTRSDGKVIEMRGQALP 738
Cdd:pfam00989   74 GFEVSFRVPDGRPRHVEVRASP 95
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
894-1000 2.65e-05

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 44.57  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  894 DRRLLRRVMQNFLANALRYT-----------RQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRryqqpfdWG 962
Cdd:cd16932     3 DQIRLQQVLADFLLNAVRFTpspggwveikvSPTKKQIGDGVHVIHLEFRITHPGQGLPEELVQEMFEENQ-------WT 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499349852  963 EQGlGLGLSICQRISRLLDHDLSARSQVGQgSMFSILL 1000
Cdd:cd16932    76 TQE-GLGLSISRKLVKLMNGDVRYLREAGR-SYFLITL 111
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
926-1001 3.34e-05

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


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 44.29  E-value: 3.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499349852  926 GAQVELQVWDTGPGIPEHHMRQIFEEFrryqqpFDWGE--QGLGLGLSICQRISRLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:cd16919    45 GNYVCLEVSDTGSGMPAEVLRRAFEPF------FTTKEvgKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1028-1093 4.29e-05

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: 44.50  E-value: 4.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499349852 1028 LRVLCVDNDREILDGMRALLGR-WQVEVI-TASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDAL 1093
Cdd:COG2197     2 IRVLIVDDHPLVREGLRALLEAePDIEVVgEAADGEEALELLEElRPDVVLLDIRMPG-MDGLEALRRL 69
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
630-976 5.18e-05

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: 47.21  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   630 QELRFNREILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGypdgMLYVGRPVADLIRynAERGELGE--GDIEDQ--- 704
Cdd:TIGR02938  123 QVVANQKLLIESVVDAAPVAFVLLDPTGRVILDNQEYKKLAT----DLRVKEPAHTVLD--LLREAWREalAENWPQqla 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   705 -IDRRIRHMRAG--SPHVFERTrsdGKVIEMRGQALPG-------GGYVTSYNDITDYKRA-ERALLDAnenLEQRVAdr 773
Cdd:TIGR02938  197 fSNREARFDRGGgrPARWLSCT---GSVIGMESDCADSffcaaeqPYLLLTIADISNLREEqERARLSA---LQALMA-- 268
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   774 srEAELAQQSKTRFLAAIsHDVLQPLNaarLFASAL-----RESHQNNEEQRHLAERVDASLRAAEELLDGLLDVSrlDA 848
Cdd:TIGR02938  269 --EEERLEAIRETLSAAI-HRLQGPMN---LISAAIsvlqrRGDDAGNPASAAMLQQALSAGREHMEALRQVIPQS--PQ 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   849 GGLRPTvedfDASALMHELAAQYAPVAGSRGLRL--QVHARALWVRSDRRLLRRVMQNFLANAL-----RYTRQGRIVLG 921
Cdd:TIGR02938  341 EIVVPV----NLNQILRDVITLSTPRLLAAGIVVdwQPAATLPAILGRELQLRSLFKALVDNAIeamniKGWKRRELSIT 416
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 499349852   922 MRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFdwgEQGLGLGLSICQRI 976
Cdd:TIGR02938  417 TALNGDLIVVSILDSGPGIPQDLRYKVFEPFFTTKGGS---RKHIGMGLSVAQEI 468
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
637-687 5.26e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.39  E-value: 5.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 499349852    637 EILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLI 687
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEEL-IGKSLLELI 50
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1030-1096 7.42e-05

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: 43.27  E-value: 7.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1030 VLCVDNDREILDGMRALLGRWQ-VEVI-TASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAA 1096
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPdIEVVgEAADGEEALALLRElRPDVVLMDLSMPG-MDGIEALRRLRRR 69
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1043-1142 7.51e-05

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: 43.29  E-value: 7.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1043 MRALLGRWQVEVITASTVDQALE-LARERPDVMLVDYHLHDrLDGLDTLDALQAAAVDP--IagaLLTADGRDELKQLAR 1119
Cdd:cd17593    17 ARALPADWDVEITFAENGEEALEiLREGRIDVLFLDLTMPV-MDGYEVLEALPVEQLETkvI---VVSGDVQPEAKERVL 92
                          90       100
                  ....*....|....*....|....
gi 499349852 1120 QRG-YRLLTKPVKPASLRAFLSAY 1142
Cdd:cd17593    93 ELGaLAFLKKPFDPEKLAQLLEEL 116
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
1030-1129 2.19e-04

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: 41.37  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1030 VLCVDNDREILDGMRALLGRWQVEVITASTVDQALE-LARERPDVMLVDYHLHDRlDGLDTLDALQAAAVD-PIagALLT 1107
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARElLASEPYDLCLTDMRLPDG-SGLELVQHIQQRLPQtPV--AVIT 77
                          90       100
                  ....*....|....*....|...
gi 499349852 1108 ADGRDELKQLARQRG-YRLLTKP 1129
Cdd:cd19926    78 AYGSLDTAIEALKAGaFDFLTKP 100
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
894-998 2.53e-04

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: 41.68  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  894 DRRLLRRVMQNFLANALRYTRQGRIV-LGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFRRYQQPFDWGEQgLGLGLSI 972
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVsISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGH-YGMGLYI 79
                          90       100
                  ....*....|....*....|....*.
gi 499349852  973 CQRISRLLDHDLSARSQVGQGSMFSI 998
Cdd:cd16975    80 AKNLVEKHGGSLIIENSQKGGAEVTV 105
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1029-1139 3.14e-04

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 43.64  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARERPDVMLVDYhLHDRLDGLDTLDALQAAAVDPIagALLTA 1108
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDV-MMPKKNGIDTLKELRQTHQTPV--IMLTA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499349852 1109 DGRDelkqLARQRGYRL-----LTKPVKP----ASLRAFL 1139
Cdd:PRK10955   80 RGSE----LDRVLGLELgaddyLPKPFNDrelvARIRAIL 115
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1029-1141 4.03e-04

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: 41.21  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVITASTVDQALE-LARERPDVMLVDYHLHDRlDGLDTLDALQAAAVDPIagALLT 1107
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEvIAREKPDAVLLDIMLPGI-DGLTLCRDLRPKYQGPI--LLLT 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499349852 1108 ADGrDELKQLArqrGYRL-----LTKPVKPASLRAFLSA 1141
Cdd:cd17622    79 ALD-SDIDHIL---GLELgaddyVVKPVEPAVLLARLRA 113
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1028-1137 4.08e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 43.99  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1028 LRVLCVDndreilDG--MRALLGRW-----QVEVI-TASTVDQALELARE-RPDVMLVDYHLhDRLDGLD---------- 1088
Cdd:PRK00742    4 IRVLVVD------DSafMRRLISEIlnsdpDIEVVgTAPDGLEAREKIKKlNPDVITLDVEM-PVMDGLDalekimrlrp 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499349852 1089 ----------------TLDALQAAAVD-------PIAGALLTAdgRDEL----KQLARQRGYRLLTKPVKPASLRA 1137
Cdd:PRK00742   77 tpvvmvssltergaeiTLRALELGAVDfvtkpflGISLGMDEY--KEELaekvRAAARARVRALPPRAAAAARAAA 150
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1029-1077 4.23e-04

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: 40.94  E-value: 4.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELA-RERPDVMLVD 1077
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAeEELPDLILLD 50
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
643-754 4.41e-04

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 40.86  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   643 LENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGmLYVGRPVADLirYNAERGELGEGDI------EDQIDRRIRHMRAGS 716
Cdd:pfam08448    1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPE-ELLGKTLAEL--LPPEDAARLERALrralegEEPIDFLEELLLNGE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 499349852   717 PHVFERT-----RSDGKVIemrgqalpggGYVTSYNDITDYKR 754
Cdd:pfam08448   78 ERHYELRltplrDPDGEVI----------GVLVISRDITERRR 110
PRK13557 PRK13557
histidine kinase; Provisional
773-1077 4.99e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 44.28  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  773 RSREAE--LAQQSKTRFLA----AISHD---VLQPLNA-ARLFASALRESHQNNEEQRHLAERVDASLRAAEELLDGLLD 842
Cdd:PRK13557  146 RRRDAEdaLRQAQKMEALGqltgGIAHDfnnLLQVMSGyLDVIQAALSHPDADRGRMARSVENIRAAAERAATLTQQLLA 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  843 VSR--------LDAGGLRPTVEDFDASALMHELAAQyapvagsrglrlQVHARALW-VRSDRRLLRRVMQNFLANA---- 909
Cdd:PRK13557  226 FARkqrlegrvLNLNGLVSGMGELAERTLGDAVTIE------------TDLAPDLWnCRIDPTQAEVALLNVLINArdam 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  910 ------------LRYTRQGRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEFrryqqpFDWGE--QGLGLGLSICQR 975
Cdd:PRK13557  294 peggrvtirtrnVEIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPF------FTTKEegKGTGLGLSMVYG 367
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  976 ISRLLDHDLSARSQVGQGSMFSILLPRVDAVpAAPVPVLAVRPQASGDSlagLRVLCVDNDREILDGMRALLGRWQVEVI 1055
Cdd:PRK13557  368 FAKQSGGAVRIYSEVGEGTTVRLYFPASDQA-ENPEQEPKARAIDRGGT---ETILIVDDRPDVAELARMILEDFGYRTL 443
                         330       340
                  ....*....|....*....|....
gi 499349852 1056 TASTVDQALELARE--RPDVMLVD 1077
Cdd:PRK13557  444 VASNGREALEILDShpEVDLLFTD 467
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
1030-1093 5.77e-04

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 40.71  E-value: 5.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499349852 1030 VLCVDNDREILDGMRALLGRWQVEVI-TASTVDQALE-LARERPDVMLVDYHLHDRLDGLDTLDAL 1093
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVTRIdTASSGEEALRmCENKTYDIVLCDYNLGKGKNGQQLLEEL 66
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
646-738 6.66e-04

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 40.31  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  646 ISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLyVGRPVADLIRynaergelgEGDIEDQIDRRIRHMRAGSPHVFERT-- 723
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEEL-IGKSLLDLIH---------PEDREELRERLENLLSGGEPVTLEVRlr 70
                          90
                  ....*....|....*
gi 499349852  724 RSDGKVIEMRGQALP 738
Cdd:cd00130    71 RKDGSVIWVLVSLTP 85
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
1029-1140 1.18e-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: 39.92  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVI-TASTVDQALELA-RERPDVMLVDYHLHDRLDGLDTLDALQAA-AVDPI---- 1101
Cdd:cd17540     2 RVLIIEDEPLIAMDLEQIVEDLGHQVVgIARTRDEAVALArRERPDLILADIQLADGSSGIDAVNEILTThDVPVIfvta 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499349852 1102 -AGALLTADGRDElkqlarqrgYRLLTKPVKPASLRAFLS 1140
Cdd:cd17540    82 yPERLLTGERPEP---------TFLITKPFDPEMVKAAIS 112
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1029-1088 1.32e-03

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: 39.81  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499349852 1029 RVLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARERPDVMLV--DYHLhDRLDGLD 1088
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVitDYNM-PEMDGFE 62
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
906-977 1.35e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 39.90  E-value: 1.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499349852  906 LANALRYTRQ----GRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEEfrryqqpfdwgEQGLGLGLSICQRIS 977
Cdd:COG2172    43 VTNAVRHAYGgdpdGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYST-----------LAEGGRGLFLIRRLM 107
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1030-1129 1.40e-03

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: 39.07  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1030 VLCVDNDREILDGMRALLGRWQVEVITASTVDQALELARER-PDVMLVDYHLHDrLDGLDTLDALQAAAVDPIagALLTA 1108
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRkPDLIILDLGLPD-MDGLEVIRRLREWSAVPV--IVLSA 77
                          90       100
                  ....*....|....*....|....
gi 499349852 1109 DGRDELKQLARQRG---YrlLTKP 1129
Cdd:cd17620    78 RDEESDKIAALDAGaddY--LTKP 99
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1028-1142 1.76e-03

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: 39.54  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1028 LRVLCVDNDREILDGMRALLGRW-QVEVI-TASTVDQALE-LARERPDVMLVDYHLHDRlDGLDTLDALQAA--AVDPIA 1102
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEQVpGFTVIgTAGTGEEALKlLKERQPDLILLDIYLPDG-NGLDLLRELRAAghDVDVIV 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 499349852 1103 galLTADGRDELKQLARQRG---YrlLTKPVKPASLRAFLSAY 1142
Cdd:cd19925    80 ---VTAANDVETVREALRLGvvdY--LIKPFTFERLRQRLERY 117
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
637-696 2.59e-03

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 37.53  E-value: 2.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852   637 EILSTTLENISAAVSVVDPDMRLTAWNRRYQQLFGYPDGMLYVGRPVADLIRYNAERGEL 696
Cdd:pfam13188    1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALEL 60
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1029-1099 2.83e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 40.40  E-value: 2.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499349852 1029 RVLCVDNDREILDGMRALLG---RWQVeVITASTVDQALELARE-RPDVMLVDYHLHDrLDGLDTLDALQAAAVD 1099
Cdd:PRK10651    8 TILLIDDHPMLRTGVKQLISmapDITV-VGEASNGEQGIELAESlDPDLILLDLNMPG-MNGLETLDKLREKSLS 80
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
901-1001 3.56e-03

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 41.44  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  901 VMQNFLANALRYTRQ---GRIVLGMRGRGAQVELQVWDTGPGIPEHHMRQIFEefrryqQPFDWGEQGLGLGLSICQRIS 977
Cdd:PRK11086  437 ILGNLIENALEAVGGeegGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFD------KGYSTKGSNRGVGLYLVKQSV 510
                          90       100
                  ....*....|....*....|....
gi 499349852  978 RLLDHDLSARSQVGQGSMFSILLP 1001
Cdd:PRK11086  511 ENLGGSIAVESEPGVGTQFFVQIP 534
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
498-1007 3.75e-03

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 41.43  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  498 LLINTGTMMVVSARWRPGVDERLRAAPFLDPYSQRPAVAGEWPGHVHVADLQALAERVVGERHAHRAFLDQAQLLERELQ 577
Cdd:COG3920    31 LALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLAAAALALALLLAALAGL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  578 PTAVADRAWVQFTERLLAASIGAASARLVLTSLLRGSGMELGEVVAVLDEAGQELRFNREILSTTLENISAAVSVVDPDM 657
Cdd:COG3920   111 LLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  658 RLTAWNRRYQQLFGYPDGMLYVGRPVADLIRYNAERGELGEGDIEDQIDRRIRHMRAGSPHVFERTRSDGKVIEMRGQAL 737
Cdd:COG3920   191 LAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLLLRALLLL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  738 PGGGYVtsynDITDYKRAERALLDANENLEQRVadrsREaelaqqsktrflaaISHDV---LQplnaarLFASALR---E 811
Cdd:COG3920   271 AAGIRL----VITERKRAEEELEASLEEKELLL----RE--------------LHHRVknnLQ------VVSSLLRlqaR 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  812 SHQNNEEQRHLAE---RVDAsLRAAEELLDGLLDVSRLDAGglrptvedfdasALMHELAAQYAPVAGSRGLRLQVHARA 888
Cdd:COG3920   323 RADDPEAREALEEsqnRIQA-LALVHELLYQSEDWEGVDLR------------DYLRELLEPLRDSYGGRGIRIELDGPD 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  889 LWVRSDRRL-LRRVMQNFLANALRY----TRQGRIVLGMRGRGAQVELQVWDTGPGIPEhhmrqifeefrryqqPFDWGE 963
Cdd:COG3920   390 VELPADAAVpLGLILNELVTNALKHaflsGEGGRIRVSWRREDGRLRLTVSDNGVGLPE---------------DVDPPA 454
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 499349852  964 QGlGLGLSICQRISRLLDHDLSARSqvGQGSMFSILLPRVDAVP 1007
Cdd:COG3920   455 RK-GLGLRLIRALVRQLGGTLELDR--PEGTRVRITFPLAELAA 495
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1029-1099 4.54e-03

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: 38.53  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852 1029 RVLCVDnDREIldgMRALLGRW-----QVEVI-TASTVDQALELARE-RPDVMLVDYHLhDRLDGLD------------- 1088
Cdd:cd17541     2 RVLIVD-DSAV---MRKLLSRIlesdpDIEVVgTARDGEEALEKIKElKPDVITLDIEM-PVMDGLEalrrimaerptpv 76
                          90       100
                  ....*....|....*....|....
gi 499349852 1089 -------------TLDALQAAAVD 1099
Cdd:cd17541    77 vmvsslteegaeiTLEALELGAVD 100
SLC5sbd_u3 cd11479
Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain; SLC5 ...
272-452 6.95e-03

Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain; SLC5 (also called the sodium/glucose cotransporter family or solute sodium symporter family) is a family of proteins that co-transports Na+ with sugars, amino acids, inorganic ions or vitamins. Prokaryotic members of this family include Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. One member of the SLC5 family, human SGLT3, has been characterized as a glucose sensor and not a transporter. This subfamily belongs to the solute carrier 5 (SLC5) transporter family.


Pssm-ID: 271373  Cd Length: 454  Bit Score: 40.28  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  272 ARW---LFGAYLVIISAMVVPIASAGVALFgQDSSVVDDA----VVLALPLSQGNTVLAlvayvggfSAATGMVIVAS-- 342
Cdd:cd11479   252 ARWggvAAGLYCVLYGVAGALIGMAAAVLL-PDLANPQNAfatmAQEVLPVGLRGLVLA--------AALAAMMSTASga 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349852  343 -IALATMVSNDLVMPvlLRRRSSADARATVASRVLwirrvaILLLALIAYGYhrSVANDTTLAAYGlMAFAAV--AQFAP 419
Cdd:cd11479   323 lLASSTVLTNDVLPR--LRRKNESERSEVRLSRLF------TLLLGVVVIVI--AVLVNDVVAALT-IAYAILvgGLLVP 391
                         170       180       190
                  ....*....|....*....|....*....|...
gi 499349852  420 gVIGGLYWRGASRKGVETGMVLGFMTWIYTLLL 452
Cdd:cd11479   392 -ILGGLFWKRATGAGALASMVAGSVVVLAGMAV 423
 
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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