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Conserved domains on  [gi|1085292533|gb|OGU69864|]
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MAG: hypothetical protein A2X62_06605 [Stygiobacter sp. GWC2_38_9]

Protein Classification

ATP-binding protein( domain architecture ID 1002581)

ATP-binding protein similar to the ATPase domains of hybrid sensor kinases that regulate diverse biological functions through distinct molecular mechanisms

CATH:  3.30.565.10
EC:  2.7.13.3
Gene Ontology:  GO:0000155|GO:0005524
PubMed:  10966457
SCOP:  4001957

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
18-254 2.68e-70

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


:

Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 220.93  E-value: 2.68e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  18 AKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEIT--TDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNL 95
Cdd:COG2205     5 ALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  96 ELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYT-LHGKIGIHAAKNisd 174
Cdd:COG2205    85 SLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSpPGGTITISARRE--- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 175 gHETLVIRVTDTGIGIAKETQEIIWNEFRQASegLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:COG2205   162 -GDGVRISVSDNGPGIPEEELERIFERFYRGD--NSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
279-401 1.73e-28

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: 108.40  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 279 ASANKKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKYSKT 357
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMP-GMDGLELLRRIRALPRLPDI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085292533 358 PVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFA 401
Cdd:COG0784    81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
 
Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
18-254 2.68e-70

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 220.93  E-value: 2.68e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  18 AKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEIT--TDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNL 95
Cdd:COG2205     5 ALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  96 ELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYT-LHGKIGIHAAKNisd 174
Cdd:COG2205    85 SLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSpPGGTITISARRE--- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 175 gHETLVIRVTDTGIGIAKETQEIIWNEFRQASegLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:COG2205   162 -GDGVRISVSDNGPGIPEEELERIFERFYRGD--NSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
17-403 9.14e-66

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 225.81  E-value: 9.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  17 LAKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNLE 96
Cdd:TIGR02956 452 KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  97 LYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYS-DRSLMRNILTELVSNAVKYTLHGKIGIhaakNIS-D 174
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQgDGPRIRQVLINLVGNAIKFTDRGSVVL----RVSlN 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 175 GHETLVIRVTDTGIGIAKETQEIIWNEFRQAsEGLNRSfEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:TIGR02956 608 DDSSLLFEVEDTGCGIAEEEQATLFDAFTQA-DGRRRS-GGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 255 vlqelDEKLAVSYADETISLANVgasankKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDI 333
Cdd:TIGR02956 686 -----GKPAEDSATLTVIDLPPQ------RVLLVEDNEVNQMVAQGFLTRLgHKVTLAESGQSALECFHQHAFDLALLDI 754
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085292533 334 NIGrEISGIDLINEVKEI-GKYSKTPVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFAEK 403
Cdd:TIGR02956 755 NLP-DGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGG 824
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
4-403 6.67e-48

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 173.97  E-value: 6.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   4 DLTQRKEAEEkmklAKEKAeemNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNN 83
Cdd:PRK11091  265 DITERKRYQD----ALEKA---SRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFND 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  84 ILDLSKLELGNLELYYEPVDVEELIDAVYN-SFLDdAAKKGIA-VEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTLH 161
Cdd:PRK11091  338 IIDMDKMERRKLQLDNQPIDFTDFLADLENlSGLQ-AEQKGLRfDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQ 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 162 GKIGIHAaknISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGL-NRSFEGTGLGLTLCKKYVELLNGKIYVESEV 240
Cdd:PRK11091  417 GGVTVRV---RYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHgGKPATGTGIGLAVSKRLAQAMGGDITVTSEE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 241 GAGSTFIAEIPVTSVLQELDEKLavsyADETISLANVgasankKILYIDDDSLSLTVVERYL-SNEYSVECVSGAPQFLE 319
Cdd:PRK11091  494 GKGSCFTLTIHAPAVAEEVEDAF----DEDDMPLPAL------NILLVEDIELNVIVARSVLeKLGNSVDVAMTGKEALE 563
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 320 KLNEAAFDCILMDINIgREISGIDLINEVKEI-GKYSKTPVVAVTAYALKSDEELiLSKGFSHYISKPFNKKDILNLLRK 398
Cdd:PRK11091  564 MFDPDEYDLVLLDIQL-PDMTGLDIARELRERyPREDLPPLVALTANVLKDKKEY-LDAGMDDVLSKPLSVPALTAMIKK 641

                  ....*
gi 1085292533 399 IFAEK 403
Cdd:PRK11091  642 FWDTQ 646
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
144-252 2.25e-36

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: 128.38  E-value: 2.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 144 MRNILTELVSNAVKYTLHGKIGIHAAK-NISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTL 222
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLeEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1085292533 223 CKKYVELLNGKIYVESEVGAGSTFIAEIPV 252
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
140-253 1.71e-28

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 107.73  E-value: 1.71e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  140 DRSLMRNILTELVSNAVKYTLH-GKIGIHAakniSDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGlNRSFEGTGL 218
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEgGRITVTL----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGL 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1085292533  219 GLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVT 253
Cdd:smart00387  77 GLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
279-401 1.73e-28

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: 108.40  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 279 ASANKKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKYSKT 357
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMP-GMDGLELLRRIRALPRLPDI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085292533 358 PVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFA 401
Cdd:COG0784    81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
32-246 1.48e-26

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 111.38  E-value: 1.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  32 FFANMSHELRTPfvgiigfaeiikeITT--------------DSEIA-NMASCIMDSSKRMTNTLNNILDLSKLELGNLE 96
Cdd:NF033092  375 FVANVSHELRTP-------------LTTmrsylealadgawkDPELApRFLGVTQNETERMIRLVNDLLQLSRMDSKDYK 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  97 LYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTLH-GKIGIHAAKNisdg 175
Cdd:NF033092  442 LNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEgGTITFRLLET---- 517
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085292533 176 HETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTF 246
Cdd:NF033092  518 HNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTI 588
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
140-253 2.34e-25

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: 98.98  E-value: 2.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 140 DRSLMRNILTELVSNAVKYTLH-GKIGIHaaknISDGHEtLVIRVTDTGIGIAKETQEIIWNEFRQASeglNRSFEGTGL 218
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKaGEITVT----LSEGGE-LTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGL 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1085292533 219 GLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVT 253
Cdd:pfam02518  74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
20-251 1.02e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 93.74  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  20 EKAEEMNKvksSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMAScIMDSSKRMTNTLNNILDLSKLELGNLELYY 99
Cdd:NF012163  234 EKNEQMRR---DFMADISHELRTPLAVLRAELEAIQDGIRKFTPESLDS-LQAEVGTLTKLVDDLHDLSMSDEGALAYQK 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 100 EPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGfTTPIYSDRSLMRNILTELVSNAVKYT-LHGKIGIHAAKNisdgHET 178
Cdd:NF012163  310 ASVDLVPLLEVEGGAFRERFASAGLELEVSLPD-SSLVFGDRDRLMQLFNNLLENSLRYTdSGGSLHISASQR----PKE 384
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085292533 179 LVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:NF012163  385 VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
285-396 7.54e-20

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: 84.06  E-value: 7.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSK-TPVVAV 362
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLgYEVDVAENGQEALELLKEEPFDLVLMDLQM-PVMDGLEATRRIRELEGGGRrTPIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1085292533 363 TAYALKSDEELILSKGFSHYISKPFNKKDILNLL 396
Cdd:cd17546    80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
23-251 1.05e-19

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 90.85  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  23 EEMNKVKSSFFANMSHELRTPFVGIIGFAEII--KEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNLELYYE 100
Cdd:NF040691  265 EELSRLQQRFVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 101 PVDVEELIDAVYNSFLDDAAKKGIAVEktVTGFTTPIYSD---RSLMRnILTELVSNAVKYTLHGKIGIHAAKNisdghE 177
Cdd:NF040691  345 PVDLRPLVRRVVDALRQLAERAGVELR--VDAPGTPVVAEvdpRRVER-VLRNLVVNAIEHGEGKPVVVTVAQD-----D 416
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085292533 178 TLV-IRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:NF040691  417 TAVaVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLP 491
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
285-397 6.93e-17

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: 76.04  E-value: 6.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEIGkySKTPVVAVT 363
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPG-MDGLELLKRIRRRD--PTTPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFNKKDILNLLR 397
Cdd:pfam00072  78 AHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
284-399 2.42e-10

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 60.20  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAaFDCILMDINIGREiSGIDLInevKEIGKYSKTPVVAV 362
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQALDLLDDS-IDLLLLDVMMPKK-NGIDTL---KELRQTHQTPVIML 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1085292533 363 TAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKI 399
Cdd:PRK10955   78 TARGSELDRVLGLELGADDYLPKPFNDRELVARIRAI 114
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
283-334 1.35e-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: 47.95  E-value: 1.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1085292533  283 KKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDIN 334
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIM 53
 
Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
18-254 2.68e-70

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 220.93  E-value: 2.68e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  18 AKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEIT--TDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNL 95
Cdd:COG2205     5 ALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  96 ELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYT-LHGKIGIHAAKNisd 174
Cdd:COG2205    85 SLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSpPGGTITISARRE--- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 175 gHETLVIRVTDTGIGIAKETQEIIWNEFRQASegLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:COG2205   162 -GDGVRISVSDNGPGIPEEELERIFERFYRGD--NSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
2-253 2.29e-68

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 219.39  E-value: 2.29e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   2 YIDLTQRKEAEEKMKLAKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEiTTDSEIANMASCIMDSSKRMTNTL 81
Cdd:COG0642    83 LLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLE-ELDEEQREYLETILRSADRLLRLI 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  82 NNILDLSKLELGNLELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTLH 161
Cdd:COG0642   162 NDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPE 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 162 G-KIGIHAakniSDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGlnRSFEGTGLGLTLCKKYVELLNGKIYVESEV 240
Cdd:COG0642   242 GgTVTVSV----RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEP 315
                         250
                  ....*....|...
gi 1085292533 241 GAGSTFIAEIPVT 253
Cdd:COG0642   316 GKGTTFTVTLPLA 328
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
17-403 9.14e-66

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 225.81  E-value: 9.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  17 LAKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNLE 96
Cdd:TIGR02956 452 KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  97 LYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYS-DRSLMRNILTELVSNAVKYTLHGKIGIhaakNIS-D 174
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQgDGPRIRQVLINLVGNAIKFTDRGSVVL----RVSlN 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 175 GHETLVIRVTDTGIGIAKETQEIIWNEFRQAsEGLNRSfEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:TIGR02956 608 DDSSLLFEVEDTGCGIAEEEQATLFDAFTQA-DGRRRS-GGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 255 vlqelDEKLAVSYADETISLANVgasankKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDI 333
Cdd:TIGR02956 686 -----GKPAEDSATLTVIDLPPQ------RVLLVEDNEVNQMVAQGFLTRLgHKVTLAESGQSALECFHQHAFDLALLDI 754
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085292533 334 NIGrEISGIDLINEVKEI-GKYSKTPVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFAEK 403
Cdd:TIGR02956 755 NLP-DGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGG 824
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
20-252 3.75e-61

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 202.48  E-value: 3.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  20 EKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKE--ITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNLEL 97
Cdd:COG5002   156 TELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKL 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  98 YYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTL-HGKIGIHAAKNisdgH 176
Cdd:COG5002   236 EKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPeGGTITVSLREE----D 311
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085292533 177 ETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPV 252
Cdd:COG5002   312 DQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
4-403 6.67e-48

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 173.97  E-value: 6.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   4 DLTQRKEAEEkmklAKEKAeemNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNN 83
Cdd:PRK11091  265 DITERKRYQD----ALEKA---SRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFND 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  84 ILDLSKLELGNLELYYEPVDVEELIDAVYN-SFLDdAAKKGIA-VEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTLH 161
Cdd:PRK11091  338 IIDMDKMERRKLQLDNQPIDFTDFLADLENlSGLQ-AEQKGLRfDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQ 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 162 GKIGIHAaknISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGL-NRSFEGTGLGLTLCKKYVELLNGKIYVESEV 240
Cdd:PRK11091  417 GGVTVRV---RYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHgGKPATGTGIGLAVSKRLAQAMGGDITVTSEE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 241 GAGSTFIAEIPVTSVLQELDEKLavsyADETISLANVgasankKILYIDDDSLSLTVVERYL-SNEYSVECVSGAPQFLE 319
Cdd:PRK11091  494 GKGSCFTLTIHAPAVAEEVEDAF----DEDDMPLPAL------NILLVEDIELNVIVARSVLeKLGNSVDVAMTGKEALE 563
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 320 KLNEAAFDCILMDINIgREISGIDLINEVKEI-GKYSKTPVVAVTAYALKSDEELiLSKGFSHYISKPFNKKDILNLLRK 398
Cdd:PRK11091  564 MFDPDEYDLVLLDIQL-PDMTGLDIARELRERyPREDLPPLVALTANVLKDKKEY-LDAGMDDVLSKPLSVPALTAMIKK 641

                  ....*
gi 1085292533 399 IFAEK 403
Cdd:PRK11091  642 FWDTQ 646
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
17-396 3.18e-47

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 172.73  E-value: 3.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  17 LAKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFA-EIIKEITTDSEIANMaSCIMDSSKRMTNTLNNILDLSKLELGNL 95
Cdd:PRK11107  281 LAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTrQTLKTPLTPTQRDYL-QTIERSANNLLAIINDILDFSKLEAGKL 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  96 ELYYEPVDVEELIDAVYNSFLDDAAKKGIA--------VEKTVTGfttpiysDRSLMRNILTELVSNAVKYTLHGKIGIH 167
Cdd:PRK11107  360 VLENIPFSLRETLDEVVTLLAHSAHEKGLEltlnidpdVPDNVIG-------DPLRLQQIITNLVGNAIKFTESGNIDIL 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 168 AAK-NISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTF 246
Cdd:PRK11107  433 VELrALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTF 512
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 247 IAEIPVtsvlqELDEkLAVSYADETISLanvgasANKKILYIDDDSLSLTVVERYLSNEysVECVSGAPQfLEKLNEAAF 326
Cdd:PRK11107  513 WFHLPL-----DLNP-NPIIDGLPTDCL------AGKRLLYVEPNSAAAQATLDILSET--PLEVTYSPT-LSQLPEAHY 577
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 327 DCILMDINIGREISGIDLINEVKEIGKYSKTPVVAVTAYALKSDEELIlSKGFSHYISKPFNKKDILNLL 396
Cdd:PRK11107  578 DILLLGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLK-QDGADACLSKPLSHTRLLPAL 646
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
7-254 1.32e-45

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 164.19  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   7 QRKEAEEKMKLAKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKE---ITTDSEIANMASCIMDSSKRMTNTLNN 83
Cdd:COG4251   260 ELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGREYLERIRDAAERMQALIDD 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  84 ILDLSKLelGNLELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEktVTGFTTpIYSDRSLMRNILTELVSNAVKYT---L 160
Cdd:COG4251   340 LLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIE--VGPLPT-VRGDPTLLRQVFQNLISNAIKYSrpgE 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 161 HGKIGIHAAKNisdgHETLVIRVTDTGIGIAKETQEIIWNEFRQASEglNRSFEGTGLGLTLCKKYVELLNGKIYVESEV 240
Cdd:COG4251   415 PPRIEIGAERE----GGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHS--RDEYEGTGIGLAIVKKIVERHGGRIWVESEP 488
                         250
                  ....*....|....
gi 1085292533 241 GAGSTFIAEIPVTS 254
Cdd:COG4251   489 GEGATFYFTLPKAP 502
PRK15347 PRK15347
two component system sensor kinase;
18-386 2.16e-41

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 155.96  E-value: 2.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  18 AKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMAscimDSSKRMTNTL----NNILDLSKLELG 93
Cdd:PRK15347  387 AKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLA----DTARQCTLSLlaiiNNLLDFSRIESG 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  94 NLELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTG-FTTPIYSDRSLMRNILTELVSNAVKYTLHGKIGIHAAKNi 172
Cdd:PRK15347  463 QMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAhVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRH- 541
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 173 sdgHETLVIRVTDTGIGIAKETQEIIWNEFRQASEglnrSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPV 252
Cdd:PRK15347  542 ---EQQLCFTVEDTGCGIDIQQQQQIFTPFYQADT----HSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPL 614
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 253 TSV---------------------------LQELDE-------------KL-----AVSYADETISLANVGASANK-KIL 286
Cdd:PRK15347  615 NEYappeplkgelsaplalhrqlsawgitcQPGHQNpalldpelaylpgRLydllqQIIQGAPNEPVINLPLQPWQlQIL 694
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 287 YIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLI----NEVKEIGkySKTPVVA 361
Cdd:PRK15347  695 LVDDVETNRDIIGMMLVELgQQVTTAASGTEALELGRQHRFDLVLMDIRM-PGLDGLETTqlwrDDPNNLD--PDCMIVA 771
                         410       420
                  ....*....|....*....|....*
gi 1085292533 362 VTAYALKSDEELILSKGFSHYISKP 386
Cdd:PRK15347  772 LTANAAPEEIHRCKKAGMNHYLTKP 796
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
4-387 1.25e-39

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 151.04  E-value: 1.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533    4 DLTQRKEAEEKMKLAKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMA-SCIMDSSKRMTNTLN 82
Cdd:PRK09959   687 DITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAiSLAYATGQSLLGLIG 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   83 NILDLSKLELGNLELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVT---GFTTPIysDRSLMRNILTELVSNAVKYT 159
Cdd:PRK09959   767 EILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfpdHYLVKI--DPQAFKQVLSNLLSNALKFT 844
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  160 LHGKIGIHAA-KNISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGlnRSFEGTGLGLTLCKKYVELLNGKIYVES 238
Cdd:PRK09959   845 TEGAVKITTSlGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAG--RQQTGSGLGLMICKELIKNMQGDLSLES 922
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  239 EVGAGSTFIAEIPVtsvlqELDEKLAV--SYADETISLANvgasaNKKILYIDDDSLSLTVVERYLS-NEYSVECVSGAP 315
Cdd:PRK09959   923 HPGIGTTFTITIPV-----EISQQVATveAKAEQPITLPE-----KLSILIADDHPTNRLLLKRQLNlLGYDVDEATDGV 992
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085292533  316 QFLEKLNEAAFDCILMDINIgREISGIDLINEVKEigKYSKTPVVAVTAYALKSDEELILSKGFSHYISKPF 387
Cdd:PRK09959   993 QALHKVSMQHYDLLITDVNM-PNMDGFELTRKLRE--QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPL 1061
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
144-252 2.25e-36

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: 128.38  E-value: 2.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 144 MRNILTELVSNAVKYTLHGKIGIHAAK-NISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTL 222
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLeEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1085292533 223 CKKYVELLNGKIYVESEVGAGSTFIAEIPV 252
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
28-246 1.50e-35

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


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 133.10  E-value: 1.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  28 VKSSFFANMSHELRTPFVGIIGFAEIIKE-ITTDSEIANMASCIM-DSSKRMTNTLNNILDLSKLELGNLELYYEPVDVE 105
Cdd:TIGR02966 113 MRRDFVANVSHELRTPLTVLRGYLETLADgPDEDPEEWNRALEIMlEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMP 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 106 ELIDAVYNSFLDDAAKKGIAVEKTVTGfTTPIYSDRSLMRNILTELVSNAVKYTLHGK-IGIHAAKniSDGHetLVIRVT 184
Cdd:TIGR02966 193 ALLDHLRDEAEALSQGKNHQITFEIDG-GVDVLGDEDELRSAFSNLVSNAIKYTPEGGtITVRWRR--DGGG--AEFSVT 267
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085292533 185 DTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTF 246
Cdd:TIGR02966 268 DTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
3-251 2.30e-35

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 138.18  E-value: 2.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   3 IDLTQRKEAEEKMKLAKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLN 82
Cdd:PRK10841  421 VDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIIS 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  83 NILDLSKLELGNLELYYEPVDVEELIDAVYNSFLDDAAKKGIA----VEKTVtgfttPIYSDRSLMR--NILTELVSNAV 156
Cdd:PRK10841  501 DILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGlycfIEPDV-----PVALNGDPMRlqQVISNLLSNAI 575
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 157 KYTLHGKIGIHAAKNisdgHETLVIRVTDTGIGIakETQEII--WNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKI 234
Cdd:PRK10841  576 KFTDTGCIVLHVRVD----GDYLSFRVRDTGVGI--PAKEVVrlFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDI 649
                         250
                  ....*....|....*..
gi 1085292533 235 YVESEVGAGSTFIAEIP 251
Cdd:PRK10841  650 SVDSEPGMGSQFTIRIP 666
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
4-253 5.61e-34

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 129.53  E-value: 5.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   4 DLTQRKEAEEKMKLAKEKAEEMNKVKS--SFFANMSHELRTPFVGIIGFAEIIKEIT----TDSEIANMASCIMDSSKRM 77
Cdd:COG4191   115 DITELERAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGNAELLRRRLedepDPEELREALERILEGAERA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  78 TNTLNNILDLSKLElgnlELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSN--- 154
Cdd:COG4191   195 AEIVRSLRAFSRRD----EEEREPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINaid 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 155 AVKYTLHGKIGIHAAKnisdGHETLVIRVTDTGIGIAKETQEIIWNEFrqaseglnrsF------EGTGLGLTLCKKYVE 228
Cdd:COG4191   271 AMEEGEGGRITISTRR----EGDYVVISVRDNGPGIPPEVLERIFEPF----------FttkpvgKGTGLGLSISYGIVE 336
                         250       260
                  ....*....|....*....|....*
gi 1085292533 229 LLNGKIYVESEVGAGSTFIAEIPVT 253
Cdd:COG4191   337 KHGGRIEVESEPGGGTTFTITLPLA 361
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
1-252 1.70e-33

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: 130.48  E-value: 1.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   1 MYIDLTQRKEAEEKMklakEKAEEMNKVkSSFFANMSHELRTPFVGIIGFAEIIKEiTTDSEIANMASCIMDSSKRMTNT 80
Cdd:COG5809   247 IFRDITERKKLEELL----RKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKD-TIDEEQKTYLDIMLSELDRIESI 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  81 LNNILDLSKLElgnlELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYT- 159
Cdd:COG5809   321 ISEFLVLAKPQ----AIKYEPKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMp 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 160 LHGKIGIHAAKnisDGHETLVIRVTDTGIGIAKETQEIIWNEFrqasegLNRSFEGTGLGLTLCKKYVELLNGKIYVESE 239
Cdd:COG5809   397 EGGNITIETKA---EDDDKVVISVTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESE 467
                         250
                  ....*....|...
gi 1085292533 240 VGAGSTFIAEIPV 252
Cdd:COG5809   468 VGKGTTFSITLPI 480
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
4-254 5.15e-32

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 124.19  E-value: 5.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   4 DLTQRKEAEEKMKLAkEKAE---EMnkvkssfFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNT 80
Cdd:COG3852   115 DITERKRLERELRRA-EKLAavgEL-------AAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNL 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  81 LNNILDLSKLELGNLElyyePVDVEELIDAVYNSFLDDAAKkGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKY-T 159
Cdd:COG3852   187 VDRLLSFSRPRPPERE----PVNLHEVLERVLELLRAEAPK-NIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAmP 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 160 LHGKIGIHAAKNISD------GHETLVIRVTDTGIGIAKETQEIIWNEFrqaseglnrsF----EGTGLGLTLCKKYVEL 229
Cdd:COG3852   262 EGGTITIRTRVERQVtlgglrPRLYVRIEVIDNGPGIPEEILDRIFEPF----------FttkeKGTGLGLAIVQKIVEQ 331
                         250       260
                  ....*....|....*....|....*
gi 1085292533 230 LNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:COG3852   332 HGGTIEVESEPGKGTTFRIYLPLEQ 356
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
18-396 1.48e-30

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 124.25  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  18 AKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELG--NL 95
Cdd:PRK11466  433 ARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNV 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  96 ELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVT-GFTTPIYSDRSLMRNILTELVSNAVKYTLHGKIGIHAAkniSD 174
Cdd:PRK11466  513 SVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIAdDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSR---TD 589
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 175 GhETLVIRVTDTGIGIAKETQEIIWNEFRQASEglNRSfeGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:PRK11466  590 G-EQWLVEVEDSGCGIDPAKLAEIFQPFVQVSG--KRG--GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRV 664
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 255 VLQELDEKLAvsyadETISLanvgasANKKILYIDDDSLSLTV-VERYLSNEYSVECVSGAPQFLEKL-NEAAFDCILMD 332
Cdd:PRK11466  665 ATAPVPKTVN-----QAVRL------DGLRLLLIEDNPLTQRItAEMLNTSGAQVVAVGNAAQALETLqNSEPFAAALVD 733
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085292533 333 INIgREISGIDLINEVKEigKYSKTPVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLL 396
Cdd:PRK11466  734 FDL-PDYDGITLARQLAQ--QYPSLVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLL 794
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
140-253 1.71e-28

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 107.73  E-value: 1.71e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  140 DRSLMRNILTELVSNAVKYTLH-GKIGIHAakniSDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGlNRSFEGTGL 218
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEgGRITVTL----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGL 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1085292533  219 GLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVT 253
Cdd:smart00387  77 GLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
279-401 1.73e-28

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: 108.40  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 279 ASANKKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKYSKT 357
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMP-GMDGLELLRRIRALPRLPDI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085292533 358 PVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFA 401
Cdd:COG0784    81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
36-253 4.21e-28

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: 114.29  E-value: 4.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  36 MSHELRTPFVGIIGFAEIIK-----EITTDSEIAN-MASCIMDSSKRMTNTLNNILDLSKLELGNLElyyePVDVEELID 109
Cdd:COG5000   208 IAHEIKNPLTPIQLSAERLRrkladKLEEDREDLErALDTIIRQVDRLKRIVDEFLDFARLPEPQLE----PVDLNELLR 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 110 AVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTL-HGKIGIHAAKNisdgHETLVIRVTDTGI 188
Cdd:COG5000   284 EVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEeGGEIEVSTRRE----DGRVRIEVSDNGP 359
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085292533 189 GIAKETqeiiwnefrqasegLNRSFE--------GTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVT 253
Cdd:COG5000   360 GIPEEV--------------LERIFEpffttkpkGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
32-246 1.48e-26

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 111.38  E-value: 1.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  32 FFANMSHELRTPfvgiigfaeiikeITT--------------DSEIA-NMASCIMDSSKRMTNTLNNILDLSKLELGNLE 96
Cdd:NF033092  375 FVANVSHELRTP-------------LTTmrsylealadgawkDPELApRFLGVTQNETERMIRLVNDLLQLSRMDSKDYK 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  97 LYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTLH-GKIGIHAAKNisdg 175
Cdd:NF033092  442 LNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEgGTITFRLLET---- 517
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085292533 176 HETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTF 246
Cdd:NF033092  518 HNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTI 588
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
140-253 2.34e-25

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: 98.98  E-value: 2.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 140 DRSLMRNILTELVSNAVKYTLH-GKIGIHaaknISDGHEtLVIRVTDTGIGIAKETQEIIWNEFRQASeglNRSFEGTGL 218
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKaGEITVT----LSEGGE-LTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGL 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1085292533 219 GLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVT 253
Cdd:pfam02518  74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
4-252 1.80e-24

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 105.44  E-value: 1.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   4 DLTQRKEAEEKMKLAKEKAeemnkVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNN 83
Cdd:PRK11360  370 DLTERKRLQRRVARQERLA-----ALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQ 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  84 ILDLSKLElgnlELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVK-YTLHG 162
Cdd:PRK11360  445 LLEFSRPR----ESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQaISARG 520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 163 KIGIhAAKNISDGHetLVIRVTDTGIGIAKETQEIIWNEF---RQAseglnrsfeGTGLGLTLCKKYVELLNGKIYVESE 239
Cdd:PRK11360  521 KIRI-RTWQYSDGQ--VAVSIEDNGCGIDPELLKKIFDPFfttKAK---------GTGLGLALSQRIINAHGGDIEVESE 588
                         250
                  ....*....|...
gi 1085292533 240 VGAGSTFIAEIPV 252
Cdd:PRK11360  589 PGVGTTFTLYLPI 601
PRK10490 PRK10490
sensor protein KdpD; Provisional
5-263 1.66e-23

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 102.81  E-value: 1.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   5 LTQRkeaEEKMKLAKEKaeemNKVKSSFFANMSHELRTPFVGIIGFAEIIkeiTTD-----SEIANMASCIMDSSKRMTN 79
Cdd:PRK10490  647 LTAS---EEQARLASER----EQLRNALLAALSHDLRTPLTVLFGQAEIL---TLDlasegSPHARQASEIRQQVLNTTR 716
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  80 TLNNILDLSKLELGNLELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEktVTGFTTPIYSDRSLMRNILTELVSNAVKYT 159
Cdd:PRK10490  717 LVNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLS--LPEPLTLIHVDGPLFERVLINLLENAVKYA 794
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 160 LHG-KIGIHAakniSDGHETLVIRVTDTGIGIAKETQEIIWNEFrqaSEGLNRS-FEGTGLGLTLCKKYVELLNGKIYVE 237
Cdd:PRK10490  795 GAQaEIGIDA----HVEGERLQLDVWDNGPGIPPGQEQLIFDKF---ARGNKESaIPGVGLGLAICRAIVEVHGGTIWAE 867
                         250       260
                  ....*....|....*....|....*...
gi 1085292533 238 SEVGAGSTFIAEIPVTSV--LQELDEKL 263
Cdd:PRK10490  868 NRPEGGACFRVTLPLETPpeLEEFHEDM 895
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
8-252 1.41e-21

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 96.01  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   8 RKEAEEKMKlAKEKAEEMNKVKssffANMSHELRTPFVGIIG----FAEIIKEITTDSEIAN-MAScimdSSKRMTNTLN 82
Cdd:PRK10364  221 RQLLQDEMK-RKEKLVALGHLA----AGVAHEIRNPLSSIKGlakyFAERAPAGGEAHQLAQvMAK----EADRLNRVVS 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  83 NILDLSKLElgnlELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYT-LH 161
Cdd:PRK10364  292 ELLELVKPT----HLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIgQH 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 162 GKIGIhAAKNISDGhetLVIRVTDTGIGIAKETQEIIWNEFrqasegLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVG 241
Cdd:PRK10364  368 GVISV-TASESGAG---VKISVTDSGKGIAADQLEAIFTPY------FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEG 437
                         250
                  ....*....|.
gi 1085292533 242 AGSTFIAEIPV 252
Cdd:PRK10364  438 KGATFTLWLPV 448
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
283-403 9.20e-21

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: 93.49  E-value: 9.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIgkYSKTPVVA 361
Cdd:COG2204     3 ARILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMP-GMDGLELLRELRAL--DPDLPVIL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1085292533 362 VTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFAEK 403
Cdd:COG2204    80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERR 121
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
20-251 1.02e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 93.74  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  20 EKAEEMNKvksSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMAScIMDSSKRMTNTLNNILDLSKLELGNLELYY 99
Cdd:NF012163  234 EKNEQMRR---DFMADISHELRTPLAVLRAELEAIQDGIRKFTPESLDS-LQAEVGTLTKLVDDLHDLSMSDEGALAYQK 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 100 EPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGfTTPIYSDRSLMRNILTELVSNAVKYT-LHGKIGIHAAKNisdgHET 178
Cdd:NF012163  310 ASVDLVPLLEVEGGAFRERFASAGLELEVSLPD-SSLVFGDRDRLMQLFNNLLENSLRYTdSGGSLHISASQR----PKE 384
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085292533 179 LVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:NF012163  385 VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
282-393 3.43e-20

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: 87.27  E-value: 3.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 282 NKKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKYSKTPVV 360
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAgYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1085292533 361 AVTAYALKSDEELILSKGFSHYISKPFNKKDIL 393
Cdd:COG3706    80 FLTALDDEEDRARALEAGADDYLTKPFDPEELL 112
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
285-396 7.54e-20

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: 84.06  E-value: 7.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSK-TPVVAV 362
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLgYEVDVAENGQEALELLKEEPFDLVLMDLQM-PVMDGLEATRRIRELEGGGRrTPIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1085292533 363 TAYALKSDEELILSKGFSHYISKPFNKKDILNLL 396
Cdd:cd17546    80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
23-251 1.05e-19

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 90.85  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  23 EEMNKVKSSFFANMSHELRTPFVGIIGFAEII--KEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNLELYYE 100
Cdd:NF040691  265 EELSRLQQRFVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 101 PVDVEELIDAVYNSFLDDAAKKGIAVEktVTGFTTPIYSD---RSLMRnILTELVSNAVKYTLHGKIGIHAAKNisdghE 177
Cdd:NF040691  345 PVDLRPLVRRVVDALRQLAERAGVELR--VDAPGTPVVAEvdpRRVER-VLRNLVVNAIEHGEGKPVVVTVAQD-----D 416
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085292533 178 TLV-IRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:NF040691  417 TAVaVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLP 491
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
279-403 1.20e-19

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: 86.76  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 279 ASANKKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSKT 357
Cdd:COG3437     3 TGQAPTVLIVDDDPENLELLRQLLRTLgYDVVTAESGEEALELLLEAPPDLILLDVRM-PGMDGFELLRLLRADPSTRDI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1085292533 358 PVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFAEK 403
Cdd:COG3437    82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELR 127
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
284-398 3.72e-19

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 82.20  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSKTPVVAV 362
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQL-PGMDGLEATRLLKEDPATRDIPVIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1085292533 363 TAYALKSDEELILSKGFSHYISKPFNKKDILNLLRK 398
Cdd:cd17548    80 TAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
4-253 5.46e-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: 88.64  E-value: 5.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   4 DLTQRKEAEEKMKlakeKAEEMNkVKSSFFANMSHELRTPFVGIIGFAEIIK-EITTDSEIANMascIMDSSKRMTNTLN 82
Cdd:COG5805   267 DITEKKEAEELMA----RSEKLS-IAGQLAAGIAHEIRNPLTSIKGFLQLLQpGIEDKEEYFDI---MLSELDRIESIIS 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  83 NILDLSKlelgNLELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTLH- 161
Cdd:COG5805   339 EFLALAK----PQAVNKEKENINELIQDVVTLLETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNg 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 162 GKIGIHAAKNisdgHETLVIRVTDTGIGIAKETQEIIWNEFRQASEglnrsfEGTGLGLTLCKKYVELLNGKIYVESEVG 241
Cdd:COG5805   415 GTITIHTEEE----DNSVIIRVIDEGIGIPEERLKKLGEPFFTTKE------KGTGLGLMVSYKIIENHNGTIDIDSKVG 484
                         250
                  ....*....|..
gi 1085292533 242 AGSTFIAEIPVT 253
Cdd:COG5805   485 KGTTFTITLPLS 496
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
283-399 1.63e-18

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: 83.08  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEIGkySKTPVVA 361
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPG-MDGLEVCRRLRARP--SDIPIIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1085292533 362 VTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKI 399
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRAL 116
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
144-251 2.09e-18

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: 80.06  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 144 MRNILTELVSNAVKYT---LHGKIGIHAakniSDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASegLNRSFEGTGLGL 220
Cdd:cd16921     1 LGQVLTNLLGNAIKFRrprRPPRIEVGA----EDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLH--SREEYEGTGVGL 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1085292533 221 TLCKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:cd16921    75 AIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
30-251 3.26e-18

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


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 85.90  E-value: 3.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  30 SSFFANMSHELRTPFVGIIGFAEII--KEITTDSEIANMASCImDSSKRMTNTLNNILDLSKLELGNLELYYEPVDVEEL 107
Cdd:TIGR01386 242 SQFSADLAHELRTPLTNLLGQTQVAlsQPRTGEEYREVLESNL-EELERLSRMVSDMLFLARADNGQLALERVRLDLAAE 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 108 IDAVYNSFLDDAAKKGIAVEKTVTGFttpIYSDRSLMRNILTELVSNAVKYTLHG-KIGIHAAKnisDGHETLViRVTDT 186
Cdd:TIGR01386 321 LAKVAEYFEPLAEERGVRIRVEGEGL---VRGDPQMFRRAISNLLSNALRHTPDGgTITVRIER---RSDEVRV-SVSNP 393
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085292533 187 GIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAgSTFIAEIP 251
Cdd:TIGR01386 394 GPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILRFP 457
PRK09303 PRK09303
histidine kinase;
11-252 6.30e-18

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 84.62  E-value: 6.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  11 AEEKMKLAKEKAE--EMNKVKSSFFANMSHELRTPFVGiigfAEI---------IKEITtDSEIANMAScIMDSSKRMTN 79
Cdd:PRK09303  131 SDELFVLRQENETllEQLKFKDRVLAMLAHDLRTPLTA----ASLaletlelgqIDEDT-ELKPALIEQ-LQDQARRQLE 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  80 TLN----NILDLSKLELGNLELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNA 155
Cdd:PRK09303  205 EIErlitDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNA 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 156 VKYT-LHGKIGIHAAknisdgHET---LVIRVTDTGIGIAKETQEIIW-NEFR-QASEGLnrsfEGTGLGLTLCKKYVEL 229
Cdd:PRK09303  285 IKYTpEGGTITLSML------HRTtqkVQVSICDTGPGIPEEEQERIFeDRVRlPRDEGT----EGYGIGLSVCRRIVRV 354
                         250       260
                  ....*....|....*....|...
gi 1085292533 230 LNGKIYVESEVGAGSTFIAEIPV 252
Cdd:PRK09303  355 HYGQIWVDSEPGQGSCFHFTLPV 377
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
20-257 9.18e-18

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 84.68  E-value: 9.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  20 EKAEEMNKvksSFFANMSHELRTPFVGIIGFAEII----KEITTDS------EIANMascimdsskrmTNTLNNILDLSK 89
Cdd:PRK10549  234 EKNEQMRR---DFMADISHELRTPLAVLRGELEAIqdgvRKFTPESvaslqaEVGTL-----------TKLVDDLHQLSL 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  90 LELGNLELYYEPVDVEELIDAVYNSFLDDAAKKGIAVEkTVTGFTTPIYSDRSLMRNILTELVSNAVKYT-LHGKIGIHA 168
Cdd:PRK10549  300 SDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQ-LSLPDSATVFGDPDRLMQLFNNLLENSLRYTdSGGSLHISA 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 169 AKNisdgHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIA 248
Cdd:PRK10549  379 EQR----DKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITV 454

                  ....*....
gi 1085292533 249 EIPVTSVLQ 257
Cdd:PRK10549  455 ELPLERDLQ 463
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
144-251 2.25e-17

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: 77.15  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 144 MRNILTELVSNAVKYTLHGKIgIHAAKNISDGHETLVIrVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLC 223
Cdd:cd16925     5 YERVVLNLLSNAFKFTPDGGR-IRCILEKFRLNRFLLT-VSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLSIV 82
                          90       100
                  ....*....|....*....|....*...
gi 1085292533 224 KKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:cd16925    83 KEFVELHGGTVTVSDAPGGGALFQVELP 110
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
285-397 6.93e-17

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: 76.04  E-value: 6.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEIGkySKTPVVAVT 363
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPG-MDGLELLKRIRRRD--PTTPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFNKKDILNLLR 397
Cdd:pfam00072  78 AHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
285-396 8.46e-17

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 75.57  E-value: 8.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKYSKTPVVAVT 363
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMP-GMDGYELARRLRELPWLANTPAIALT 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFNKKDILNLL 396
Cdd:cd17580    80 GYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
32-251 1.22e-16

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 81.21  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  32 FFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIM-DSSKRMTNTLNNILDLSKLELGNLELYYEPVDVEELIDA 110
Cdd:PRK11006  207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMrEQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPMMLRV 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 111 V---YNSFLDDAAKKGIAVEKTVTgfttpIYSDRSLMRNILTELVSNAVKYTLHG-KIGIHAAKNiSDGHEtlvIRVTDT 186
Cdd:PRK11006  287 LereAQTLSQGKHTITFEVDNSLK-----VFGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQRV-PQGAE---FSVEDN 357
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085292533 187 GIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:PRK11006  358 GPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
29-93 3.61e-16

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 72.24  E-value: 3.61e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085292533  29 KSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELG 93
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
286-386 4.94e-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: 73.03  E-value: 4.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 286 LYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKysKTPVVAVTA 364
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMP-GMDGLELLRKLRELPP--DIPVIVLTA 77
                          90       100
                  ....*....|....*....|..
gi 1085292533 365 YALKSDEELILSKGFSHYISKP 386
Cdd:cd00156    78 KADEEDAVRALELGADDYLVKP 99
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
282-401 7.02e-15

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 71.15  E-value: 7.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 282 NKKILYIDDDSLSLTVVERYLSNEYSVECV---SGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKysKTP 358
Cdd:COG4565     3 MIRVLIVEDDPMVAELLRRYLERLPGFEVVgvaSSGEEALALLAEHRPDLILLDIYLP-DGDGLELLRELRARGP--DVD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085292533 359 VVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFA 401
Cdd:COG4565    80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
35-243 7.20e-15

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 76.04  E-value: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  35 NMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNLELYYEPVDVEELIDAVYNS 114
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 115 FLDDAAKKGIAVEKTVTGFTtpIYSDRSLMRNILTELVSNAVKYT-LHGKIGIHAAKNisdgHETLVIRVTDTGIGIAKE 193
Cdd:PRK11100  342 REAQAAAKGITLRLRPDDAR--VLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVD----GEQVALSVEDQGPGIPDY 415
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1085292533 194 TQEIIWNEF----RQASEGlnrsfEGTGLGLTLCKKYVELLNGKIYVESEVGAG 243
Cdd:PRK11100  416 ALPRIFERFyslpRPANGR-----KSTGLGLAFVREVARLHGGEVTLRNRPEGG 464
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
29-93 1.29e-14

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 67.98  E-value: 1.29e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085292533   29 KSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELG 93
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
139-246 3.29e-14

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: 68.47  E-value: 3.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 139 SDRSLMRNILTELVSNAVKYT-LHGKIGIHAAKNisdGHETlVIRVTDTGIGIAKETQEIIWNEFRQASEGlNRSFEGTG 217
Cdd:cd16948     1 TDAKWLSFIIGQIVSNALKYSkQGGKIEIYSETN---EQGV-VLSIKDFGIGIPEEDLPRVFDKGFTGENG-RNFQESTG 75
                          90       100
                  ....*....|....*....|....*....
gi 1085292533 218 LGLTLCKKYVELLNGKIYVESEVGAGSTF 246
Cdd:cd16948    76 MGLYLVKKLCDKLGHKIDVESEVGEGTTF 104
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
20-251 1.03e-13

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 72.50  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  20 EKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEI-IKEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELGNLELY 98
Cdd:PRK09835  253 ERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIaLSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPE 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  99 YEPVDVEELIDAVYNSFLDDAAKKGIAVEktVTGFTTPIYSDRSLMRNILTELVSNAVKYTLHGK-IGIHaaknISDGHE 177
Cdd:PRK09835  333 KKMLDLADEVGKVFDFFEAWAEERGVELR--FVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEaITVR----CQEVDH 406
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085292533 178 TLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAgSTFIAEIP 251
Cdd:PRK09835  407 QVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDARG-TRFVISLP 479
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
135-238 4.88e-13

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: 65.61  E-value: 4.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 135 TPIYS--DRSLMRNILTELVSNAVKYTLHGK-IGIhaakNISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNR 211
Cdd:cd16947    10 RPIYAnaNTEALQRILKNLISNAIKYGSDGKfLGM----TLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNS 85
                          90       100
                  ....*....|....*....|....*..
gi 1085292533 212 SFEGTGLGLTLCKKYVELLNGKIYVES 238
Cdd:cd16947    86 AKQGNGLGLTITKRLAESMGGSIYVNS 112
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
284-386 1.03e-12

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: 64.02  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNEYSVECV----SGApQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIgkYSKTPV 359
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAGFEVVgeaeNGE-EALELLEEHKPDLVITDINMP-GMDGLELLEAIREL--DPDTKI 76
                          90       100
                  ....*....|....*....|....*..
gi 1085292533 360 VAVTAYALKSDEELILSKGFSHYISKP 386
Cdd:COG4753    77 IILSGYSDFEYAQEAIKLGADDYLLKP 103
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
26-89 1.13e-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: 1.13e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085292533  26 NKVKSSFFANMSHELRTPFVGIIGFAEIIKE-ITTDSEIANMASCIMDSSKRMTNTLNNILDLSK 89
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEeLLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
280-403 1.20e-12

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: 65.71  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 280 SANKKILYIDDDSLSLTVVERYL-SNEYSVECVSGAPQFLEKLNEAAFDCILMDINIGREiSGIDLINEVKEIgkYSKTP 358
Cdd:COG4567     2 AEDRSLLLVDDDEAFARVLARALeRRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDG-SGLDLIEALRER--DPDAR 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1085292533 359 VVAVTAYAlkSD---EELIlSKGFSHYISKPFNKKDILNLLRKIFAEK 403
Cdd:COG4567    79 IVVLTGYA--SIataVEAI-KLGADDYLAKPADADDLLAALERAEGDA 123
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
14-263 1.58e-12

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 69.19  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  14 KMKLAKEKAEEMNKVKSSFFANMSHELRTPFVGIIGFAEIIKEITTDSEIANMASCIMDSSKRMTNTLNNILDLSKLELG 93
Cdd:PRK10618  435 KLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQ 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  94 NLELYYEPVDVEELIDAVYNSFLDDAAKKG--------IAVEKTVTGfttpiysDRSLMRNILTELVSNAVKYTLHGKIG 165
Cdd:PRK10618  515 DWKPEQELFSLQDLIDEVLPEVLPAIKRKGlqllihnhLKAEQLRIG-------DRDALRKILLLLLNYAITTTAYGKIT 587
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 166 IHAakNISDGH-ETLVIRVTDTGIGIAkeTQEIIWNEFRQASEGLNRSFeGTGLGLT------LCKKyvelLNGKIYVES 238
Cdd:PRK10618  588 LEV--DQDESSpDRLTIRILDTGAGVS--IKELDNLHFPFLNQTQGDRY-GKASGLTfflcnqLCRK----LGGHLTIKS 658
                         250       260
                  ....*....|....*....|....*...
gi 1085292533 239 EVGAGSTFIAEIPVTSVLQEL---DEKL 263
Cdd:PRK10618  659 REGLGTRYSIHLKMLAADPEVeeeEEKL 686
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
286-386 2.39e-12

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 62.81  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 286 LYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEigKYSKTPVVAVTA 364
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLP-GMDGFEVCRRLRE--KGSDIPIIMLTA 77
                          90       100
                  ....*....|....*....|....*.
gi 1085292533 365 yalKSDEELILsKGFSH----YISKP 386
Cdd:cd17574    78 ---KDEEEDKV-LGLELgaddYITKP 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
285-399 4.78e-12

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 62.32  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLInevKEIGKYSKTPVVAVT 363
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEgFNVRAAHDGEQGLAALLEGSPDLVVLDVMLP-KMNGLDVL---KELRKTSQVPVLMLT 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFNKKDILNLLRKI 399
Cdd:cd17623    77 ARGDDIDRILGLELGADDYLPKPFNPRELVARIRAI 112
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
284-399 8.32e-12

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 64.45  E-value: 8.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNEYSVECV---SGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKysKTPVV 360
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDLEVVgeaSNGEEALELLEEHKPDLVFLDIQMP-GLDGFELARQLRELDP--PPPII 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085292533 361 AVTAYalksDEELIlsKGFSH----YISKPFNKKDILNLLRKI 399
Cdd:COG3279    80 FTTAY----DEYAL--EAFEVnavdYLLKPIDEERLAKALEKA 116
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
282-399 9.40e-12

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 61.73  E-value: 9.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 282 NKKILYIDDDS---LSLTVVeryLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGkySKT 357
Cdd:COG5803     2 MKKILIVDDQAgirMLLKEV---LKKEgYEVFQAANGKEALEKVKELKPDLVLLDMKMP-GMDGIEILKEIKEID--PDI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1085292533 358 PVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKI 399
Cdd:COG5803    76 PVIMMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKL 117
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
108-254 1.36e-11

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 65.64  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 108 IDAVYNSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVKYTL-----HGKIGIHaaknISDGHETLVIR 182
Cdd:COG3290   246 LAALLLGKAARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIEAVEklpeeERRVELS----IRDDGDELVIE 321
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085292533 183 VTDTGIGIAKETQEIIWNEFRQASEGlnrsfEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:COG3290   322 VEDSGPGIPEELLEKIFERGFSTKLG-----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEG 388
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
124-243 1.55e-11

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: 60.88  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 124 IAVEKTVTGfttpiysDRSLMRNILTELVSNAVKYTLHG-KIGIhaaknISDGHETLVIRVTDTGIGIAKETQEIIWNEF 202
Cdd:cd16940     1 SAADIQVQG-------DALLLFLLLRNLVDNAVRYSPQGsRVEI-----KLSADDGAVIRVEDNGPGIDEEELEALFERF 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1085292533 203 -RQASeglnRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAG 243
Cdd:cd16940    69 yRSDG----QNYGGSGLGLSIVKRIVELHGGQIFLGNAQGGG 106
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
283-393 2.74e-11

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


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 60.11  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSV-ECVSGAPQFLEKLNEAAFDCILMDINIGREISGIDLineVKEIGKYSKTPVV 360
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLgYEVvGIADSGEEAIELAEENKPDLILMDINLKGDMDGIEA---AREIREKFDIPVI 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1085292533 361 AVTAYalkSDEElILSK----GFSHYISKPFNKKDIL 393
Cdd:cd17534    78 FLTAY---SDEE-TLERaketNPYGYLVKPFNERELK 110
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
2-254 3.66e-11

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 65.08  E-value: 3.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533   2 YIDLtQRKEAE-EKMKLAKEKAEEMNKVkSSFFANMSHELRTPFVGIIGFAEIIKE-ITTDSEIANMASCIMDSSKRMTN 79
Cdd:PRK13837  424 AIER-RRLETErDALERRLEHARRLEAV-GTLASGIAHNFNNILGAILGYAEMALNkLARHSRAARYIDEIISAGARARL 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  80 TLNNILDLSKLELGNLElyyePVDVEELIDAVYnSFLDDAAKKGIAVEKTVTGFTTPIYSDRSLMRNILTELVSNAVK-Y 158
Cdd:PRK13837  502 IIDQILAFGRKGERNTK----PFDLSELVTEIA-PLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQaM 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 159 TLHGKIGIH-------AAKNISDGHET----LVIRVTDTGIGIAKETQEIIWNEFRQASEGlnrsfeGTGLGLTLCKKYV 227
Cdd:PRK13837  577 DGAGRVDISlsraklrAPKVLSHGVLPpgryVLLRVSDTGAGIDEAVLPHIFEPFFTTRAG------GTGLGLATVHGIV 650
                         250       260
                  ....*....|....*....|....*..
gi 1085292533 228 ELLNGKIYVESEVGAGSTFIAEIPVTS 254
Cdd:PRK13837  651 SAHAGYIDVQSTVGRGTRFDVYLPPSS 677
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
175-251 4.15e-11

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 64.55  E-value: 4.15e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085292533 175 GHETLVIRVTDTGIGIAKETQEIIwneFRQ--ASEGLNRsfegtGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:PRK11086  464 RNGWLHCEVSDDGPGIAPDEIDAI---FDKgySTKGSNR-----GVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
140-241 4.99e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 59.40  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 140 DRSLMRNILTELVSNAVKYT-LHGKIGIHAAKNisdgHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGL 218
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTdTGGKLRIRAAQT----PQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                          90       100
                  ....*....|....*....|....
gi 1085292533 219 GLTLCKKYVELLNGKIYVE-SEVG 241
Cdd:cd16946    77 GLAICHNIALAHGGTISAEhSPLG 100
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
147-251 6.42e-11

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: 58.84  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 147 ILTELVSNAVKYTLHGKIG---IHAAknISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRsfegtGLGLTLC 223
Cdd:cd16915     4 IVGNLIDNALDALAATGAPnkqVEVF--LRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGER-----GIGLALV 76
                          90       100
                  ....*....|....*....|....*...
gi 1085292533 224 KKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:cd16915    77 RQSVERLGGSITVESEPGGGTTFSIRIP 104
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
37-221 8.46e-11

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 63.41  E-value: 8.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  37 SHELRTPFVGI-IGFAEIIKEITTDSEIANmascIMDSSKRMTNTLNNILDLSKLELgNLELYYEPVDVEELIDAVynsf 115
Cdd:PRK09470  251 SHELRTPLTRLqLATALLRRRQGESKELER----IETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWSEV---- 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 116 LDDAA------KKGIAVEKTVTGFttPIYSDRSLMRNILTELVSNAVKYTlHGKIGIHaaknISDGHETLVIRVTDTGIG 189
Cdd:PRK09470  322 LEDAKfeaeqmGKSLTVSAPPGPW--PINGNPNALASALENIVRNALRYS-HTKIEVA----FSVDKDGLTITVDDDGPG 394
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1085292533 190 IAKETQEIIWNEFRQASEGLNRSFEGTGLGLT 221
Cdd:PRK09470  395 VPEEEREQIFRPFYRVDEARDRESGGTGLGLA 426
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
284-400 1.05e-10

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 58.50  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSN---EYSVECVSGApQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSKTPVV 360
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKElgfNNVEEAEDGV-DALEKLKAGGFDFVITDWNM-PNMDGLELLKTIRADGALSHLPVL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1085292533 361 AVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIF 400
Cdd:cd19923    80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
151-237 1.59e-10

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


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 57.72  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 151 LVSNAVKYTlHGKIGIHAAKNisdgHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELL 230
Cdd:cd16949     8 VLRNALRYS-PSKILLDISQD----GDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIEQH 82

                  ....*..
gi 1085292533 231 NGKIYVE 237
Cdd:cd16949    83 GGKIKAS 89
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
284-399 2.42e-10

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 60.20  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAaFDCILMDINIGREiSGIDLInevKEIGKYSKTPVVAV 362
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQALDLLDDS-IDLLLLDVMMPKK-NGIDTL---KELRQTHQTPVIML 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1085292533 363 TAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKI 399
Cdd:PRK10955   78 TARGSELDRVLGLELGADDYLPKPFNDRELVARIRAI 114
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
141-252 3.50e-10

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: 56.66  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 141 RSLMRNILTELVSNAVK-YTLHGKIGIHAAknisDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEglnrSFEGTGLG 219
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQaMEGRGRITIRTW----AHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKP----VGEGTGLG 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1085292533 220 LTLCKKYVELLNGKIYVESEVGAGSTFIAEIPV 252
Cdd:cd16943    73 LSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
144-251 5.41e-10

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: 56.44  E-value: 5.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 144 MRNILTELVSNAVKYTLHG-KIGIHAAKNISDGHetlvIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTL 222
Cdd:cd16952     1 LRSAFSNLVSNAVKYTPPSdTITVRWSQEESGAR----LSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAI 76
                          90       100
                  ....*....|....*....|....*....
gi 1085292533 223 CKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:cd16952    77 VKHVMSRHDARLLIASELGKGSRFTCLFP 105
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
288-402 7.03e-10

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 58.19  E-value: 7.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 288 IDDDSLSLTVVERYL-SNEYSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGkySKTPVVAVTAY- 365
Cdd:COG4566     5 VDDDEAVRDSLAFLLeSAGLRVETFASAEAFLAALDPDRPGCLLLDVRMP-GMSGLELQEELAARG--SPLPVIFLTGHg 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085292533 366 -------ALKsdeelilsKGFSHYISKPFNKKDILNLLRKIFAE 402
Cdd:COG4566    82 dvpmavrAMK--------AGAVDFLEKPFDDQALLDAVRRALAR 117
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
100-255 1.05e-09

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 59.92  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 100 EPVDVEELIDAVYNSFLDDAAKKGIAVEKTVTGFTTPIysDRSL---MrnILTELVSNAVKY----TLHGKIGIHaaknI 172
Cdd:COG3920   357 EGVDLRDYLRELLEPLRDSYGGRGIRIELDGPDVELPA--DAAVplgL--ILNELVTNALKHaflsGEGGRIRVS----W 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 173 SDGHETLVIRVTDTGIGIAKETQEIiwnefrqaseglnrsfEGTGLGLTLCKKYVELLNGKIYVESEvgAGSTFIAEIPV 252
Cdd:COG3920   429 RREDGRLRLTVSDNGVGLPEDVDPP----------------ARKGLGLRLIRALVRQLGGTLELDRP--EGTRVRITFPL 490

                  ...
gi 1085292533 253 TSV 255
Cdd:COG3920   491 AEL 493
PRK13557 PRK13557
histidine kinase; Provisional
180-399 1.14e-09

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 60.07  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 180 VIRVTDTGIGIAKETQEIIWNEF-RQASEGlnrsfEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVTSVLQE 258
Cdd:PRK13557  326 SIAVTDTGSGMPPEILARVMDPFfTTKEEG-----KGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAEN 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 259 LDEKLAVSYADETislanvgasANKKILYIDDD----SLSLTVVERYlsnEYSVECVSGAPQFLEKLN-EAAFDCILMDI 333
Cdd:PRK13557  401 PEQEPKARAIDRG---------GTETILIVDDRpdvaELARMILEDF---GYRTLVASNGREALEILDsHPEVDLLFTDL 468
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085292533 334 NIGREISGIDLINEVKEigKYSKTPVVAVTAYALKSDEELILSKGFSHYISKPFNKKDilnLLRKI 399
Cdd:PRK13557  469 IMPGGMNGVMLAREARR--RQPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAE---LARRV 529
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
147-251 2.37e-09

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 54.32  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 147 ILTELVSNAVKYTLHGKI--GIHAAKNISDGHETLVIRVTDTGIGIAKETQEIIWNEF-RQASEGLnrsfegtGLGLTLC 223
Cdd:cd16920     4 VLINLVRNGIEAMSEGGCerRELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFyTTKSEGL-------GMGLSIC 76
                          90       100
                  ....*....|....*....|....*...
gi 1085292533 224 KKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:cd16920    77 RSIIEAHGGRLSVESPAGGGATFQFTLP 104
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
284-388 3.14e-09

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: 54.37  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSN--EYSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKYSKTPVVA 361
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSagYLEVVSFTDPREALAWCRENPPDLILLDYMMP-GMDGLEFIRRLRALPGLEDVPIVM 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1085292533 362 VTAYalkSDEEL---ILSKGFSHYISKPFN 388
Cdd:cd17551    81 ITAD---TDREVrlrALEAGATDFLTKPFD 107
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
96-254 6.95e-09

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 56.17  E-value: 6.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  96 ELYYEPVDVEELIDAVyNSFLDDAAKK-GIAVEKTVTGFTTPIYSD--RSLMRnILTELVSNAVKytlhgkigiHA-AKN 171
Cdd:COG4585   114 GLRPPALDDLGLAAAL-EELAERLLRAaGIRVELDVDGDPDRLPPEveLALYR-IVQEALTNALK---------HAgATR 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 172 I----SDGHETLVIRVTDTGIGIAKETQEiiwnefrqaseglnrsfeGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFI 247
Cdd:COG4585   183 VtvtlEVDDGELTLTVRDDGVGFDPEAAP------------------GGGLGLRGMRERAEALGGTLTIGSAPGGGTRVR 244

                  ....*..
gi 1085292533 248 AEIPVTS 254
Cdd:COG4585   245 ATLPLAA 251
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
285-386 7.65e-09

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 52.77  E-value: 7.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEIGKYSKTPVVAVT 363
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQgFTVIAASNGLEALDLLNQYIPDLIISDIIMPG-VDGYSLLGKLRKNADFDTIPVIFLT 79
                          90       100
                  ....*....|....*....|...
gi 1085292533 364 AYALKSDEELILSKGFSHYISKP 386
Cdd:cd19927    80 AKGMTSDRIKGYNAGCDGYLSKP 102
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
285-401 1.40e-08

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: 52.51  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNEYSVECVSGA---PQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEIgkYSKTPVVA 361
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPDIEVVGEAadgEEALALLRELRPDVVLMDLSMPG-MDGIEALRRLRRR--YPDLKVIV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085292533 362 VTAYalkSDEELI---LSKGFSHYISKPFNKKDILNLLRKIFA 401
Cdd:cd17535    78 LTAH---DDPEYVlraLKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
285-387 1.41e-08

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 52.13  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGKYSKTPVVAVT 363
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAgYRVLVATDGQQALQRAQAEPPDLILLDVMMP-GMDGFEVCRRLKADPATRHIPVIFLT 79
                          90       100
                  ....*....|....*....|....
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPF 387
Cdd:cd19920    80 ALTDTEDKVKGFELGAVDYITKPF 103
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
283-399 2.22e-08

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 51.84  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEigKYSKTPVVA 361
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEgYEVVTAGNGEEALEKLESEDPDLVILDIKM-PGMDGLETLRKIRE--KKPDLPVII 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1085292533 362 VTAYA-LKSDEELILSkgfSHYISKPFNKKDILNLLRKI 399
Cdd:cd17554    78 CTAYSeYKSDFSSWAA---DAYVVKSSDLTELKETIKRL 113
PRK13856 PRK13856
two-component response regulator VirG; Provisional
283-397 5.73e-08

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 53.28  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLS-NEYSVECVSGAPQFLEKLNEAAFDCILMDINIGREiSGIDLineVKEIGKYSKTPVVA 361
Cdd:PRK13856    2 KHVLVIDDDVAMRHLIVEYLTiHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGRE-DGLEI---VRSLATKSDVPIII 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1085292533 362 VTAYAL-KSDEELILSKGFSHYISKPFNKKDILNLLR 397
Cdd:PRK13856   78 ISGDRLeEADKVVALELGATDFIAKPFGTREFLARIR 114
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
144-251 6.94e-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: 50.08  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 144 MRNILTELVSNAVKYTLHGKIgIHAAKNISDghETLVIRVTDTGIGIAKETQEIIWNEFRQASEglNRSFEGTGLGLTLC 223
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPENTR-IYITSFLTD--DVVNIMFKNPSSHPLDFKLEKLFERFYRGDN--SRNTEGAGLGLSIA 75
                          90       100
                  ....*....|....*....|....*...
gi 1085292533 224 KKYVELLNGKIYVESEvGAGSTFIAEIP 251
Cdd:cd16923    76 KAIIELHGGSASAEYD-DNHDLFKVRLP 102
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
283-396 7.09e-08

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 50.52  E-value: 7.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGREiSGIDLINEVKEIgkYSKTPVVA 361
Cdd:cd17563     1 KSLLLVDDDEVFAERLARALERRgFEVETAHSVEEALALAREEKPDYAVLDLRLGGD-SGLDLIPPLRAL--QPDARIVV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085292533 362 VTAY--------ALKSdeelilskGFSHYISKPFNKKDILNLL 396
Cdd:cd17563    78 LTGYasiataveAIKL--------GADDYLAKPADADEILAAL 112
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
283-399 7.19e-08

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 50.38  E-value: 7.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSV-ECVSGApQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEIGKYSKTPVV 360
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAgYEVvEAADGR-DALSKAQSKKFDLIITDQNMPN-MDGIELIKELRKLPAYKFTPIL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1085292533 361 AVTAYAlkSDEELILSK--GFSHYISKPFNKKDILNLLRKI 399
Cdd:cd17562    79 MLTTES--SDEKKQEGKaaGATGWLVKPFDPEQLLEVVKKV 117
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
284-398 7.93e-08

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 50.14  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYL-SNEYSVECVSGAPQFLEKLNEAAFDCILMDINIGREiSGIDLInevKEIGKYSKTPVVAV 362
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLrERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQE-SGLDLL---RTIRARSDVPIIII 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1085292533 363 TAYAL-KSDEELILSKGFSHYISKPFNKKDILNLLRK 398
Cdd:cd17594    77 SGDRRdEIDRVVGLELGADDYLAKPFGLRELLARVRA 113
PRK10610 PRK10610
chemotaxis protein CheY;
279-400 9.80e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 50.36  E-value: 9.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 279 ASANKKILYIDDDSLSLTVVERYLSNE--YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSK 356
Cdd:PRK10610    2 ADKELKFLVVDDFSTMRRIVRNLLKELgfNNVEEAEDGVDALNKLQAGGFGFVISDWNM-PNMDGLELLKTIRADGAMSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085292533 357 TPVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIF 400
Cdd:PRK10610   81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIF 124
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
283-334 1.35e-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: 47.95  E-value: 1.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1085292533  283 KKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDIN 334
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIM 53
PRK10604 PRK10604
sensor protein RstB; Provisional
35-252 1.90e-07

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 52.68  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  35 NMSHELRTPFVGIIGFAEIIKEITTDSEIAnmascimdsSKRMTNTLNNILD----LSKLELGNLELYYEPVDVEELIDA 110
Cdd:PRK10604  218 GIAHELRTPLVRLRYRLEMSDNLSAAESQA---------LNRDIGQLEALIEelltYARLDRPQNELHLSEPDLPAWLST 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 111 VYNSFLDDAAKKGIAVEKTVTGftTPIYSDRSLMRNILTELVSNAVKYTlHGKIGIHAAknISDGHETLviRVTDTGIGI 190
Cdd:PRK10604  289 HLADIQAVTPEKTVRLDTPHQG--DYGALDMRLMERVLDNLLNNALRYA-HSRVRVSLL--LDGNQACL--IVEDDGPGI 361
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085292533 191 AKETQEIIWNEFRQASEGLNRSFEGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPV 252
Cdd:PRK10604  362 PPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPV 423
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
285-393 2.02e-07

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 49.31  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGREiSGIDLINEVKEigkYSKTPVVAVT 363
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEgYDVSEAGDGEEMRQILARQDIDLVLLDINLPGK-DGLSLTRELRE---QSEVGIILVT 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFNKKDIL 393
Cdd:cd17619    79 GRDDEVDRIVGLEIGADDYVTKPFNPRELL 108
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
286-393 2.08e-07

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


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 49.19  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 286 LYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSKTPVVAVTA 364
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEgYEVVTAYDGEEALKRAKDEKPDLIILDLML-PGIDGLEVCRILRSDPKTSSIPIIMLTA 79
                          90       100
                  ....*....|....*....|....*....
gi 1085292533 365 YALKSDEELILSKGFSHYISKPFNKKDIL 393
Cdd:cd19937    80 KGEEFDKVLGLELGADDYITKPFSPRELL 108
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
285-398 2.56e-07

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 48.74  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYL--SNEYSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGkySKTPVVAV 362
Cdd:cd17537     2 TVYVVDDDEAVRDSLAFLlrSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRM-PGMSGLELQDELLARG--SNIPIIFI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085292533 363 TAY--------ALKsdeelilsKGFSHYISKPFNKKDILNLLRK 398
Cdd:cd17537    79 TGHgdvpmaveAMK--------AGAVDFLEKPFRDQVLLDAIEQ 114
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
137-245 3.15e-07

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 50.03  E-value: 3.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 137 IYSDRSLMRNILTELVSNAVKYT--LHGKIGIHAAK---NISDGHETLVIRVTDTGIGIAKETQEIIWN----------- 200
Cdd:cd16929    37 FPYVPSHLYYILFELLKNAMRATveSHGDDSDDLPPikvTVAKGDEDLTIKISDRGGGIPREDLARLFSymystapqpsl 116
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1085292533 201 -EFRQASEGLNRSF-EGTGLGLTLCKKYVELLNGKIYVESEVGAGST 245
Cdd:cd16929   117 dDFSDLISGTQPSPlAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTD 163
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
284-387 3.90e-07

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: 47.88  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNEYS--VECVSGaPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSKTPVVA 361
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYevLTADSG-QEALALAEEELPDLILLDVMM-PGMDGFEVCRRLKEDPETRHIPVIM 78
                          90       100
                  ....*....|....*....|....*...
gi 1085292533 362 VTayALKSDEELI--LSKGFSHYISKPF 387
Cdd:cd17538    79 IT--ALDDREDRIrgLEAGADDFLSKPI 104
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
179-251 4.58e-07

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: 48.14  E-value: 4.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085292533 179 LVIRVTDTGIGIAKETQEIIWNEFRqASEGLNRsfeGTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:cd16919    48 VCLEVSDTGSGMPAEVLRRAFEPFF-TTKEVGK---GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
289-387 5.30e-07

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 47.99  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 289 DDDSLSLTVVERYLSNEYSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKysKTPVVAVTAYALK 368
Cdd:cd17625     5 DEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIML-PGMDGLEVLKSLREEGI--ETPVLLLTALDAV 81
                          90
                  ....*....|....*....
gi 1085292533 369 SDEELILSKGFSHYISKPF 387
Cdd:cd17625    82 EDRVKGLDLGADDYLPKPF 100
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
284-397 6.95e-07

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: 49.18  E-value: 6.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNE-YSV-ECVSGAPQFLEKLNEAAFDCILMDInigrEISGIDLINEVKEIGKYSKTPVVA 361
Cdd:COG3707     5 RVLVVDDEPLRRADLREGLREAgYEVvAEAADGEDAVELVRELKPDLVIVDI----DMPDRDGLEAARQISEERPAPVIL 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1085292533 362 VTAYalkSDEELI---LSKGFSHYISKPFNKKDILNLLR 397
Cdd:COG3707    81 LTAY---SDPELIeraLEAGVSAYLVKPLDPEDLLPALE 116
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
285-387 1.18e-06

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 46.57  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSL-TVVERYLSNEYSVECVSGAPQFLEKLNE-AAFDCILMDINIGREISGIDLINEVKEIgkYSKTPVVAV 362
Cdd:cd18161     1 VLVVEDDPDVRrLTAEVLEDLGYTVLEAASGDEALDLLESgPDIDLLVTDVIMPGGMNGSQLAEEARRR--RPDLKVLLT 78
                          90       100
                  ....*....|....*....|....*
gi 1085292533 363 TAYALKSDEELILSKGFShYISKPF 387
Cdd:cd18161    79 SGYAENAIEGGDLAPGVD-VLSKPF 102
envZ PRK09467
osmolarity sensor protein; Provisional
34-234 1.34e-06

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 50.29  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533  34 ANMSHELRTPFVGIIGFAEIIKEitTDSEIANmaSCIMDsskrmTNTLNNILD--LSKLELGNlELYYEPVDVEELIDAV 111
Cdd:PRK09467  234 AGVSHDLRTPLTRIRLATEMMSE--EDGYLAE--SINKD-----IEECNAIIEqfIDYLRTGQ-EMPMEMADLNALLGEV 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 112 YnsflddAAKKGIAVEKTVTGFTTPIYSD-RSL-MRNILTELVSNAVKYTlHGKIgihaakNISDGHE--TLVIRVTDTG 187
Cdd:PRK09467  304 I------AAESGYEREIETALQPGPIEVPmNPIaIKRALANLVVNAARYG-NGWI------KVSSGTEgkRAWFQVEDDG 370
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1085292533 188 IGIAKETQEIIWNEFRQASEGlnRSFEGTGLGLTLCKKYVELLNGKI 234
Cdd:PRK09467  371 PGIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVKRIVDQHNGKV 415
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
284-397 1.35e-06

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 46.69  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDInigrEISGIDLINEVKEIGKYSKTPVVAV 362
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDL----MLPGIDGIEVCRQIRAESGVPIVML 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1085292533 363 TAYALKSDEELILSKGFSHYISKPFNKKDILNLLR 397
Cdd:cd17626    78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
283-401 1.68e-06

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: 46.63  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDInigR--EISGIDLINEVKEigKYSKTPV 359
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRREgYEVLTATSGEEALEILKQEPVDVVISDQ---RmpGMDGAELLKRVRE--RYPDTVR 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1085292533 360 VAVTAYAlksDEELILS---KGFSH-YISKPFNKKDILNLLRKIFA 401
Cdd:cd17569    76 ILLTGYA---DLDAAIEainEGEIYrFLTKPWDDEELKETIRQALE 118
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
318-399 1.68e-06

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 46.56  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 318 LEKLNEAAFDCILMDINIGReISGIDLINEVKEIgkYSKTPVVAVTAY--------ALKSdeelilskGFSHYISKPFNK 389
Cdd:cd17536    38 LELIEEHKPDIVITDIRMPG-MDGLELIEKIREL--YPDIKIIILSGYddfeyaqkAIRL--------GVVDYLLKPVDE 106
                          90
                  ....*....|
gi 1085292533 390 KDILNLLRKI 399
Cdd:cd17536   107 EELEEALEKA 116
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
144-251 1.73e-06

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: 46.29  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 144 MRNILTELVSNAVKYTlHGKIGIHaakniSDGHET-LVIRVTDTGIGIAKETQEIIWNEFRQASEGlnRSFEGTGLGLTL 222
Cdd:cd16950     1 LKRVLSNLVDNALRYG-GGWVEVS-----SDGEGNrTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAI 72
                          90       100
                  ....*....|....*....|....*....
gi 1085292533 223 CKKYVELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:cd16950    73 VQRISDAHGGSLTLANRAGGGLCARIELP 101
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
285-397 1.95e-06

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 46.22  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEIGkySKTPVVAVT 363
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEgYEVETAVDGAEALRVISGNRPDAVVLDVMMPR-LDGLEVCRRLRAAG--NDLPILVLT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFNKKDILNLLR 397
Cdd:cd17627    78 ARDSVSDRVAGLDAGADDYLVKPFALEELLARVR 111
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
285-398 2.23e-06

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 46.71  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLS-NEYSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGkySKTPVVAVT 363
Cdd:cd17549     1 VLLVDDDADVREALQQTLElAGFRVRAFADAEEALAALSPDFPGVVISDIRMP-GMDGLELLAQIRELD--PDLPVILIT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1085292533 364 AY-----ALKSdeeliLSKGFSHYISKPFNKKDILNLLRK 398
Cdd:cd17549    78 GHgdvpmAVEA-----MRAGAYDFLEKPFDPERLLDVVRR 112
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
140-250 2.60e-06

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: 45.92  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 140 DRSLMRNILTELVSNAVKYTLHGK-IGIHaaknISDGHETLVIRVTDTGIGIAKETQEIIWNEFRQASEGlNRSFEGTGL 218
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGtVSIS----IYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTS-RRSGGHYGM 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1085292533 219 GLTLCKKYVELLNGKIYVESEVGAGSTFIAEI 250
Cdd:cd16975    76 GLYIAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
285-400 2.85e-06

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 45.70  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVER-YLSNEYSVECVSGAPQFLEKLNEAA--FDCILMDINIgreiSGIDLINEVKEIGKYSKTPVVA 361
Cdd:cd17584     1 VLVVDDDPTCLAILKRmLLRCGYQVTTCTDAEEALSMLRENKdeFDLVITDVHM----PDMDGFEFLELIRLEMDLPVIM 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1085292533 362 VTA-YALKSDEELIlSKGFSHYISKPFNKKDILNLLRKIF 400
Cdd:cd17584    77 MSAdGSTSTVMKGL-AHGACDYLLKPVSIEDLKNIWQHVV 115
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
147-252 4.19e-06

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 45.67  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 147 ILTELVSNAVKYT----LHGKIGIHaaknISDGHETLVIRVTDTGIGIaketqeiiwnEFRQASEGLNRSFEGtGLGLTL 222
Cdd:COG2172    38 AVSEAVTNAVRHAyggdPDGPVEVE----LELDPDGLEIEVRDEGPGF----------DPEDLPDPYSTLAEG-GRGLFL 102
                          90       100       110
                  ....*....|....*....|....*....|
gi 1085292533 223 CKKYVEllngKIYVESEVGaGSTFIAEIPV 252
Cdd:COG2172   103 IRRLMD----EVEYESDPG-GTTVRLVKRL 127
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
117-251 4.63e-06

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 46.81  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 117 DDAAKKGIAVEKTVTGFTTPIysDRSLMRNI---LTELVSNAVKYTL-------------HGKIGIHAAKniSDGHetLV 180
Cdd:cd16916    11 DLARELGKQVELVVEGEDTEL--DKSVLEKLadpLTHLLRNAVDHGIeapeerlaagkppEGTITLRAEH--QGNQ--VV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 181 IRVTDTGIGIAKET--QEIIWNEFRQASEGLNRS---------------------FEGTGLGLTLCKKYVELLNGKIYVE 237
Cdd:cd16916    85 IEVSDDGRGIDREKirEKAIERGLITADEAATLSddevlnlifapgfstaeqvtdVSGRGVGMDVVKRSIESLGGTIEVE 164
                         170
                  ....*....|....
gi 1085292533 238 SEVGAGSTFIAEIP 251
Cdd:cd16916   165 SEPGQGTTFTIRLP 178
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
284-398 5.32e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 48.33  E-value: 5.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNEySVECVS--GAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEigKYSKTPVVA 361
Cdd:PRK10923    5 IVWVVDDDSSIRWVLERALAGA-GLTCTTfeNGNEVLEALASKTPDVLLSDIRM-PGMDGLALLKQIKQ--RHPMLPVII 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1085292533 362 VTAYalkSDEELILS---KGFSHYISKPFNKKDILNLLRK 398
Cdd:PRK10923   81 MTAH---SDLDAAVSayqQGAFDYLPKPFDIDEAVALVER 117
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
284-393 7.24e-06

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 44.68  E-value: 7.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgreiSGIDLINEVKEIGKYSKTPVVAV 362
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAgYAPTLLAHGDQVLPYVRHTPPDLILLDLML----PGTDGLTLCREIRRFSDVPIIMV 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1085292533 363 TAYALKSDEELILSKGFSHYISKPFNKKDIL 393
Cdd:cd19938    77 TARVEEIDRLLGLELGADDYICKPYSPREVV 107
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
280-401 1.05e-05

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 47.33  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 280 SANKKILYIDDDSLSLTVVERYLSN-EYSVECVSGAPQFLEKLNEAAFDCILMDINIGrEISGIDLINEVKEIGkySKTP 358
Cdd:PRK10365    3 HDNIDILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMA-EMDGIATLKEIKALN--PAIP 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085292533 359 VVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRKIFA 401
Cdd:PRK10365   80 VLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
283-393 1.10e-05

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 44.16  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKYSKTPVVA 361
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAgFDVVEAEDAESAVNLIVEPRPDLILLDWML-PGGSGIQFIRRLKRDEMTRDIPIIM 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1085292533 362 VTAyalKSDEELI---LSKGFSHYISKPFNKKDIL 393
Cdd:cd17618    80 LTA---RGEEEDKvrgLEAGADDYITKPFSPRELV 111
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
285-393 1.45e-05

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 43.95  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLineVKEIGKYSKTPVVAVT 363
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEgYEVVTAYDGREALEKVEEEQPDLILLDLML-PEKDGLEV---CREVRKTSNVPIIMLT 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFNKKDIL 393
Cdd:cd17614    77 AKDSEVDKVLGLELGADDYVTKPFSNRELL 106
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
285-397 1.47e-05

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 43.81  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDD-SLSLTVVERYLSNEYSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKysKTPVVAVT 363
Cdd:cd19934     1 LLLVEDDaLLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGL-PGMDGLSVLRRWRSEGR--ATPVLILT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFNKKDILNLLR 397
Cdd:cd19934    78 ARDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
ompR PRK09468
osmolarity response regulator; Provisional
282-393 1.57e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 45.74  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 282 NKKILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGREiSGIDLINEVKEIGkySKTPVV 360
Cdd:PRK09468    5 NYKILVVDDDMRLRALLERYLTEQgFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGE-DGLSICRRLRSQN--NPTPII 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1085292533 361 AVTAYALKSDEELILSKGFSHYISKPFNKKDIL 393
Cdd:PRK09468   82 MLTAKGEEVDRIVGLEIGADDYLPKPFNPRELL 114
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
147-251 1.61e-05

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 42.93  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 147 ILTELVSNAVKytlHGKiGIHAAKNISDGHETLVIRVTDTGIGIAKETQEiiwnefrqaseglnrsfEGTGLGLTLCKKY 226
Cdd:cd16917     4 IVQEALTNALK---HAG-ASRVRVTLSYTADELTLTVVDDGVGFDGPAPP-----------------GGGGFGLLGMRER 62
                          90       100
                  ....*....|....*....|....*
gi 1085292533 227 VELLNGKIYVESEVGAGSTFIAEIP 251
Cdd:cd16917    63 AELLGGTLTIGSRPGGGTRVTARLP 87
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
147-250 2.64e-05

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: 42.83  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 147 ILTELVSNA---VKYTLHGKIGIHAakNISDGHetLVIRVTDTGIGIAKETQEIIWNEFRQASE-GlnrsfEGTGLGLTL 222
Cdd:cd16976     4 VLMNLLQNAldaMGKVENPRIRIAA--RRLGGR--LVLVVRDNGPGIAEEHLSRVFDPFFTTKPvG-----KGTGLGLSI 74
                          90       100
                  ....*....|....*....|....*...
gi 1085292533 223 CKKYVELLNGKIYVESEVGAGSTFIAEI 250
Cdd:cd16976    75 SYGIVEEHGGRLSVANEEGAGARFTFDL 102
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
285-387 3.19e-05

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 42.86  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGReISGIDLINEVKeiGKYSKTPVVAVT 363
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPD-GDGLDLLRRWR--RQGQSLPVLILT 77
                          90       100
                  ....*....|....*....|....*...
gi 1085292533 364 AYalKSDEELIlsKGFSH----YISKPF 387
Cdd:cd17624    78 AR--DGVDDRV--AGLDAgaddYLVKPF 101
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
138-247 8.22e-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: 41.49  E-value: 8.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 138 YSDRSLMRNILTELVSNAVKYT--LHGKIGIHAA---KNISDGHET--LVIRVTDTGIGIAKETQEIIWNEFRQASEgln 210
Cdd:cd16932     1 YGDQIRLQQVLADFLLNAVRFTpsPGGWVEIKVSptkKQIGDGVHVihLEFRITHPGQGLPEELVQEMFEENQWTTQ--- 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1085292533 211 rsfegTGLGLTLCKKYVELLNGKI-YV-ESEVgagSTFI 247
Cdd:cd16932    78 -----EGLGLSISRKLVKLMNGDVrYLrEAGR---SYFL 108
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
285-386 8.66e-05

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 41.28  E-value: 8.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEIgkySKTPVVAVT 363
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPR-MDGMELLQRLRQK---STLPVIFLT 76
                          90       100
                  ....*....|....*....|...
gi 1085292533 364 AYALKSDEELILSKGFSHYISKP 386
Cdd:cd19936    77 SKDDEIDEVFGLRMGADDYITKP 99
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
144-252 9.01e-05

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: 41.26  E-value: 9.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 144 MRNILTELVSNAVKYTlHGKIGIhaAKNISDGheTLVIRVTDTGIGIAKETQEIIWNEFRQASEGLNRSFEGTGLGLTLC 223
Cdd:cd16939     1 MARALDNLLRNALRYA-HRTVRI--ALLVSGG--RLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIV 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 1085292533 224 KKYVELLNGKIYV-ESEVGaGSTFIAEIPV 252
Cdd:cd16939    76 HRVALWHGGHVECdDSELG-GACFRLTWPR 104
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
285-364 1.12e-04

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 40.89  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGKysKTPVVAVT 363
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEgYAVDVAYDGEDGLHLALTNEYDLIILDVML-PGLDGLEVLRRLRAAGK--QTPVLMLT 77

                  .
gi 1085292533 364 A 364
Cdd:cd19935    78 A 78
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
285-398 1.57e-04

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 40.94  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVECVSGAPQFLEKLNEAAFDCILMDINIGReISGIDLINEVKEigKYSKTPVV--- 360
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPD-MDGLELLKEIKE--KYPDLPVImis 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1085292533 361 -------AVTAyalksdeeliLSKGFSHYISKPFNKKDILNLLRK 398
Cdd:cd17550    78 ghgtietAVKA----------TKLGAYDFIEKPLSLDRLLLTIER 112
fixJ PRK09390
response regulator FixJ; Provisional
288-402 2.99e-04

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 41.53  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 288 IDDD-----SLS--LTvverylSNEYSVECVSGAPQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGkySKTPVV 360
Cdd:PRK09390    9 VDDDeamrdSLAflLD------SAGFEVRLFESAQAFLDALPGLRFGCVVTDVRM-PGIDGIELLRRLKARG--SPLPVI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1085292533 361 AVTAY--------ALKSdeelilskGFSHYISKPFNKKDILNLLRKIFAE 402
Cdd:PRK09390   80 VMTGHgdvplaveAMKL--------GAVDFIEKPFEDERLIGAIERALAQ 121
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
179-251 3.61e-04

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: 39.69  E-value: 3.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085292533 179 LVIRVTDTGIGIAKETQEIIWNEFRQASEGlnrsfeGTGLGLTLCKKYVELLNGKIYVESEVGAgSTFIAEIP 251
Cdd:cd16918    44 LRVSVIDNGPGIPPDLQDTIFYPMVSGREN------GTGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
151-253 4.24e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 42.31  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 151 LVSNAVKYTL-----HGKIGIHAAKNisdgHETLVIRVTDTGIGIAKETQEIIWNEFRQASeglnrsfEGTGLGLTLCKK 225
Cdd:COG2972   344 LVENAIEHGIepkegGGTIRISIRKE----GDRLVITVEDNGVGMPEEKLEKLLEELSSKG-------EGRGIGLRNVRE 412
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1085292533 226 YVELLNGKIY---VESEVGAGSTFIAEIPVT 253
Cdd:COG2972   413 RLKLYYGEEYgleIESEPGEGTTVTIRIPLE 443
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
285-386 9.70e-04

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: 38.30  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSNE-YSVecvSGAPQFLEKLNEAA---FDCILMDINIgREISGIDLINEVKEIgkySKTPVV 360
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHgYRV---FEAETGQEGLLEAAtrkPDLIILDLGL-PDMDGLEVIRRLREW---SAVPVI 73
                          90       100
                  ....*....|....*....|....*.
gi 1085292533 361 AVTAYALKSDEELILSKGFSHYISKP 386
Cdd:cd17620    74 VLSARDEESDKIAALDAGADDYLTKP 99
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
215-295 1.11e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 40.94  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 215 GTGLGLTLCKKYVELLNGKIYVESEVGAGSTFIAEIPVT-SVLQEL-----DEKLAV--SYADETISL--ANVGASANKK 284
Cdd:COG0643   381 GRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTlAIIDGLlvrvgGETYAIplSSVEEVLRLdpDDIETVEGRE 460
                          90
                  ....*....|.
gi 1085292533 285 ILYIDDDSLSL 295
Cdd:COG0643   461 VIRLRGELLPL 471
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
284-345 1.43e-03

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: 38.33  E-value: 1.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNEYSVECV---SGAPQFLEKLNEAAFDCILMDINIgREISGIDLI 345
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEPDIEVVgeaADGEEALELLEELRPDVVLLDIRM-PGMDGLEAL 66
PRK10766 PRK10766
two-component system response regulator TorR;
283-399 2.26e-03

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 39.25  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNE-YSV-ECVSGApQFLEKLNEAAFDCILMDINIGREiSGIDLINEVKEigkYSKTPVV 360
Cdd:PRK10766    3 YHILVVEDEPVTRARLQGYFEQEgYTVsEAASGA-GMREIMQNQHVDLILLDINLPGE-DGLMLTRELRS---RSTVGII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085292533 361 AVTAYALKSDEELILSKGFSHYISKPFNKKDIL----NLLRKI 399
Cdd:PRK10766   78 LVTGRTDSIDRIVGLEMGADDYVTKPLELRELLvrvkNLLWRI 120
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
140-244 2.33e-03

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 37.52  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 140 DRSLMRNILTELVSNAVKYTLHGKIG-IHAAKNISDGHET-LVIRVTDTGIGIAKETqeiiwnefrqasegLNRSFE--- 214
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGRPSDvGEVRIRVEADQDGrIVLIVCDNGKGFPREM--------------RHRATEpyv 66
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1085292533 215 -----GTGLGLTLCKKYVELLNGKIYVESEVGAGS 244
Cdd:cd16944    67 ttrpkGTGLGLAIVKKIMEEHGGRISLSNREAGGA 101
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
146-251 2.57e-03

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


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 37.03  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 146 NILTELVSNAVKYTLHGKIGIHAAKNIS--DGHEtLVIRVTDTGIGIAKETQeiiwnefrqaSEGLNRSFEgtGLGLTLC 223
Cdd:cd16956     4 LTLQPIVENAVKHGLSGLLDGGRVEITArlDGQH-LLLEVEDNGGGMDPDTL----------ARILIRSSN--GLGLNLV 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1085292533 224 KKYVELLNGKIY---VESEVGAGSTFIAEIP 251
Cdd:cd16956    71 DKRLRQAFGNDYgldIECAPGEGTRITIRLP 101
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
282-388 2.72e-03

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: 37.53  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 282 NKKILYIDDDSLSLTVVERYLSNE--YSVECVSGAPQFLEKLNEAAFDCILMDInIGREISGIDLINEVKEIGKYSKTPV 359
Cdd:cd17552     1 SKRILVIDDEEDIREVVQACLEKLagWEVLTASSGQEGLEKAATEQPDAILLDV-MMPDMDGLATLKKLQANPETQSIPV 79
                          90       100
                  ....*....|....*....|....*....
gi 1085292533 360 VAVTAYALKSDEELILSKGFSHYISKPFN 388
Cdd:cd17552    80 ILLTAKAQPSDRQRFASLGVAGVIAKPFD 108
PRK14084 PRK14084
DNA-binding response regulator;
284-403 3.55e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 38.96  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 284 KILYIDDDSLSLTVVERYLSNEYSVECVSGA---PQFLEKLNEAAFDCILMDINIGREiSGIDLINEVKEIgKYSKTPVV 360
Cdd:PRK14084    2 KALIVDDEPLARNELTYLLNEIGGFEEINEAenvKETLEALLINQYDIIFLDINLMDE-SGIELAAKIQKM-KEPPAIIF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1085292533 361 AvTA---YALKSDEELILSkgfshYISKPFNKKDILNLLRKIFAEK 403
Cdd:PRK14084   80 A-TAhdqFAVKAFELNATD-----YILKPFEQKRIEQAVNKVRATK 119
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
318-399 3.83e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 38.55  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 318 LEKLNEAAFDCILMDINIGREiSGIDLINEVKEIGKYSKTPVVAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLR 397
Cdd:PRK10161   39 VNQLNEPWPDLILLDWMLPGG-SGIQFIKHLKRESMTRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117

                  ..
gi 1085292533 398 KI 399
Cdd:PRK10161  118 AV 119
glnL PRK11073
nitrogen regulation protein NR(II);
159-238 3.84e-03

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 38.91  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 159 TLHGKIGIHAAKnisdghetlvIRVTDTGIGIAKETQEIIWNEFRQASEGlnrsfeGTGLGLTLCKKYVELLNGKIYVES 238
Cdd:PRK11073  271 TLHGERYRLAAR----------IDIEDNGPGIPPHLQDTLFYPMVSGREG------GTGLGLSIARNLIDQHSGKIEFTS 334
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
283-398 4.90e-03

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: 36.75  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 283 KKILYIDDDSLSLTVVERYLSNEYSVE---CVSGApQFLEKLNEAAFDCILMDINIgREISGIDLINEVKEIGkySKTPV 359
Cdd:cd17593     1 MKVLICDDSSMARKQLARALPADWDVEitfAENGE-EALEILREGRIDVLFLDLTM-PVMDGYEVLEALPVEQ--LETKV 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1085292533 360 VAVTAYALKSDEELILSKGFSHYISKPFNKKDILNLLRK 398
Cdd:cd17593    77 IVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEE 115
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
147-228 5.02e-03

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 36.09  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 147 ILTELVSNAVKYT--LHGKIGIHAAknISDGHETLVIRVTDTGIGIAketqeiiwneFRQASEGLNRSFEGtGLGLTLCK 224
Cdd:cd16936     4 AVSEAVTNAVRHAyrHDGPGPVRLE--LDLDPDRLRVEVTDSGPGFD----------PLRPADPDAGLREG-GRGLALIR 70

                  ....
gi 1085292533 225 KYVE 228
Cdd:cd16936    71 ALMD 74
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
285-399 6.37e-03

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 36.11  E-value: 6.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085292533 285 ILYIDDDSLSLTVVERYLSN-EYSVECVSGAPQFLEKLNEAAFDCILMDINIGREisgiDLINEVKEIGKYSKTPVVAVT 363
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYF----DGFYWCREIRQISNVPIIFIS 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1085292533 364 AYALKSDEELILSKGFSHYISKPFnkkDILNLLRKI 399
Cdd:cd18159    77 SRDDNMDQVMAINMGGDDYITKPF---DLDVLLAKI 109
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
327-388 7.42e-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: 36.07  E-value: 7.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085292533 327 DCILMDINIGREISGIDLINEVKEIGKYsktPVVAVTAYAlksdEELILSKGF--SHYISKPFN 388
Cdd:cd17540    47 DLILADIQLADGSSGIDAVNEILTTHDV---PVIFVTAYP----ERLLTGERPepTFLITKPFD 103
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
326-388 9.92e-03

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 35.48  E-value: 9.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085292533 326 FDCILMDINIGrEISGIDLINEVKEigKYSKTPVVAVTAYALKSDEELILSKGFSHYISKPFN 388
Cdd:cd17573    43 YDLVLVSDKLP-DGNGLSIVSRIKE--KHPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFD 102
 
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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