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Conserved domains on  [gi|1819251900|ref|WP_164962262|]
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MULTISPECIES: response regulator [unclassified Rubrivivax]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMAO_torS super family cl37193
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
477-891 6.47e-88

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]


The actual alignment was detected with superfamily member TIGR02956:

Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 300.93  E-value: 6.47e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 477 ERRRLERELDGHRHHLEMLVASRTAELEAARAQADAASQ--------------AKSAFLANMSHEIRTPLNAILGFTHLM 542
Cdd:TIGR02956 410 DERQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKnhakaraeaeeanrAKSAFLATMSHEIRTPLNGILGTLELL 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 543 RRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQVAERARTKALRLESDVD-DV 621
Cdd:TIGR02956 490 GDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPeQL 569
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 622 PDVLFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRLlareGPWLQLGFTVADTGIGIEAAKLGQLFTAFAQADATmaRR 701
Cdd:TIGR02956 570 PNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL----NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGR--RR 643
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 702 FGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVATACPAVDgeaelrqRHAGARVLLAEDNPVNQE 781
Cdd:TIGR02956 644 SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVI-------DLPPQRVLLVEDNEVNQM 716
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 782 VGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAL-PAHAATPIVAMTANAFGEDRQACL 860
Cdd:TIGR02956 717 VAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYL 796
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1819251900 861 DAGMDDHVAKPVDPAQLYSvllhWLGRQAAG 891
Cdd:TIGR02956 797 AAGFDGFLAKPVVEEQLTA----MIAVILAG 823
PAS COG2202
PAS domain [Signal transduction mechanisms];
363-498 6.85e-33

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 128.22  E-value: 6.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 363 LRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNR 442
Cdd:COG2202    10 ERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNR 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251900 443 RKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVAS 498
Cdd:COG2202    90 RKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVEN 145
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
21-559 2.87e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 54.49  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900   21 LPLRVFLRRLIWLCVGpmlllgaaiafyrvqsSLEQRQQAAERIVARLTLLADQMLESRLAGLMMLAQGVDPSASLDEMR 100
Cdd:COG3321    863 LPTYPFQREDAAAALL----------------AAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAAL 926
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  101 RLGESYARGYGSHVLLVDADGRVAMNSRLPQDVEQPPLPRPAALDAAQAALREGRPVVGNLFVGPIAGVPIVSVAVP-LP 179
Cdd:COG3321    927 AALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALAlLA 1006
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  180 PEPGRSPRLLLSTIEASQFQPLLERLLLPPGWSLELRDAAGQAVARRGEPIVGEDGRLRSAALERASWTAVVRIPPQVLH 259
Cdd:COG3321   1007 AAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALAL 1086
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  260 DAVAAEALPLVAGVLGATLIGVLGGTIAGRRLGRDVASLAAPAGTPEAQSGVAEIAAVRRQLDDAAQRRRLSEDALRRSQ 339
Cdd:COG3321   1087 AAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAA 1166
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  340 LQTQLSMDEAVSARARAEAAAASLRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPA 419
Cdd:COG3321   1167 LLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVA 1246
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  420 DTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVASR 499
Cdd:COG3321   1247 ALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALL 1326
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  500 TAELEAARAQADAASQAKSAFLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARVD 559
Cdd:COG3321   1327 AAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
477-891 6.47e-88

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: 300.93  E-value: 6.47e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 477 ERRRLERELDGHRHHLEMLVASRTAELEAARAQADAASQ--------------AKSAFLANMSHEIRTPLNAILGFTHLM 542
Cdd:TIGR02956 410 DERQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKnhakaraeaeeanrAKSAFLATMSHEIRTPLNGILGTLELL 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 543 RRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQVAERARTKALRLESDVD-DV 621
Cdd:TIGR02956 490 GDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPeQL 569
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 622 PDVLFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRLlareGPWLQLGFTVADTGIGIEAAKLGQLFTAFAQADATmaRR 701
Cdd:TIGR02956 570 PNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL----NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGR--RR 643
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 702 FGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVATACPAVDgeaelrqRHAGARVLLAEDNPVNQE 781
Cdd:TIGR02956 644 SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVI-------DLPPQRVLLVEDNEVNQM 716
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 782 VGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAL-PAHAATPIVAMTANAFGEDRQACL 860
Cdd:TIGR02956 717 VAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYL 796
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1819251900 861 DAGMDDHVAKPVDPAQLYSvllhWLGRQAAG 891
Cdd:TIGR02956 797 AAGFDGFLAKPVVEEQLTA----MIAVILAG 823
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
517-884 9.94e-86

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 294.06  E-value: 9.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLM--------RRDAPDavTAERlarvdgAAQHLLAVLNDILDLSKIEAGRLELHEH 588
Cdd:PRK11107  293 KSEFLANMSHELRTPLNGVIGFTRQTlktpltptQRDYLQ--TIER------SANNLLAIINDILDFSKLEAGKLVLENI 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 589 DFSLRELVSRCIEQVAERARTKALRLESDVD-DVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRLLAREGPWLQ 667
Cdd:PRK11107  365 PFSLRETLDEVVTLLAHSAHEKGLELTLNIDpDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQ 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 668 LGFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGE-- 745
Cdd:PRK11107  445 LEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPnp 524
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900     --------------------------------------------------------------------------------
Cdd:PRK11107  525 iidglptdclagkrllyvepnsaaaqatldilsetplevtysptlsqlpeahydilllglpvtfrepltmlherlakaks 604
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 746 ----TVVATACPAVDGEAELRQRHAGA-------------------------------------RVLLAEDNPVNQEVGR 784
Cdd:PRK11107  605 mtdfLILALPCHEQVLAEQLKQDGADAclskplshtrllpallepchhkqppllpptdesrlplTVMAVDDNPANLKLIG 684
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 785 ELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMTANAFGEDRQACLDAGM 864
Cdd:PRK11107  685 ALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGM 764
                         490       500
                  ....*....|....*....|
gi 1819251900 865 DDHVAKPVDPAQLYSVLLHW 884
Cdd:PRK11107  765 DDYLAKPIDEAMLKQVLLRY 784
hybrid_HK_HrmK NF038297
hybrid histidine kinase/response regulator HrmK; HrmK (hormogonium hybrid histidine kinase) is ...
517-873 7.01e-73

hybrid histidine kinase/response regulator HrmK; HrmK (hormogonium hybrid histidine kinase) is a regulator found in heterocyst-forming Cyanobacteria. It affects the formation of hormogonia, motility-conferring filaments produced only by heterocyst-forming cyanobacteria.


Pssm-ID: 468459 [Multi-domain]  Cd Length: 606  Bit Score: 251.38  E-value: 7.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLMRRDAPDAvTAER----LARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSL 592
Cdd:NF038297  234 KNQFLANTSHEIRTPLSSIIGFTHLLLAQGYDP-TRERhqeyLNIIQSSGKHLLALINDILDLSKIEANQLEVQWETVDV 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 593 RELVSRCIEQVAERARTKALRLESDVDdvPDV--LFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRllaREGPWLQlgF 670
Cdd:NF038297  313 PELCRNVLALVKEKAANKGLKLRLEID--PDVttLVADSLRLKQMLLNLLFNALKFTNTGTVGLQVK---SQGSFVH--F 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 671 TVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVAT 750
Cdd:NF038297  386 TVWDTGTGISKENQAELFQPYFQIANSVVSREEGTGLGLAVTRKLAEIHGGWVEVESEVNQGSRFTIVLPLKPEGEVLEA 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 751 ACPAVDGEAELRQRHA-------GARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPG 823
Cdd:NF038297  466 EREVEEEKETSSSPLPitpstssSPDILLVEDDLPNAELMQIYLEKLGYQVTWVKNAAEMWEALSQQEPAVILMDIYLPD 545
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1819251900 824 VDGLEATRRIRALPAHAATPIVAMTANAFGEDRQACLDAGMDDHVAKPVD 873
Cdd:NF038297  546 GNGLNLVQQLRENPQYQNIPIIAQTAMAMKGDRETCLAAGVNDYISKPID 595
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
442-742 3.13e-68

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 230.18  E-value: 3.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 442 RRKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVASRTAELEAARAQADAASQAKSAFL 521
Cdd:COG0642    35 LLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 522 ANMSHEIRTPLNAILGFTHLMRRDAPDAVtAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIE 601
Cdd:COG0642   115 ANVSHELRTPLTAIRGYLELLLEELDEEQ-REYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVE 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 602 QVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGvSLQVRLLAREGpwlQLGFTVADTGIGIEA 681
Cdd:COG0642   194 LFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGG-TVTVSVRREGD---RVRISVEDTGPGIPP 269
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819251900 682 AKLGQLFTAFAQADAtmARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLR 742
Cdd:COG0642   270 EDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
632-741 7.92e-49

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: 168.05  E-value: 7.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFTEQGGVSLQVRLLAREGPWLQLGFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAI 711
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 712 TRRLALLMGGDVAVDSRVGEGSRFSFSVRL 741
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PAS COG2202
PAS domain [Signal transduction mechanisms];
363-498 6.85e-33

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 128.22  E-value: 6.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 363 LRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNR 442
Cdd:COG2202    10 ERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNR 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251900 443 RKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVAS 498
Cdd:COG2202    90 RKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVEN 145
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
627-742 1.88e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 115.82  E-value: 1.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  627 GDSMRIAQALLNLLSNAVKFTEQGG-VSLQVRllaREGPWLQlgFTVADTGIGIEAAKLGQLFTAFAQADATmARRFGGT 705
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGrITVTLE---RDGDHVE--ITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1819251900  706 GLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLR 742
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
378-738 4.20e-28

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: 120.63  E-value: 4.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 378 VI-TDPEARIQYVNQAFLDQTGYSREEILG-STPE--RLRSARTpadtvaslWRTLQagETWRGEFVNRRKDGSEYVESA 453
Cdd:NF033092  271 VIaTDRRGRVILINDPALEMLNVSRETVLGqSILDvlGLEEEYT--------LRDLL--EEQDSLLLDFSTEEEPLILRA 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 454 VVTPLRSPEGRVTHFVAVSEDITERRRLEREldghrhhlemlvasrtaeleaaraqadaasqaKSAFLANMSHEIRTPLN 533
Cdd:NF033092  341 NFSVIQRESGFINGLIAVLHDVTEQEKIEQE--------------------------------RREFVANVSHELRTPLT 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 534 AILGFThlmrrdapdavtaERLArvDGA------AQHLLAV-----------LNDILDLSKIEAGRLELHEHDFSLRELV 596
Cdd:NF033092  389 TMRSYL-------------EALA--DGAwkdpelAPRFLGVtqnetermirlVNDLLQLSRMDSKDYKLNKEWVNFNEFF 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 597 SRCIEQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGpwlQLGFTVADTG 676
Cdd:NF033092  454 NYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGT-ITFRLLETHN---RIIISISDQG 529
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819251900 677 IGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFS 738
Cdd:NF033092  530 LGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFT 591
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
627-742 2.43e-26

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: 103.99  E-value: 2.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 627 GDSMRIAQALLNLLSNAVKFTEQGGvslQVRLLAREGPWLQlgFTVADTGIGIEAAKLGQLFTAFAQADAtmaRRFGGTG 706
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAG---EITVTLSEGGELT--LTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTG 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819251900 707 LGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLR 742
Cdd:pfam02518  73 LGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
369-498 5.06e-24

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


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 106.91  E-value: 5.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 369 AVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKDGSE 448
Cdd:TIGR02938   9 TVDQAPLAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGEL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1819251900 449 YVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVAS 498
Cdd:TIGR02938  89 YLAELTVAPVLNEAGETTHFLGMHRDITELHRLEQVVANQKLLIESVVDA 138
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
520-756 3.45e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 101.26  E-value: 3.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 520 FLANMSHEIRTPLNAILGFTHLM--RRDAPDAVTA-------ERLARVDgaaqhllAVLNDILDLSKIEAGRLELHEHDF 590
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATArsaellhTELDRFE-------SLLSDLLEISRFDAGAAELDVEPV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 591 SLRELVSRCIEQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVslQVRLLAREGpwlQLGF 670
Cdd:NF040691  347 DLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPV--VVTVAQDDT---AVAV 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 671 TVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVAT 750
Cdd:NF040691  422 TVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAGDRLTTS 501

                  ....*.
gi 1819251900 751 ACPAVD 756
Cdd:NF040691  502 PLPLVP 507
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
517-721 4.29e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 94.51  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLMrRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELV 596
Cdd:NF012163  240 RRDFMADISHELRTPLAVLRAELEAI-QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 597 SRCIEQVAERARTKALRLESDVDDVPdVLFGDSMRIAQALLNLLSNAVKFTEQGGvslQVRLLAREGPwLQLGFTVADTG 676
Cdd:NF012163  319 EVEGGAFRERFASAGLELEVSLPDSS-LVFGDRDRLMQLFNNLLENSLRYTDSGG---SLHISASQRP-KEVTLTVADSA 393
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1819251900 677 IGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGG 721
Cdd:NF012163  394 PGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGG 438
PRK13558 PRK13558
bacterio-opsin activator; Provisional
380-497 3.53e-19

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 92.59  E-value: 3.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 380 TDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVTPLR 459
Cdd:PRK13558  167 TLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIR 246
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1819251900 460 SPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVA 497
Cdd:PRK13558  247 DEDGTVTHYVGFQTDVTERKEAELALQRERRKLQRLLE 284
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
385-477 1.24e-15

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 72.88  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 385 RIQYVNQAFLDQTGYSREEILGSTPERLRsarTPADTVASLWRTLQAGET-WRGEFVNRRKDGSEYVESAVVTPLRSPEG 463
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDLF---AEPEDSERLREALREGKAvREFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
                          90
                  ....*....|....
gi 1819251900 464 RVTHFVAVSEDITE 477
Cdd:pfam13426  80 ELVGIIAILRDITE 93
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
377-475 5.38e-11

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 59.95  E-value: 5.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 377 IVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVT 456
Cdd:cd00130     5 VIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84
                          90
                  ....*....|....*....
gi 1819251900 457 PLRSPEGRVTHFVAVSEDI 475
Cdd:cd00130    85 PIRDEGGEVIGLLGVVRDI 103
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
21-559 2.87e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 54.49  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900   21 LPLRVFLRRLIWLCVGpmlllgaaiafyrvqsSLEQRQQAAERIVARLTLLADQMLESRLAGLMMLAQGVDPSASLDEMR 100
Cdd:COG3321    863 LPTYPFQREDAAAALL----------------AAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAAL 926
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  101 RLGESYARGYGSHVLLVDADGRVAMNSRLPQDVEQPPLPRPAALDAAQAALREGRPVVGNLFVGPIAGVPIVSVAVP-LP 179
Cdd:COG3321    927 AALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALAlLA 1006
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  180 PEPGRSPRLLLSTIEASQFQPLLERLLLPPGWSLELRDAAGQAVARRGEPIVGEDGRLRSAALERASWTAVVRIPPQVLH 259
Cdd:COG3321   1007 AAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALAL 1086
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  260 DAVAAEALPLVAGVLGATLIGVLGGTIAGRRLGRDVASLAAPAGTPEAQSGVAEIAAVRRQLDDAAQRRRLSEDALRRSQ 339
Cdd:COG3321   1087 AAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAA 1166
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  340 LQTQLSMDEAVSARARAEAAAASLRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPA 419
Cdd:COG3321   1167 LLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVA 1246
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  420 DTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVASR 499
Cdd:COG3321   1247 ALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALL 1326
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  500 TAELEAARAQADAASQAKSAFLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARVD 559
Cdd:COG3321   1327 AAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
364-408 1.07e-06

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 46.62  E-value: 1.07e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1819251900  364 RELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGST 408
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
72-178 4.02e-03

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 38.31  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  72 ADQMLESrlAGLMMLAQGVDPSASLDEMRRLGESYARGYG--SHVLLVDADGRVAMNSrlPQDVEQPPLPRPAALDAAQA 149
Cdd:cd18773     4 ADLLLRS--LASALEALAALGSADREELQALLRRLLERNPeiSGIYVVDADGRVVASS--DRDPGGGDDDDDRDRFWYQA 79
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 150 ALREGRPVVGNLFVGPIAGVPIVSVAVPL 178
Cdd:cd18773    80 AKATGKLVISEPYISRVTGKPVITLSRPI 108
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
477-891 6.47e-88

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: 300.93  E-value: 6.47e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 477 ERRRLERELDGHRHHLEMLVASRTAELEAARAQADAASQ--------------AKSAFLANMSHEIRTPLNAILGFTHLM 542
Cdd:TIGR02956 410 DERQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKnhakaraeaeeanrAKSAFLATMSHEIRTPLNGILGTLELL 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 543 RRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQVAERARTKALRLESDVD-DV 621
Cdd:TIGR02956 490 GDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPeQL 569
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 622 PDVLFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRLlareGPWLQLGFTVADTGIGIEAAKLGQLFTAFAQADATmaRR 701
Cdd:TIGR02956 570 PNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL----NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGR--RR 643
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 702 FGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVATACPAVDgeaelrqRHAGARVLLAEDNPVNQE 781
Cdd:TIGR02956 644 SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVI-------DLPPQRVLLVEDNEVNQM 716
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 782 VGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAL-PAHAATPIVAMTANAFGEDRQACL 860
Cdd:TIGR02956 717 VAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYL 796
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1819251900 861 DAGMDDHVAKPVDPAQLYSvllhWLGRQAAG 891
Cdd:TIGR02956 797 AAGFDGFLAKPVVEEQLTA----MIAVILAG 823
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
517-884 9.94e-86

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 294.06  E-value: 9.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLM--------RRDAPDavTAERlarvdgAAQHLLAVLNDILDLSKIEAGRLELHEH 588
Cdd:PRK11107  293 KSEFLANMSHELRTPLNGVIGFTRQTlktpltptQRDYLQ--TIER------SANNLLAIINDILDFSKLEAGKLVLENI 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 589 DFSLRELVSRCIEQVAERARTKALRLESDVD-DVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRLLAREGPWLQ 667
Cdd:PRK11107  365 PFSLRETLDEVVTLLAHSAHEKGLELTLNIDpDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQ 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 668 LGFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGE-- 745
Cdd:PRK11107  445 LEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPnp 524
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900     --------------------------------------------------------------------------------
Cdd:PRK11107  525 iidglptdclagkrllyvepnsaaaqatldilsetplevtysptlsqlpeahydilllglpvtfrepltmlherlakaks 604
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 746 ----TVVATACPAVDGEAELRQRHAGA-------------------------------------RVLLAEDNPVNQEVGR 784
Cdd:PRK11107  605 mtdfLILALPCHEQVLAEQLKQDGADAclskplshtrllpallepchhkqppllpptdesrlplTVMAVDDNPANLKLIG 684
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 785 ELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMTANAFGEDRQACLDAGM 864
Cdd:PRK11107  685 ALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGM 764
                         490       500
                  ....*....|....*....|
gi 1819251900 865 DDHVAKPVDPAQLYSVLLHW 884
Cdd:PRK11107  765 DDYLAKPIDEAMLKQVLLRY 784
PRK15347 PRK15347
two component system sensor kinase;
492-881 4.88e-75

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 264.20  E-value: 4.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 492 LEMLVASRTAELEAARAQADAASQAKSAFLANMSHEIRTPLNAILGFTHLMRRdapDAVTAERLARVDGAAQ---HLLAV 568
Cdd:PRK15347  373 LENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQN---TPLTAEQMDLADTARQctlSLLAI 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 569 LNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQVAERARTKALRLESDV-DDVPDVLFGDSMRIAQALLNLLSNAVKFT 647
Cdd:PRK15347  450 INNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVgAHVPLYLHLDSLRLRQILVNLLGNAVKFT 529
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 648 EQGGVSLQVRllaREGPwlQLGFTVADTGIGIEAAKLGQLFTAFAQADATMArrfgGTGLGLAITRRLALLMGGDVAVDS 727
Cdd:PRK15347  530 ETGGIRLRVK---RHEQ--QLCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQ----GTGLGLTIASSLAKMMGGELTLFS 600
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 728 RVGEGSRFSFSVRLR-------LGETVVATAC-------------------PAVDGE-----AELRQRHAGA-------- 768
Cdd:PRK15347  601 TPGVGSCFSLVLPLNeyappepLKGELSAPLAlhrqlsawgitcqpghqnpALLDPElaylpGRLYDLLQQIiqgapnep 680
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 -----------RVLLAEDNPVNQE-VGRELLEMaGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAL 836
Cdd:PRK15347  681 vinlplqpwqlQILLVDDVETNRDiIGMMLVEL-GQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDD 759
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1819251900 837 PAH--AATPIVAMTANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:PRK15347  760 PNNldPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL 806
hybrid_HK_HrmK NF038297
hybrid histidine kinase/response regulator HrmK; HrmK (hormogonium hybrid histidine kinase) is ...
517-873 7.01e-73

hybrid histidine kinase/response regulator HrmK; HrmK (hormogonium hybrid histidine kinase) is a regulator found in heterocyst-forming Cyanobacteria. It affects the formation of hormogonia, motility-conferring filaments produced only by heterocyst-forming cyanobacteria.


Pssm-ID: 468459 [Multi-domain]  Cd Length: 606  Bit Score: 251.38  E-value: 7.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLMRRDAPDAvTAER----LARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSL 592
Cdd:NF038297  234 KNQFLANTSHEIRTPLSSIIGFTHLLLAQGYDP-TRERhqeyLNIIQSSGKHLLALINDILDLSKIEANQLEVQWETVDV 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 593 RELVSRCIEQVAERARTKALRLESDVDdvPDV--LFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRllaREGPWLQlgF 670
Cdd:NF038297  313 PELCRNVLALVKEKAANKGLKLRLEID--PDVttLVADSLRLKQMLLNLLFNALKFTNTGTVGLQVK---SQGSFVH--F 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 671 TVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVAT 750
Cdd:NF038297  386 TVWDTGTGISKENQAELFQPYFQIANSVVSREEGTGLGLAVTRKLAEIHGGWVEVESEVNQGSRFTIVLPLKPEGEVLEA 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 751 ACPAVDGEAELRQRHA-------GARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPG 823
Cdd:NF038297  466 EREVEEEKETSSSPLPitpstssSPDILLVEDDLPNAELMQIYLEKLGYQVTWVKNAAEMWEALSQQEPAVILMDIYLPD 545
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1819251900 824 VDGLEATRRIRALPAHAATPIVAMTANAFGEDRQACLDAGMDDHVAKPVD 873
Cdd:NF038297  546 GNGLNLVQQLRENPQYQNIPIIAQTAMAMKGDRETCLAAGVNDYISKPID 595
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
442-742 3.13e-68

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 230.18  E-value: 3.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 442 RRKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVASRTAELEAARAQADAASQAKSAFL 521
Cdd:COG0642    35 LLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 522 ANMSHEIRTPLNAILGFTHLMRRDAPDAVtAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIE 601
Cdd:COG0642   115 ANVSHELRTPLTAIRGYLELLLEELDEEQ-REYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVE 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 602 QVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGvSLQVRLLAREGpwlQLGFTVADTGIGIEA 681
Cdd:COG0642   194 LFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGG-TVTVSVRREGD---RVRISVEDTGPGIPP 269
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819251900 682 AKLGQLFTAFAQADAtmARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLR 742
Cdd:COG0642   270 EDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
390-881 2.83e-65

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 234.06  E-value: 2.83e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 390 NQAFLDQTGYSREEILGSTPERLRS---ARTPADTVASLWRTLQA--GETWRgEFVNRRKdgsEYVESAVVtPLRSPEGR 464
Cdd:PRK11091  181 NRAMELLTGKSEKQLIGLTPKDVYSpeaAEKVIETDEKVFRHNVSltYEQWL-DYPDGRK---ACFELRKV-PFYDRVGK 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 465 VTHFVAVSEDITERRRLERELDGhrhhlemlvASRtaeleaaraqadaasqAKSAFLANMSHEIRTPLNAILGFTHlMRR 544
Cdd:PRK11091  256 RHGLMGFGRDITERKRYQDALEK---------ASR----------------DKTTFISTISHELRTPLNGIVGLSR-ILL 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 545 DAPdaVTAER---LARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQVAERARTKALRLESDVD-D 620
Cdd:PRK11091  310 DTE--LTAEQrkyLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLlP 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 621 VPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRLLAREgpwlQLGFTVADTGIGIEAAKLGQLFTAFAQA-DATMA 699
Cdd:PRK11091  388 LPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGD----MLTFEVEDSGIGIPEDELDKIFAMYYQVkDSHGG 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 700 RRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVAtaCPAVDGEAELRQRHagarVLLAEDNPVN 779
Cdd:PRK11091  464 KPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVE--DAFDEDDMPLPALN----ILLVEDIELN 537
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 780 QEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRA-LPAHAATPIVAMTANAFGeDRQA 858
Cdd:PRK11091  538 VIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRErYPREDLPPLVALTANVLK-DKKE 616
                         490       500
                  ....*....|....*....|...
gi 1819251900 859 CLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:PRK11091  617 YLDAGMDDVLSKPLSVPALTAMI 639
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
517-739 6.51e-63

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 212.07  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLMRRDA--PDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRE 594
Cdd:COG2205    16 KSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLSLELEPVDLAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 595 LVSRCIEQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGG-VSLQVRllaREGPWLQlgFTVA 673
Cdd:COG2205    96 LLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGtITISAR---REGDGVR--ISVS 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251900 674 DTGIGIEAAKLGQLFTAFAQADATmaRRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSV 739
Cdd:COG2205   171 DNGPGIPEEELERIFERFYRGDNS--RGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
335-738 2.58e-62

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 215.96  E-value: 2.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 335 LRRSQLQTQLSMDEAVSARARAEAAAASLRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRS 414
Cdd:COG5002    15 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 415 ARTPADTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLEREldghrhhlem 494
Cdd:COG5002    95 LLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQM---------- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 495 lvasrtaeleaaraqadaasqaKSAFLANMSHEIRTPLNAILGFTHLMRRDA--PDAVTAERLARVDGAAQHLLAVLNDI 572
Cdd:COG5002   165 ----------------------RREFVANVSHELRTPLTSIRGYLELLLDGAadDPEERREYLEIILEEAERLSRLVNDL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 573 LDLSKIEAGRLELHEHDFSLRELVSRCIEQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGG- 651
Cdd:COG5002   223 LDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGt 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 652 VSLQVRllaREGPWLQlgFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGE 731
Cdd:COG5002   303 ITVSLR---EEDDQVR--ISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGK 377

                  ....*..
gi 1819251900 732 GSRFSFS 738
Cdd:COG5002   378 GTTFTIT 384
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
474-892 8.07e-57

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 211.37  E-value: 8.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 474 DITERRRLERELDghrhhlEMLVASRTAEleaaraqadaasQAKSAFLANMSHEIRTPLNAILGF-----THLMRRDAPD 548
Cdd:PRK10841  422 DVSARVKMEESLQ------EMAQAAEQAS------------QSKSMFLATVSHELRTPLYGIIGNldllqTKELPKGVDR 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 549 AVTAerlarVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQVAERARTKALRLESDVD-DVPDVLFG 627
Cdd:PRK10841  484 LVTA-----MNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEpDVPVALNG 558
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 628 DSMRIAQALLNLLSNAVKFTEQGGVSLQVRllaREGPWLQlgFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGL 707
Cdd:PRK10841  559 DPMRLQQVISNLLSNAIKFTDTGCIVLHVR---VDGDYLS--FRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGL 633
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 708 GLAITRRLALLMGGDVAVDSRVGEGSRFS---------------------------------------------FSVRLR 742
Cdd:PRK10841  634 GLAICEKLINMMDGDISVDSEPGMGSQFTiriplygaqypqkkgveglqgkrcwlavrnasleqfletllqrsgIQVQRY 713
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 743 LGETVVAT--------ACPAVDGEA--ELRQRHAGA-------------------------------------------- 768
Cdd:PRK10841  714 EGQEPTPEdvlitddpVQKKWQGRAviTFCRRHIGIpleiapgewvhstatphelpallariyrielesddsanalpstd 793
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 ---------RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaH 839
Cdd:PRK10841  794 kavsdnddmMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQL--G 871
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1819251900 840 AATPIVAMTANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAAGR 892
Cdd:PRK10841  872 LTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVYAERVRKSR 924
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
364-736 6.10e-55

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 194.29  E-value: 6.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 364 RELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPadTVASLWRTLQAGET-WRGEFVNR 442
Cdd:COG3852     7 ELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP--LRELLERALAEGQPvTEREVTLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 443 RKDGSEYVESAVVTPLRSPEGRvTHFVAVSEDITERRRLERELdghrHHLEMLVASRTaeleaaraqadaasqaksaFLA 522
Cdd:COG3852    85 RKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLEREL----RRAEKLAAVGE-------------------LAA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 523 NMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHehdfSLRELVSRCIEQ 602
Cdd:COG3852   141 GLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPV----NLHEVLERVLEL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 603 V-AERARTKALRLESDvDDVPDVLfGDSMRIAQALLNLLSNAVKFTEQGG-------VSLQVRLL-AREGPWLQLgfTVA 673
Cdd:COG3852   217 LrAEAPKNIRIVRDYD-PSLPEVL-GDPDQLIQVLLNLVRNAAEAMPEGGtitirtrVERQVTLGgLRPRLYVRI--EVI 292
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251900 674 DTGIGIEAAKLGQLFTAFaqadatmarrF----GGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFS 736
Cdd:COG3852   293 DNGPGIPEEILDRIFEPF----------FttkeKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFR 349
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
483-885 7.29e-54

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 202.44  E-value: 7.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 483 RELDGHRHHLEMLVASRTAELEA-------ARAQADAASQAKSAFLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAERL 555
Cdd:PRK11466  403 HALNRHREQLAAQVKARTAELQElviehrqARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDL 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 556 ARVDGAAQHLLAVLNDILDLSKIEAG--RLELHEHDFSLRELVSRCIEQVAERARTKALRLESDV-DDVPDVLFGDSMRI 632
Cdd:PRK11466  483 RAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIaDDLPTALMGDPRRI 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 633 AQALLNLLSNAVKFTEQGgvSLQVRLLAREGPWLqlgFTVADTGIGIEAAKLGQLFTAFAQADAtmarRFGGTGLGLAIT 712
Cdd:PRK11466  563 RQVITNLLSNALRFTDEG--SIVLRSRTDGEQWL---VEVEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTIS 633
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 713 RRLALLMGGDVAVDSRVGEGSRFSFSVRLRLgetvvatACPAVDGEAELRQRHAGARVLLAEDNPVNQEVGRELLEMAGL 792
Cdd:PRK11466  634 SRLAQAMGGELSATSTPEVGSCFCLRLPLRV-------ATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGA 706
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 793 CVDVADDG-EAAVACAAAGDYAAILMDMQMPGVDGLEATRRIraLPAHAATPIVAMTANAFGED---RQACLDAGMddhV 868
Cdd:PRK11466  707 QVVAVGNAaQALETLQNSEPFAAALVDFDLPDYDGITLARQL--AQQYPSLVLIGFSAHVIDETlrqRTSSLFRGI---I 781
                         410
                  ....*....|....*..
gi 1819251900 869 AKPVDPAQLYSVLLHWL 885
Cdd:PRK11466  782 PKPVPREVLGQLLAHYL 798
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
364-747 1.39e-49

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: 182.87  E-value: 1.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 364 RELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRR 443
Cdd:COG5809   141 EKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWT 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 444 KDGSEYVESAVVTPLrSPEGRVTHFVAVSEDITERRRLERELDghrhHLEMLvaSRTAELeaaraqadaasqaksafLAN 523
Cdd:COG5809   221 KDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKLEELLR----KSEKL--SVVGEL-----------------AAG 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 524 MSHEIRTPLNAILGFTHLMRRDAPDA------VTAERLARvdgaaqhLLAVLNDILDLSKIEAGRLELhehdFSLRELvs 597
Cdd:COG5809   277 IAHEIRNPLTSLKGFIQLLKDTIDEEqktyldIMLSELDR-------IESIISEFLVLAKPQAIKYEP----KDLNTL-- 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 598 rcIEQVAERARTKAL------RLESDvDDVPDVLfGDSMRIAQALLNLLSNAVKFTEQGG-VSLQVRLLAREgpwlQLGF 670
Cdd:COG5809   344 --IEEVIPLLQPQALlknvqiELELE-DDIPDIL-GDENQLKQVFINLLKNAIEAMPEGGnITIETKAEDDD----KVVI 415
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251900 671 TVADTGIGIEAAKLGQLFTAFAqadatmARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETV 747
Cdd:COG5809   416 SVTDEGCGIPEERLKKLGEPFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQV 486
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
632-741 7.92e-49

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: 168.05  E-value: 7.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFTEQGGVSLQVRLLAREGPWLQLGFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAI 711
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 712 TRRLALLMGGDVAVDSRVGEGSRFSFSVRL 741
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
222-738 8.11e-45

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 169.58  E-value: 8.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 222 AVARRGEPIVGEDGRLRSAALERASWTAVVRIPPQVLHDAVAAEALPLVAGVLGATLIGVLGGTIAGRRLGRDVASLAAP 301
Cdd:COG4251     6 LLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 302 AGTPEAQSGVAEIAAVRRQLDDAAQRRRLSEDALRRSQLQTQLSMDEAVSARARAEAAAASLRELSLAVEQTSSSIVITD 381
Cdd:COG4251    86 LLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 382 PEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVnRRKDGSEYVESAVVTPLRSP 461
Cdd:COG4251   166 LILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGG-LGLLLLLLLLLVLLLLLILL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 462 EGRVTHFVAVSEDITERRRLERELDGHRHHLEMlvasRTAELEaaraqadaasqaksAFLANMSHEIRTPLNAILGFTHL 541
Cdd:COG4251   245 LLLLILVLELLELRLELEELEEELEERTAELER----SNEELE--------------QFAYVASHDLREPLRKISGFSQL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 542 MRRD---APDAVTAERLARVDGAAQHLLAVLNDILDLSKIeaGRLELHEHDFSLRELVSRCIEQVAERARTKALRLEsdV 618
Cdd:COG4251   307 LEEDygdKLDEEGREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIE--V 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 619 DDVPDVlFGDSMRIAQALLNLLSNAVKFTeQGGVSLQVRLLAREGP--WLqlgFTVADTGIGIEAAKLGQLFTAFAQADA 696
Cdd:COG4251   383 GPLPTV-RGDPTLLRQVFQNLISNAIKYS-RPGEPPRIEIGAEREGgeWV---FSVRDNGIGIDPEYAEKIFEIFQRLHS 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1819251900 697 tmARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFS 738
Cdd:COG4251   458 --RDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFT 497
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
503-872 1.50e-43

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 171.46  E-value: 1.50e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  503 LEAARAQADAASQAKSAFLANMSHEIRTPLNAILGFTHLMRRDA---PDAVTAERLARVDGaaQHLLAVLNDILDLSKIE 579
Cdd:PRK09959   698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGlskEQRVEAISLAYATG--QSLLGLIGEILDVDKIE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  580 AGRLELHEHDFSLRELVSRCIEQVAERARTKALRLeSDVDDVPD--VLFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVR 657
Cdd:PRK09959   776 SGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIAL-SCSSTFPDhyLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTS 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  658 LLAREGPWLQLGFTVADTGIGIEAAKLGQLFTAFAQADAtmARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSF 737
Cdd:PRK09959   855 LGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSA--GRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTI 932
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  738 SVRLRLGETVVATACPAvDGEAELRQRHAgarVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILM 817
Cdd:PRK09959   933 TIPVEISQQVATVEAKA-EQPITLPEKLS---ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLIT 1008
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1819251900  818 DMQMPGVDGLEATRRIRAlpAHAATPIVAMTANAFGEDRQACLDAGMDDHVAKPV 872
Cdd:PRK09959  1009 DVNMPNMDGFELTRKLRE--QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPL 1061
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
770-881 1.50e-42

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: 150.31  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALP-AHAATPIVAMT 848
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEgGGRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
764-890 1.32e-38

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: 139.60  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 764 RHAGARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATP 843
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIP 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1819251900 844 IVAMTANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAA 890
Cdd:COG0784    82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
370-736 6.09e-36

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: 141.25  E-value: 6.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 370 VEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGEtwrgefVNRRKDGSEY 449
Cdd:COG5000    96 LENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALERGWQEE------IELTRDGRRT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 450 VeSAVVTPLRSPEgrvthFVAVSEDITERRRLEReldghrhhLEML--VASRtaeleaaraqadaasqaksaflanMSHE 527
Cdd:COG5000   170 L-LVRASPLRDDG-----YVIVFDDITELLRAER--------LAAWgeLARR------------------------IAHE 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 528 IRTPLNAILGFTHLMRRDAPDAVTAER------LARVDGAAQHLLAVLNDILDLSKIEAGRLElhehDFSLRELVSRCIE 601
Cdd:COG5000   212 IKNPLTPIQLSAERLRRKLADKLEEDRedleraLDTIIRQVDRLKRIVDEFLDFARLPEPQLE----PVDLNELLREVLA 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 602 QVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGvslQVRL-LAREGPWLQLgfTVADTGIGIE 680
Cdd:COG5000   288 LYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGG---EIEVsTRREDGRVRI--EVSDNGPGIP 362
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251900 681 AAKLGQLFTAFaqadatMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFS 736
Cdd:COG5000   363 EEVLERIFEPF------FTTKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFT 412
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
467-737 3.03e-33

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: 131.18  E-value: 3.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 467 HFVAVSEDITERRRLEReldghrhhlemlvasrtaeleaaraqadaasqAKSAFLANMSHEIRTPLNAILGFTHLMrRDA 546
Cdd:TIGR02966  96 QKLLVARDVTRLRRLEQ--------------------------------MRRDFVANVSHELRTPLTVLRGYLETL-ADG 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 547 PDAVTAER---LARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQVAERARTKALRLESDVDDVPD 623
Cdd:TIGR02966 143 PDEDPEEWnraLEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFEIDGGVD 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 624 VlFGDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGpwlQLGFTVADTGIGIEAAKLGQLFTAFAQADATMARRFG 703
Cdd:TIGR02966 223 V-LGDEDELRSAFSNLVSNAIKYTPEGGT-ITVRWRRDGG---GAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTG 297
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1819251900 704 GTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSF 737
Cdd:TIGR02966 298 GTGLGLAIVKHVLSRHHARLEIESELGKGSTFSF 331
PAS COG2202
PAS domain [Signal transduction mechanisms];
363-498 6.85e-33

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 128.22  E-value: 6.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 363 LRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNR 442
Cdd:COG2202    10 ERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNR 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251900 443 RKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVAS 498
Cdd:COG2202    90 RKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVEN 145
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
470-738 1.53e-30

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 124.14  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 470 AVSEDITERRRLERELdgHRHHLEMLVASRTA---ELeaaraqadaasqaksafLANMSHEIRTPLNAILGFTHLMRRDA 546
Cdd:COG4191   111 ELERDITELERAEEEL--RELQEQLVQSEKLAalgEL-----------------AAGIAHEINNPLAAILGNAELLRRRL 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 547 PDAVTAER----LARVDGAAQHLLAVLNDILDLSKIEAGRLElhehDFSLRELVSRCIEQVAERARTKALRLESDVDDVP 622
Cdd:COG4191   172 EDEPDPEElreaLERILEGAERAAEIVRSLRAFSRRDEEERE----PVDLNELIDEALELLRPRLKARGIEVELDLPPDL 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 623 DVLFGDSMRIAQALLNLLSNAVK-FTEQGGVSLQVRlLAREGPWLQLgfTVADTGIGIEAAKLGQLFTAFaqadATMARR 701
Cdd:COG4191   248 PPVLGDPGQLEQVLLNLLINAIDaMEEGEGGRITIS-TRREGDYVVI--SVRDNGPGIPPEVLERIFEPF----FTTKPV 320
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1819251900 702 FGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFS 738
Cdd:COG4191   321 GKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTIT 357
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
769-880 1.61e-30

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: 116.10  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMT 848
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQLYSV 880
Cdd:cd17548    81 AYAMKGDREKILEAGCDGYISKPIDTREFLET 112
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
627-742 1.88e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 115.82  E-value: 1.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  627 GDSMRIAQALLNLLSNAVKFTEQGG-VSLQVRllaREGPWLQlgFTVADTGIGIEAAKLGQLFTAFAQADATmARRFGGT 705
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGrITVTLE---RDGDHVE--ITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1819251900  706 GLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLR 742
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
768-881 2.83e-28

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: 111.92  E-value: 2.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAM 847
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFL 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:COG3706    82 TALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
378-738 4.20e-28

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: 120.63  E-value: 4.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 378 VI-TDPEARIQYVNQAFLDQTGYSREEILG-STPE--RLRSARTpadtvaslWRTLQagETWRGEFVNRRKDGSEYVESA 453
Cdd:NF033092  271 VIaTDRRGRVILINDPALEMLNVSRETVLGqSILDvlGLEEEYT--------LRDLL--EEQDSLLLDFSTEEEPLILRA 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 454 VVTPLRSPEGRVTHFVAVSEDITERRRLEREldghrhhlemlvasrtaeleaaraqadaasqaKSAFLANMSHEIRTPLN 533
Cdd:NF033092  341 NFSVIQRESGFINGLIAVLHDVTEQEKIEQE--------------------------------RREFVANVSHELRTPLT 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 534 AILGFThlmrrdapdavtaERLArvDGA------AQHLLAV-----------LNDILDLSKIEAGRLELHEHDFSLRELV 596
Cdd:NF033092  389 TMRSYL-------------EALA--DGAwkdpelAPRFLGVtqnetermirlVNDLLQLSRMDSKDYKLNKEWVNFNEFF 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 597 SRCIEQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGpwlQLGFTVADTG 676
Cdd:NF033092  454 NYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGT-ITFRLLETHN---RIIISISDQG 529
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819251900 677 IGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFS 738
Cdd:NF033092  530 LGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFT 591
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
627-742 2.43e-26

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: 103.99  E-value: 2.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 627 GDSMRIAQALLNLLSNAVKFTEQGGvslQVRLLAREGPWLQlgFTVADTGIGIEAAKLGQLFTAFAQADAtmaRRFGGTG 706
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAG---EITVTLSEGGELT--LTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTG 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819251900 707 LGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLR 742
Cdd:pfam02518  73 LGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
770-881 3.54e-26

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: 103.77  E-value: 3.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHaaTPIVAMTA 849
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT--TPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
365-736 4.23e-26

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: 113.29  E-value: 4.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 365 ELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTperLRSARTPAD--TVASLWRTLQAGETwRGEFVNR 442
Cdd:COG5805   158 RLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKN---LLELLHPCDkeEFKERIESITEVWQ-EFIIERE 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 443 R--KDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELdghrHHLEML-VASRTAeleaaraqadaasqaksa 519
Cdd:COG5805   234 IitKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELM----ARSEKLsIAGQLA------------------ 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 520 flANMSHEIRTPLNAILGFTHLMRRDAPDA-----VTAERLARVDgaaqhllAVLNDILDLSKIEAGRLELhehdFSLRE 594
Cdd:COG5805   292 --AGIAHEIRNPLTSIKGFLQLLQPGIEDKeeyfdIMLSELDRIE-------SIISEFLALAKPQAVNKEK----ENINE 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 595 LVSRCIEQVAERARTKALRLESDV-DDVPDVLfGDSMRIAQALLNLLSNAVKFTEQGG-VSLQVRLlarEGPWLQLgfTV 672
Cdd:COG5805   359 LIQDVVTLLETEAILHNIQIRLELlDEDPFIY-CDENQIKQVFINLIKNAIEAMPNGGtITIHTEE---EDNSVII--RV 432
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819251900 673 ADTGIGIEAAKLGQLFTAFaqadATMARRfgGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFS 736
Cdd:COG5805   433 IDEGIGIPEERLKKLGEPF----FTTKEK--GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFT 490
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
377-737 5.80e-25

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 110.83  E-value: 5.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 377 IVITDPEARIQYVNQAFLDQTGYSREEILGstpERLRSARTPADTVAS-LWRTLQAGETWRGEFVNRRKDGSEYVESAVV 455
Cdd:PRK11360  275 VIAIDRQGKITTMNPAAEVITGLQRHELVG---KPYSELFPPNTPFASpLLDTLEHGTEHVDLEISFPGRDRTIELSVST 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 456 TPLRSPEGRVTHFVAVSEDITERRRLERELdgHRhhlemlvASRTAELeaaraqadaasqakSAFLANMSHEIRTPLNAI 535
Cdd:PRK11360  352 SLLHNTHGEMIGALVIFSDLTERKRLQRRV--AR-------QERLAAL--------------GELVAGVAHEIRNPLTAI 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 536 LGFTHLMRRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLElhehDFSLRELVSRCIEQVAERARTKALRLE 615
Cdd:PRK11360  409 RGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQ----PVSLNALVEEVLQLFQTAGVQARVDFE 484
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 616 SDVD-DVPDVLFgDSMRIAQALLNLLSNAVKFTEQGG-VSLQVRLLAREgpwlQLGFTVADTGIGIEAAKLGQLFTAFAQ 693
Cdd:PRK11360  485 TELDnELPPIWA-DPELLKQVLLNILINAVQAISARGkIRIRTWQYSDG----QVAVSIEDNGCGIDPELLKKIFDPFFT 559
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1819251900 694 ADATmarrfgGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSF 737
Cdd:PRK11360  560 TKAK------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
768-877 1.32e-24

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: 102.34  E-value: 1.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHaaTPIVAM 847
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSD--IPIIML 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:COG0745    80 TARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
369-498 5.06e-24

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


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 106.91  E-value: 5.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 369 AVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKDGSE 448
Cdd:TIGR02938   9 TVDQAPLAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGEL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1819251900 449 YVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVAS 498
Cdd:TIGR02938  89 YLAELTVAPVLNEAGETTHFLGMHRDITELHRLEQVVANQKLLIESVVDA 138
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
768-892 1.43e-23

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: 99.85  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAM 847
Cdd:COG3437     7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFL 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAAGR 892
Cdd:COG3437    87 TALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQR 131
PRK13557 PRK13557
histidine kinase; Provisional
369-834 7.90e-23

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 103.60  E-value: 7.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 369 AVEQTSSSIVITDP---EARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKD 445
Cdd:PRK13557   35 AVETTRMPMIVTDPnqpDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKD 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 446 GSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLEreldghrhhlEMLVASRTAEleaaraqadaasqAKSAFLANMS 525
Cdd:PRK13557  115 GSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAE----------DALRQAQKME-------------ALGQLTGGIA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 526 HEIRTPLNAILGFTHLMRR--DAPDAvTAERLAR--------VDGAA---QHLLAVlndildlskieAGRLELHEHDFSL 592
Cdd:PRK13557  172 HDFNNLLQVMSGYLDVIQAalSHPDA-DRGRMARsveniraaAERAAtltQQLLAF-----------ARKQRLEGRVLNL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 593 RELVSRcIEQVAERARTKALRLESDVD-DVPDVLFgDSMRIAQALLNLLSNAVKFTEQGG-VSLQVR--LLAREGPWLQL 668
Cdd:PRK13557  240 NGLVSG-MGELAERTLGDAVTIETDLApDLWNCRI-DPTQAEVALLNVLINARDAMPEGGrVTIRTRnvEIEDEDLAMYH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 669 GF--------TVADTGIGIEAAKLGQLFTAFAqadaTMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSrfsfSVR 740
Cdd:PRK13557  318 GLppgryvsiAVTDTGSGMPPEILARVMDPFF----TTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGT----TVR 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 741 LRLgetvvatacPAVDGEAELRQ--------RHAGARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDY 812
Cdd:PRK13557  390 LYF---------PASDQAENPEQepkaraidRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPE 460
                         490       500
                  ....*....|....*....|....
gi 1819251900 813 AAILM-DMQMPG-VDGLEATRRIR 834
Cdd:PRK13557  461 VDLLFtDLIMPGgMNGVMLAREAR 484
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
770-881 2.98e-22

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: 92.52  E-value: 2.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMTA 849
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
520-756 3.45e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 101.26  E-value: 3.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 520 FLANMSHEIRTPLNAILGFTHLM--RRDAPDAVTA-------ERLARVDgaaqhllAVLNDILDLSKIEAGRLELHEHDF 590
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATArsaellhTELDRFE-------SLLSDLLEISRFDAGAAELDVEPV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 591 SLRELVSRCIEQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVslQVRLLAREGpwlQLGF 670
Cdd:NF040691  347 DLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPV--VVTVAQDDT---AVAV 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 671 TVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVAT 750
Cdd:NF040691  422 TVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAGDRLTTS 501

                  ....*.
gi 1819251900 751 ACPAVD 756
Cdd:NF040691  502 PLPLVP 507
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
520-743 9.94e-22

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 98.93  E-value: 9.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 520 FLANMSHEIRTPLNAILGFTHLMRRDAPDA--------VTAERLARVDGAAQHLLAvlndildLSKIEAG-RLELHEH-D 589
Cdd:PRK11006  207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGalrekalhTMREQTQRMEGLVKQLLT-------LSKIEAApTIDLNEKvD 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 590 FSLrelVSRCIEQVAERARTKALRLESDVDDVPDVlFGDSMRIAQALLNLLSNAVKFTEQGgVSLQVRllaregpWLQLG 669
Cdd:PRK11006  280 VPM---MLRVLEREAQTLSQGKHTITFEVDNSLKV-FGNEDQLRSAISNLVYNAVNHTPEG-THITVR-------WQRVP 347
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819251900 670 ----FTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRL 743
Cdd:PRK11006  348 qgaeFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPERL 425
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
523-743 2.14e-21

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 98.38  E-value: 2.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 523 NMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQ 602
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 603 VAERARTKALRLESDVDDVpdVLFGDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGpwlQLGFTVADTGIGIEAA 682
Cdd:PRK11100  342 REAQAAAKGITLRLRPDDA--RVLGDPFLLRQALGNLLDNAIDFSPEGGT-ITLSAEVDGE---QVALSVEDQGPGIPDY 415
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819251900 683 KLGQLFTAFaqadATMARRFGG---TGLGLAITRRLALLMGGDVAVDSRVGEGSRfsfsVRLRL 743
Cdd:PRK11100  416 ALPRIFERF----YSLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGVL----ATLTL 471
PRK09303 PRK09303
histidine kinase;
521-739 2.16e-21

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 97.33  E-value: 2.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 521 LANMSHEIRTPLNAI---LGFTHLMRRDAPDAVTAERLARVDGAAQHLLAVLN----DILDLSKIEAGRLELHEHDFSLR 593
Cdd:PRK09303  155 LAMLAHDLRTPLTAAslaLETLELGQIDEDTELKPALIEQLQDQARRQLEEIErlitDLLEVGRTRWEALRFNPQKLDLG 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 594 ELVSRCIEQVAERARTKALRLESDV-DDVPDVlFGDSMRIAQALLNLLSNAVKFTEQGGvSLQVRLLAREGPWLQlgFTV 672
Cdd:PRK09303  235 SLCQEVILELEKRWLAKSLEIQTDIpSDLPSV-YADQERIRQVLLNLLDNAIKYTPEGG-TITLSMLHRTTQKVQ--VSI 310
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 673 ADTGIGIEAAKLGQLFTA---FAQADATmarrfGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSV 739
Cdd:PRK09303  311 CDTGPGIPEEEQERIFEDrvrLPRDEGT-----EGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTL 375
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
517-721 4.29e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 94.51  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLMrRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELV 596
Cdd:NF012163  240 RRDFMADISHELRTPLAVLRAELEAI-QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 597 SRCIEQVAERARTKALRLESDVDDVPdVLFGDSMRIAQALLNLLSNAVKFTEQGGvslQVRLLAREGPwLQLGFTVADTG 676
Cdd:NF012163  319 EVEGGAFRERFASAGLELEVSLPDSS-LVFGDRDRLMQLFNNLLENSLRYTDSGG---SLHISASQRP-KEVTLTVADSA 393
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1819251900 677 IGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGG 721
Cdd:NF012163  394 PGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGG 438
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
518-739 9.55e-20

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: 93.22  E-value: 9.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 518 SAFLANMSHEIRTPLNAILGFTHLM---RRDAPDAVTA--------ERLARVdgaaqhllavLNDILDLSKIEAGRLELH 586
Cdd:TIGR01386 242 SQFSADLAHELRTPLTNLLGQTQVAlsqPRTGEEYREVlesnleelERLSRM----------VSDMLFLARADNGQLALE 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 587 EHDFSLRELVSRCI---EQVAERaRTKALRLESDVddvpdVLFGDSMRIAQALLNLLSNAVKFTEQGGvSLQVRLLAREG 663
Cdd:TIGR01386 312 RVRLDLAAELAKVAeyfEPLAEE-RGVRIRVEGEG-----LVRGDPQMFRRAISNLLSNALRHTPDGG-TITVRIERRSD 384
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251900 664 PWLqlgFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEgSRFSFSV 739
Cdd:TIGR01386 385 EVR---VSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILRF 456
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
366-485 1.51e-19

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 85.04  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 366 LSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVN-RRK 444
Cdd:TIGR00229   5 YRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRK 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1819251900 445 DGSEYVESAVVTPLRSpEGRVTHFVAVSEDITERRRLEREL 485
Cdd:TIGR00229  85 DGSEIWVEVSVSPIRT-NGGELGVVGIVRDITERKEAEEAL 124
PRK13558 PRK13558
bacterio-opsin activator; Provisional
380-497 3.53e-19

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 92.59  E-value: 3.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 380 TDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVTPLR 459
Cdd:PRK13558  167 TLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIR 246
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1819251900 460 SPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVA 497
Cdd:PRK13558  247 DEDGTVTHYVGFQTDVTERKEAELALQRERRKLQRLLE 284
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
465-893 5.50e-19

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 92.43  E-value: 5.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 465 VTHFVAVSEDITERRRLERELDgHRHHLEMLvasrtaeleaaraqadaasqakSAFLANMSHEIRTPLNAILGFTHL-MR 543
Cdd:PRK13837  421 LAHAIERRRLETERDALERRLE-HARRLEAV----------------------GTLASGIAHNFNNILGAILGYAEMaLN 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 544 RDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLElhehDFSLRELVSRCIEQVAErARTKALRLESDVDDVPD 623
Cdd:PRK13837  478 KLARHSRAARYIDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSELVTEIAPLLRV-SLPPGVELDFDQDQEPA 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 624 VLFGDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGP--------------WLQLgfTVADTGIGIEAAKLGQLFT 689
Cdd:PRK13837  553 VVEGNPAELQQVLMNLCSNAAQAMDGAGR-VDISLSRAKLRapkvlshgvlppgrYVLL--RVSDTGAGIDEAVLPHIFE 629
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 690 AFaqadatMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLRLGETVVATACPAVDGEAelrqRHAGAR 769
Cdd:PRK13837  630 PF------FTTRAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQAFFGPGPLP----RGRGET 699
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELL-----------EMAGLCVDVADDGEAavacaaagdyaailMDMQMPGVDGLEATRRIRALPA 838
Cdd:PRK13837  700 VLLVEPDDATLERYEEKLaalgyepvgfsTLAAAIAWISKGPER--------------FDLVLVDDRLLDEEQAAAALHA 765
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1819251900 839 HAATPIVAMTANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAAGRG 893
Cdd:PRK13837  766 AAPTLPIILGGNSKTMALSPDLLASVAEILAKPISSRTLAYALRTALATARAAAA 820
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
771-871 7.62e-19

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: 82.28  E-value: 7.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 771 LLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHaaTPIVAMTAN 850
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD--IPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1819251900 851 AFGEDRQACLDAGMDDHVAKP 871
Cdd:cd00156    79 ADEEDAVRALELGADDYLVKP 99
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
771-871 2.59e-17

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: 77.83  E-value: 2.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 771 LLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHaaTPIVAMTAN 850
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1819251900 851 AFGEDRQACLDAGMDDHVAKP 871
Cdd:cd17574    79 DEEEDKVLGLELGADDYITKP 99
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
517-581 2.85e-17

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 76.87  E-value: 2.85e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAG 581
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
363-741 2.86e-17

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 84.90  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 363 LRELSLAVEQTSSSIVITDPEARIQYVNQAFldqtgysrEEILGstperLRSARTPADTVASlwRTLQAGETWRGEFVNR 442
Cdd:COG3290    83 VEEREAVLESIREGVIAVDRDGRITLINDAA--------RRLLG-----LDAIGRPIDEVLA--EVLETGERDEEILLNG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 443 RkdgseyVESAVVTPLRSpEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVASRtaeleaaraqadaasqaksafla 522
Cdd:COG3290   148 R------VLVVNRVPIRD-DGRVVGAVATFRDRTELERLEEELEGVKELAEALRAQR----------------------- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 523 nmsHEIRTPLNAILGFTHLmrrdapdavtaerlarvdGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELvsrcIEQ 602
Cdd:COG3290   198 ---HDFRNHLHTISGLLQL------------------GEYDEALEYIDEISEELQELIDSLLSRIGNPVLAAL----LLG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 603 VAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVSL-QVRLLAR-EGPWLQlgFTVADTGIGIE 680
Cdd:COG3290   253 KAARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIEAVEKLPEEErRVELSIRdDGDELV--IEVEDSGPGIP 330
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251900 681 AAKLGQLFTafaqadatmaRRF-----GGTGLGLAITRRLALLMGGDVAVDSRVGEGSRfsFSVRL 741
Cdd:COG3290   331 EELLEKIFE----------RGFstklgEGRGLGLALVKQIVEKYGGTIEVESEEGEGTV--FTVRL 384
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
518-736 3.54e-17

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 84.92  E-value: 3.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 518 SAFLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAER-----LARVDgAAQhllAVLNDILDLSKIEAGRLELhehdFSL 592
Cdd:COG5806   202 SELAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQyiriaLEELD-RAE---AIITDYLTFAKPQPEKLEK----IDV 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 593 RELVSRCIEQVAERARTKALRLESDVDDvPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGpwlQLGFTV 672
Cdd:COG5806   274 SEELEHVIDVLSPYANMNNVEIQTELEP-GLYIEGDRQKLQQCLINIIKNGIEAMPNGGT-LTIDVSIDKN---KVIISI 348
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819251900 673 ADTGIGI---EAAKLGQLFtafaqadatmarrFG----GTGLGLAITRRLALLMGGDVAVDSRVGEGSRFS 736
Cdd:COG5806   349 KDTGVGMtkeQLERLGEPY-------------FStkekGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFT 406
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
768-877 5.44e-17

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: 77.48  E-value: 5.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLC-VDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVA 846
Cdd:cd17551     1 MRILIVDDNPTNLLLLEALLRSAGYLeVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1819251900 847 MTANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17551    81 ITADTDREVRLRALEAGATDFLTKPFDPVEL 111
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
769-872 7.79e-17

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: 76.77  E-value: 7.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMT 848
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                          90       100
                  ....*....|....*....|....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPV 872
Cdd:cd17538    81 ALDDREDRIRGLEAGADDFLSKPI 104
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
517-581 1.37e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 74.91  E-value: 1.37e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819251900  517 KSAFLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAG 581
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
628-735 1.48e-16

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: 76.38  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 628 DSMRIAQALLNLLSNAVKFTEQGGvSLQVRLLAREGPWLQLgfTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGL 707
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGG-RIRCILEKFRLNRFLL--TVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                          90       100
                  ....*....|....*....|....*...
gi 1819251900 708 GLAITRRLALLMGGDVAVDSRVGEGSRF 735
Cdd:cd16925    78 GLSIVKEFVELHGGTVTVSDAPGGGALF 105
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-738 3.06e-16

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: 75.06  E-value: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFTEQGGVSlQVRLLAREGP--WLqlgFTVADTGIGIEAAKLGQLFTAFAQADATMArrFGGTGLGL 709
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRRPP-RIEVGAEDVGeeWT---FYVRDNGIGIDPEYAEKVFGIFQRLHSREE--YEGTGVGL 74
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 710 AITRRLALLMGGDVAVDSRVGEGSRFSFS 738
Cdd:cd16921    75 AIVRKIIERHGGRIWLESEPGEGTTFYFT 103
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
768-877 3.45e-16

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: 75.36  E-value: 3.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAM 847
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17618    81 TARGEEEDKVRGLEAGADDYITKPFSPREL 110
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
519-711 3.82e-16

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 81.99  E-value: 3.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 519 AFLANMSHEIRTPLNAILGFTHLMRrDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSR 598
Cdd:PRK10549  242 DFMADISHELRTPLAVLRGELEAIQ-DGVRKFTPESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLLEV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 599 CIEQVAERARTKALRLESDVDDVPdVLFGDSMRIAQALLNLLSNAVKFTEQGGvSLQVRLLAREGPWLqlgFTVADTGIG 678
Cdd:PRK10549  321 AGGAFRERFASRGLTLQLSLPDSA-TVFGDPDRLMQLFNNLLENSLRYTDSGG-SLHISAEQRDKTLR---LTFADSAPG 395
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1819251900 679 IEAAKLGQLFTAFAQADATMARRFGGTGLGLAI 711
Cdd:PRK10549  396 VSDEQLQKLFERFYRTEGSRNRASGGSGLGLAI 428
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
770-872 4.00e-16

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: 74.85  E-value: 4.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMTA 849
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                          90       100
                  ....*....|....*....|...
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPV 872
Cdd:cd19920    81 LTDTEDKVKGFELGAVDYITKPF 103
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
522-735 9.39e-16

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 80.99  E-value: 9.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 522 ANMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARV-DGAAQHLLAVLNDILDLSKieAGRLELHEHDfsLRELVSRCI 600
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVmAKEADRLNRVVSELLELVK--PTHLALQAVD--LNDLINHSL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 601 EQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVslqvrlLAREGPWL--QLGFTVADTGIG 678
Cdd:PRK10364  318 QLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGV------ISVTASESgaGVKISVTDSGKG 391
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251900 679 IEAAKLGQLFTAFAQADATmarrfgGTGLGLAITRRLALLMGGDVAVDSRVGEGSRF 735
Cdd:PRK10364  392 IAADQLEAIFTPYFTTKAE------GTGLGLAVVHNIVEQHGGTIQVASQEGKGATF 442
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
768-892 1.20e-15

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: 80.01  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIVAM 847
Cdd:COG2204     3 ARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRAL--DPDLPVILL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAAGR 892
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRR 125
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
385-477 1.24e-15

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 72.88  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 385 RIQYVNQAFLDQTGYSREEILGSTPERLRsarTPADTVASLWRTLQAGET-WRGEFVNRRKDGSEYVESAVVTPLRSPEG 463
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDLF---AEPEDSERLREALREGKAvREFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
                          90
                  ....*....|....
gi 1819251900 464 RVTHFVAVSEDITE 477
Cdd:pfam13426  80 ELVGIIAILRDITE 93
PRK13559 PRK13559
hypothetical protein; Provisional
369-500 1.97e-15

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 79.09  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 369 AVEQTSSSIVITD---PEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKD 445
Cdd:PRK13559   48 AMEQTRMAMCITDphqPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKD 127
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1819251900 446 GSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRlERELDGHRHHLEMLVASRT 500
Cdd:PRK13559  128 GEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRA-VRALEAHERRLAREVDHRS 181
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
769-881 2.22e-15

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 73.20  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEA--AVACAAAGDYAAILMDMQMPGVDGLEATRRIRAL-PAHAATPIV 845
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEEclNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKLfGRRERPLIV 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819251900 846 AMTANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:cd19933    82 ALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
364-475 2.55e-15

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 72.84  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 364 RELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVN-R 442
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSfR 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1819251900 443 RKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDI 475
Cdd:pfam00989  81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
PRK10490 PRK10490
sensor protein KdpD; Provisional
517-741 3.33e-15

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 80.08  E-value: 3.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLMRRDapdaVTAERLARVDGAA---QHLLA---VLNDILDLSKIEAGRLELHEHDF 590
Cdd:PRK10490  664 RNALLAALSHDLRTPLTVLFGQAEILTLD----LASEGSPHARQASeirQQVLNttrLVNNLLDMARIQSGGFNLRKEWL 739
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 591 SLRELVSRCIEQVAE--RARTKALRLESDVDdvpdVLFGDSMRIAQALLNLLSNAVKFT-EQGGVSLQVRLlarEGPWLQ 667
Cdd:PRK10490  740 TLEEVVGSALQMLEPglSGHPINLSLPEPLT----LIHVDGPLFERVLINLLENAVKYAgAQAEIGIDAHV---EGERLQ 812
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819251900 668 LgfTVADTGIGIEAAKLGQLFTAFAQADATMArrFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRL 741
Cdd:PRK10490  813 L--DVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPL 882
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
519-741 1.01e-14

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 78.82  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 519 AFLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSR 598
Cdd:PRK10618  452 AFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDE 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 599 CIEQVAERARTKALRLESDVD-DVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVSLQVRLLA-REGpwlQLGFTVADTG 676
Cdd:PRK10618  532 VLPEVLPAIKRKGLQLLIHNHlKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDEsSPD---RLTIRILDTG 608
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251900 677 IGIEAAKLGQL---FTAFAQADatmarRFG-GTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRL 741
Cdd:PRK10618  609 AGVSIKELDNLhfpFLNQTQGD-----RYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKM 672
PAS COG2202
PAS domain [Signal transduction mechanisms];
328-485 1.94e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.29  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 328 RRLSEDALRRSQlqtqlsmdeavsararaeaaaaslRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGS 407
Cdd:COG2202   125 RKRAEEALRESE------------------------ERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGK 180
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251900 408 TPERLRSARTPADTVASLWRTLQAG-ETWRGEFVNRRKDGSEYVESAVVTPLRSpEGRVTHFVAVSEDITERRRLEREL 485
Cdd:COG2202   181 SLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
PRK10604 PRK10604
sensor protein RstB; Provisional
523-738 2.18e-14

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 76.57  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 523 NMSHEIRTPLnAILGFTHLMRrDAPDAVTAERLARVDGAaqhLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIEQ 602
Cdd:PRK10604  218 GIAHELRTPL-VRLRYRLEMS-DNLSAAESQALNRDIGQ---LEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLAD 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 603 VAERARTKALRLesDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQggvslQVRLlareGPWLQLGF---TVADTGIGI 679
Cdd:PRK10604  293 IQAVTPEKTVRL--DTPHQGDYGALDMRLMERVLDNLLNNALRYAHS-----RVRV----SLLLDGNQaclIVEDDGPGI 361
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251900 680 EAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFS 738
Cdd:PRK10604  362 PPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFS 420
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-726 2.97e-14

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 69.41  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 628 DSMRIAQALLNLLSNAVKFTEQGGvSLQVRLlAREGPWLQLgfTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGL 707
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRA-AQTPQEVRL--DVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                          90
                  ....*....|....*....
gi 1819251900 708 GLAITRRLALLMGGDVAVD 726
Cdd:cd16946    77 GLAICHNIALAHGGTISAE 95
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-738 3.01e-14

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: 69.38  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFTEQggvSLQVRLLAREGpWLQLgfTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAI 711
Cdd:cd16939     1 MARALDNLLRNALRYAHR---TVRIALLVSGG-RLTL--IVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                          90       100
                  ....*....|....*....|....*..
gi 1819251900 712 TRRLALLMGGDVAVDSRVGEGSRFSFS 738
Cdd:cd16939    75 VHRVALWHGGHVECDDSELGGACFRLT 101
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
769-893 6.08e-14

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 69.61  E-value: 6.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLE-MAGL-CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHaaTPIVA 846
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLErLPGFeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPD--VDVIV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1819251900 847 MTANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAAGRG 893
Cdd:COG4565    83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
627-734 8.09e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli 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: 68.59  E-value: 8.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 627 GDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGPwlqlGFTVADTGIGIEAAKLGQLFTAFAQADATMArrfGGTG 706
Cdd:cd16940     9 GDALLLFLLLRNLVDNAVRYSPQGSR-VEIKLSADDGA----VIRVEDNGPGIDEEELEALFERFYRSDGQNY---GGSG 80
                          90       100
                  ....*....|....*....|....*...
gi 1819251900 707 LGLAITRRLALLMGGDVAVDSRVGEGSR 734
Cdd:cd16940    81 LGLSIVKRIVELHGGQIFLGNAQGGGLE 108
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
771-877 1.30e-13

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: 68.02  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 771 LLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMTAN 850
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTAL 78
                          90       100
                  ....*....|....*....|....*..
gi 1819251900 851 AFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17625    79 DAVEDRVKGLDLGADDYLPKPFSLAEL 105
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
517-577 2.82e-13

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: 65.31  E-value: 2.82e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHLMRRDA-PDAVTAERLARVDGAAQHLLAVLNDILDLSK 577
Cdd:cd00082     4 KGEFLANVSHELRTPLTAIRGALELLEEELlDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
769-877 3.47e-13

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 67.06  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLC--VDVADDGE-------AAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAH 839
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPneLHVVRDGEealdflrGEGEYADAPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1819251900 840 AATPIVAMTANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17557    81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEF 118
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-742 3.78e-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: 67.15  E-value: 3.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 615 ESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGpwlQLGFTVADTGIGIEAAKLGQLFTAFAQA 694
Cdd:cd16947     4 EINIPDRPIYANANTEALQRILKNLISNAIKYGSDGKF-LGMTLREDEK---HVYIDIWDKGKGISETEKDHVFERLYTL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1819251900 695 DATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVGEgsRFSFSVRLR 742
Cdd:cd16947    80 EDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYE--KTVFTVTLK 125
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
770-871 3.83e-13

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: 65.92  E-value: 3.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMTA 849
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLMLTA 78
                          90       100
                  ....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKP 871
Cdd:cd19935    79 RDSVEDRVKGLDLGADDYLVKP 100
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
388-471 4.30e-13

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 65.44  E-value: 4.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 388 YVNQAFLDQTGYSREEILGsTPERLRSARTPAD---TVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVTPLRSPEGR 464
Cdd:pfam08447   3 YWSPRFEEILGYTPEELLG-KGESWLDLVHPDDrerVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGK 81

                  ....*..
gi 1819251900 465 VTHFVAV 471
Cdd:pfam08447  82 PVRVIGV 88
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
521-712 4.50e-13

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 72.27  E-value: 4.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 521 LANMSHEIRTPLNAILGFTHLMRR---DAPDavtaerLARVDGAAQHLLAVLNDILDLSKIEAgRLELHEHDFSLRELVS 597
Cdd:PRK09470  247 LSDISHELRTPLTRLQLATALLRRrqgESKE------LERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWS 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 598 RCIEQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQggvSLQVRLLAREGpwlQLGFTVADTGI 677
Cdd:PRK09470  320 EVLEDAKFEAEQMGKSLTVSAPPGPWPINGNPNALASALENIVRNALRYSHT---KIEVAFSVDKD---GLTITVDDDGP 393
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1819251900 678 GIEAAKLGQLFTAFAQADATMARRFGGTGLGLAIT 712
Cdd:PRK09470  394 GVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIV 428
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
787-877 5.52e-13

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: 66.14  E-value: 5.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 787 LEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMTANAFGEDRQACLDAGMDD 866
Cdd:cd19937    17 LEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAKGEEFDKVLGLELGADD 96
                          90
                  ....*....|.
gi 1819251900 867 HVAKPVDPAQL 877
Cdd:cd19937    97 YITKPFSPREL 107
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
630-735 1.83e-12

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 64.37  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 630 MRIAQALLNLLSNAVKFTEQGGvslqvRLLAREGPWL-QLGFTVADTGIGIEAAKLGQLFTAFAqadaTMARRFGGTGLG 708
Cdd:cd16943     2 SQLNQVLLNLLVNAAQAMEGRG-----RITIRTWAHVdQVLIEVEDTGSGIDPEILGRIFDPFF----TTKPVGEGTGLG 72
                          90       100
                  ....*....|....*....|....*..
gi 1819251900 709 LAITRRLALLMGGDVAVDSRVGEGSRF 735
Cdd:cd16943    73 LSLSYRIIQKHGGTIRVASVPGGGTRF 99
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
770-877 2.82e-12

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: 64.23  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMTA 849
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRS--EGRATPVLILTA 78
                          90       100
                  ....*....|....*....|....*...
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd19934    79 RDSWQDKVEGLDAGADDYLTKPFHIEEL 106
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
635-737 4.20e-12

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: 63.38  E-value: 4.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 635 ALLNLLSNAVKFTEQGGvSLQVRLLAREGpwlQLGFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRR 714
Cdd:cd16952     4 AFSNLVSNAVKYTPPSD-TITVRWSQEES---GARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKH 79
                          90       100
                  ....*....|....*....|...
gi 1819251900 715 LALLMGGDVAVDSRVGEGSRFSF 737
Cdd:cd16952    80 VMSRHDARLLIASELGKGSRFTC 102
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
770-877 4.27e-12

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: 63.66  E-value: 4.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMTA 849
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTA 78
                          90       100
                  ....*....|....*....|....*...
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17624    79 RDGVDDRVAGLDAGADDYLVKPFALEEL 106
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
770-877 6.57e-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: 63.09  E-value: 6.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAMTA 849
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR---KTSQVPVLMLTA 77
                          90       100
                  ....*....|....*....|....*...
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17623    78 RGDDIDRILGLELGADDYLPKPFNPREL 105
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
768-881 6.98e-12

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: 63.09  E-value: 6.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAM 847
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:cd17562    81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
370-480 7.01e-12

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


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 62.82  E-value: 7.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 370 VEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADtVASLWRTLQAGETWRGEFVNRRKDGSEY 449
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAAR-LERALRRALEGEEPIDFLEELLLNGEER 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1819251900 450 VESAVVTPLRSPEGRVTHFVAVSEDITERRR 480
Cdd:pfam08448  80 HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
769-877 1.27e-11

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 62.39  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpaHAATPIVAMT 848
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE---HSHVPILMLT 77
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd19939    78 ARTEEMDRVLGLEMGADDYLCKPFSPREL 106
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
520-739 1.87e-11

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


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 67.85  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 520 FLANMS----HEIRTPLnAIL--GFTHLMRRDAPDAvTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLR 593
Cdd:TIGR03785 484 YLENMSsrlsHELRTPV-AVVrsSLENLELQALEQE-KQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLS 561
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 594 ELVSRCIEqvAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGVsLQVRLLAREGPWLqlgFTVA 673
Cdd:TIGR03785 562 EVLSGCMQ--GYQMTYPPQRFELNIPETPLVMRGSPELIAQMLDKLVDNAREFSPEDGL-IEVGLSQNKSHAL---LTVS 635
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251900 674 DTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRV-GEGSRFSFSV 739
Cdd:TIGR03785 636 NEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISL 702
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
770-877 1.95e-11

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: 61.63  E-value: 1.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMTA 849
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLTA 78
                          90       100
                  ....*....|....*....|....*...
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17627    79 RDSVSDRVAGLDAGADDYLVKPFALEEL 106
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
768-877 1.96e-11

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: 61.63  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAM 847
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR---EQSEVGIILV 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17619    78 TGRDDEVDRIVGLEIGADDYVTKPFNPREL 107
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
769-871 2.02e-11

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 61.33  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLE-MAGL-CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIVA 846
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEwEAGFeVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL--DPDTKIII 78
                          90       100
                  ....*....|....*....|....*
gi 1819251900 847 MTANAFGEDRQACLDAGMDDHVAKP 871
Cdd:COG4753    79 LSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-732 2.32e-11

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 60.93  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFteqGGVSLQVRllaREGPWLQLGFTVADTGIGIEAAKLGQLFTAFAQADAtmARRFGGTGLGLAI 711
Cdd:cd16950     1 LKRVLSNLVDNALRY---GGGWVEVS---SDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDN--ARGTSGTGLGLAI 72
                          90       100
                  ....*....|....*....|.
gi 1819251900 712 TRRLALLMGGDVAVDSRVGEG 732
Cdd:cd16950    73 VQRISDAHGGSLTLANRAGGG 93
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
364-489 3.18e-11

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 66.33  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 364 RELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTpadtvasLWRTLQAGETWRGEFVNRR 443
Cdd:COG3829    11 EELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSP-------LLEVLKTGKPVTGVIQKTG 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1819251900 444 KDGSEYVESAvvTPLRSpEGRVTHFVAVSEDITERRRLERELDGHR 489
Cdd:COG3829    84 GKGKTVIVTA--IPIFE-DGEVIGAVETFRDITELKRLERKLREEE 126
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
517-739 5.36e-11

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 65.95  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 517 KSAFLANMSHEIRTPLNAILGFTHL-MRRDAPDAVTAERLARVDGAAQHLLAVLNDILDLSKIEAGRLELHEHDFSLREL 595
Cdd:PRK09835  262 QSNFSADIAHEIRTPITNLITQTEIaLSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADE 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 596 VSRCIEQVAERARTKALRLESDVDdvPDVLFGDSMRIAQALLNLLSNAVKFTEQG-GVSLQVRLLARegpwlQLGFTVAD 674
Cdd:PRK09835  342 VGKVFDFFEAWAEERGVELRFVGD--PCQVAGDPLMLRRAISNLLSNALRYTPAGeAITVRCQEVDH-----QVQLVVEN 414
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819251900 675 TGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLAITRRLALLMGGDVAVDSRVgEGSRFSFSV 739
Cdd:PRK09835  415 PGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISL 478
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
377-475 5.38e-11

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 59.95  E-value: 5.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 377 IVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVT 456
Cdd:cd00130     5 VIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84
                          90
                  ....*....|....*....
gi 1819251900 457 PLRSPEGRVTHFVAVSEDI 475
Cdd:cd00130    85 PIRDEGGEVIGLLGVVRDI 103
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
769-877 5.75e-11

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 60.47  E-value: 5.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAMT 848
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLR---PKYQGPILLLT 78
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17622    79 ALDSDIDHILGLELGADDYVVKPVEPAVL 107
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
621-739 5.91e-11

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 60.93  E-value: 5.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 621 VPDVLFGDSMRIAQALLNLLSNAVKFTEQGG-VSLQVRLLA--------REGPW--------LQLGFTVADTGIGIEAAK 683
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGnITFRVFLEGgsedrsdrDWGPWrpsmsdesVEIRFEVEINDSGSPSIE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 684 LGQLFtafaqadATMARRFG----GTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSV 739
Cdd:cd16938    81 SASMR-------NSLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
767-881 6.84e-11

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 62.28  E-value: 6.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 767 GARVLLAEDNPVNQEVGRELLEMAG-LCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIV 845
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAGyEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQIS---EERPAPVI 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819251900 846 AMTANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:COG3707    80 LLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
768-877 9.06e-11

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: 59.79  E-value: 9.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAM 847
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR---AESGVPIVML 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17626    78 TAKSDTVDVVLGLESGADDYVAKPFKPKEL 107
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
520-721 1.02e-10

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 64.22  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 520 FLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAeRLARVDgaaqHLLAVLNDILDLSKIEAGRLELHEHDFSLRELV--- 596
Cdd:PRK10755  140 FTADVAHELRTPLAGIRLHLELLEKQHHIDVAP-LIARLD----QMMHTVEQLLQLARAGQSFSSGHYQTVKLLEDVilp 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 597 SRciEQVAERARTKALRLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFTEQGGvSLQVRLLAREGPwlqLGFTVADTG 676
Cdd:PRK10755  215 SQ--DELSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGS-TITIKLSQEDGG---AVLAVEDEG 288
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1819251900 677 IGIEAAKLGQLFTAFAQadatMARRFGGTGLGLAITRRLALLMGG 721
Cdd:PRK10755  289 PGIDESKCGELSKAFVR----MDSRYGGIGLGLSIVSRITQLHHG 329
PRK11517 PRK11517
DNA-binding response regulator HprR;
769-877 1.25e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 62.22  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEAtrrIRALPAHAATPIVAMT 848
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQI---LQTLRTAKQTPVICLT 78
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK11517   79 ARDSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
769-877 1.25e-10

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: 59.31  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPahaATPIVAMT 848
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVT 77
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd19938    78 ARVEEIDRLLGLELGADDYICKPYSPREV 106
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-740 1.45e-10

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: 58.95  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFTEQGGVS---LQVRLLAREGPWLQLgfTVADTGIGIEAAKLGQLFTAFAQADATmarrfgGTGLG 708
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCErreLTIRTSPADDRAVTI--SVKDTGPGIAEEVAGQLFDPFYTTKSE------GLGMG 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819251900 709 LAITRRLALLMGGDVAVDSRVGEGSRFSFSVR 740
Cdd:cd16920    73 LSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
769-871 1.58e-10

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 59.29  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMT 848
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFLT 78
                          90       100
                  ....*....|....*....|...
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKP 871
Cdd:cd17615    79 AKDSVEDRIAGLTAGGDDYVTKP 101
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
769-877 2.40e-10

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: 58.72  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEM-AGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAM 847
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKlAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILL 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17552    83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTL 112
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
769-877 3.13e-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: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAG-LCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAM 847
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGfNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd19923    82 TAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-743 3.83e-10

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


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 57.72  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFTEQggvslQVRL-LAREGPwlQLGFTVADTGIGIEAAKLGQLFTAFAQADATMARRFGGTGLGLA 710
Cdd:cd16949     1 LARALENVLRNALRYSPS-----KILLdISQDGD--QWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLA 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1819251900 711 ITRRLALLMGGDVAVDSRVGEGSRfsfsVRLRL 743
Cdd:cd16949    74 IAERAIEQHGGKIKASNRKPGGLR----VRIWL 102
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
770-877 4.66e-10

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: 57.91  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMA-GLC-VDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAM 847
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEpDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17535    79 TAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
364-487 5.29e-10

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 63.25  E-value: 5.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 364 RELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPER-LRSARTPADTVASLWRTLQAGETWRGEFVNR 442
Cdd:PRK11359  136 RQLIIAVDHLDRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPDTlLNIPEFPADNRIRLQQLLWKTARDQDEFLLL 215
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1819251900 443 RKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLeRELDG 487
Cdd:PRK11359  216 TRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQI-RQLEG 259
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
770-879 6.14e-10

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 57.72  E-value: 6.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMTA 849
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQLYS 879
Cdd:cd17598    81 LSDPRDVIRGLECGADNFITKPYDEKYLLS 110
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
766-873 7.14e-10

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: 57.50  E-value: 7.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 766 AGARVLLaednpvnqevgRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIV 845
Cdd:COG5803    12 AGIRMLL-----------KEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEI--DPDIPVI 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1819251900 846 AMTanAFGED---RQAcLDAGMDDHVAKPVD 873
Cdd:COG5803    79 MMT--AYGELdmvEEA-KELGAKGYFTKPFD 106
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
770-871 8.47e-10

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 57.00  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAA---------ILMDMQMPGVDGLEATRRIRALPAHA 840
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGndlskeldlIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1819251900 841 ATPIVAMTANAFGEDRQACLDAGMDDHVAKP 871
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
770-871 1.70e-09

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: 55.63  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpahAATPIVAMTA 849
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREW---SAVPVIVLSA 77
                          90       100
                  ....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKP 871
Cdd:cd17620    78 RDEESDKIAALDAGADDYLTKP 99
ompR PRK09468
osmolarity response regulator; Provisional
765-877 2.54e-09

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 58.83  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 765 HAGARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPI 844
Cdd:PRK09468    3 QENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRS--QNNPTPI 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1819251900 845 VAMTANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK09468   81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPREL 113
pleD PRK09581
response regulator PleD; Reviewed
768-879 3.23e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 60.30  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNqevgRELLEmAGLC-----VDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAAT 842
Cdd:PRK09581    3 ARILVVDDIPAN----VKLLE-AKLLaeyytVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHI 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1819251900 843 PIVAMTANAFGEDRQACLDAGMDDHVAKPVDPAQLYS 879
Cdd:PRK09581   78 PVVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFA 114
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
770-871 4.45e-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: 54.69  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMTA 849
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKP 871
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
769-890 1.76e-08

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 54.92  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIVAMT 848
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRER--DPDARIVVLT 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAA 890
Cdd:COG4567    84 GYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPA 125
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
768-849 1.92e-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: 52.99  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAM 847
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIIC 78

                  ..
gi 1819251900 848 TA 849
Cdd:cd17554    79 TA 80
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
769-877 2.04e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 55.96  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEaAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAMT 848
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGE-QALDLLDDSIDLLLLDVMMPKKNGIDTLKELR---QTHQTPVIMLT 78
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK10955   79 ARGSELDRVLGLELGADDYLPKPFNDREL 107
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
769-881 2.64e-08

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 52.67  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGL-CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAAtpIVAM 847
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYeVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK--VIMC 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1819251900 848 TAnafgEDRQA----CLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:cd17542    80 SA----MGQEEmvkeAIKAGAKDFIVKPFQPERVLEAV 113
PRK10337 PRK10337
sensor protein QseC; Provisional
520-732 3.83e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 56.58  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 520 FLANMSHEIRTPLNAIlgfthlmrrdapdAVTAE--RLARVDGAA-QHLLAVL-----------NDILDLSKIEAGRLEL 585
Cdd:PRK10337  240 FTSDAAHELRSPLAAL-------------KVQTEvaQLSDDDPQArKKALLQLhagidratrlvDQLLTLSRLDSLDNLQ 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 586 HEHDFSLRELV-SRCIEQ--VAERARtKALRLESDVDDVPdvlfgdsmRIAQALL------NLLSNAVKFTEQGGVsLQV 656
Cdd:PRK10337  307 DVAEIPLEDLLqSAVMDIyhTAQQAG-IDVRLTLNAHPVI--------RTGQPLLlsllvrNLLDNAIRYSPQGSV-VDV 376
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251900 657 RLLAREgpwlqlgFTVADTGIGIEA---AKLGQLFTAFAQADATmarrfgGTGLGLAITRRLALLMGGDVAVDSRVGEG 732
Cdd:PRK10337  377 TLNARN-------FTVRDNGPGVTPealARIGERFYRPPGQEAT------GSGLGLSIVRRIAKLHGMNVSFGNAPEGG 442
PRK13560 PRK13560
hypothetical protein; Provisional
363-495 4.22e-08

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 56.99  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 363 LRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARtPADTVASL-WRTLQAGETWRGEFVN 441
Cdd:PRK13560  203 LHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQ-PADDYQEAdAAKFDADGSQIIEAEF 281
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 442 RRKDGSEYVESAVVTPLR--SPEGRVTHFVAVSEDITERRRLEREL----DGHRHHLEML 495
Cdd:PRK13560  282 QNKDGRTRPVDVIFNHAEfdDKENHCAGLVGAITDISGRRAAERELlekeDMLRAIIEAA 341
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
770-877 5.23e-08

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 52.03  E-value: 5.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMTA 849
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRL--AKVKTPILILSG 78
                          90       100
                  ....*....|....*....|....*...
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17616    79 LADIEDKVKGLGFGADDYMTKPFHKDEL 106
PRK10610 PRK10610
chemotaxis protein CheY;
769-877 5.96e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 52.28  E-value: 5.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGL-CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAM 847
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK10610   87 TAEAKKENIIAAAQAGASGYVVKPFTAATL 116
PRK15479 PRK15479
transcriptional regulator TctD;
769-877 7.40e-08

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 53.96  E-value: 7.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMT 848
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRK--RGQTLPVLLLT 79
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK15479   80 ARSAVADRVKGLNVGADDYLPKPFELEEL 108
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
769-881 9.04e-08

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 51.26  E-value: 9.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGL-CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAM 847
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYeVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT---SENIAPIVLL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:cd19932    79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
768-892 1.06e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 53.49  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMA-GLC-VDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIV 845
Cdd:PRK10651    7 ATILLIDDHPMLRTGVKQLISMApDITvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE--KSLSGRIV 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1819251900 846 AMTANAFGEDRQACLDAGMDDHVAKPVDPAQlysvLLHWLGRQAAGR 892
Cdd:PRK10651   85 VFSVSNHEEDVVTALKRGADGYLLKDMEPED----LLKALQQAAAGE 127
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-741 1.16e-07

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: 50.86  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFTEQGG--------VSLQVRLlAREGPWLQLGFTVADTGIGIEAAKLGQLFTAFaqadatMARRFG 703
Cdd:cd16918     1 LIQVFLNLVRNAAQALAGSGgeiilrtrTQRQVTL-GHPRHRLALRVSVIDNGPGIPPDLQDTIFYPM------VSGREN 73
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1819251900 704 GTGLGLAITRRLALLMGGDVAVDSRVGegsRFSFSVRL 741
Cdd:cd16918    74 GTGLGLAIAQNIVSQHGGVIECDSQPG---HTVFSVSL 108
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
769-875 2.14e-07

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 50.47  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGL--CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVA 846
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILESDPDieVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIM---AERPTPVVM 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1819251900 847 MTANAFGEDRQA--CLDAGMDDHVAKPVDPA 875
Cdd:cd17541    79 VSSLTEEGAEITleALELGAVDFIAKPSGGI 109
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
639-738 2.46e-07

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: 49.98  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 639 LLSNAVKFTEQGGvSLQVRLlAREGPWLQLgfTVADTGIGIEAAKLGQLFTAFAQAdaTMARRFG-GTGLGLAITRRLAL 717
Cdd:cd16948    13 IVSNALKYSKQGG-KIEIYS-ETNEQGVVL--SIKDFGIGIPEEDLPRVFDKGFTG--ENGRNFQeSTGMGLYLVKKLCD 86
                          90       100
                  ....*....|....*....|.
gi 1819251900 718 LMGGDVAVDSRVGEGSRFSFS 738
Cdd:cd16948    87 KLGHKIDVESEVGEGTTFTIT 107
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
21-559 2.87e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 54.49  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900   21 LPLRVFLRRLIWLCVGpmlllgaaiafyrvqsSLEQRQQAAERIVARLTLLADQMLESRLAGLMMLAQGVDPSASLDEMR 100
Cdd:COG3321    863 LPTYPFQREDAAAALL----------------AAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAAL 926
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  101 RLGESYARGYGSHVLLVDADGRVAMNSRLPQDVEQPPLPRPAALDAAQAALREGRPVVGNLFVGPIAGVPIVSVAVP-LP 179
Cdd:COG3321    927 AALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALAlLA 1006
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  180 PEPGRSPRLLLSTIEASQFQPLLERLLLPPGWSLELRDAAGQAVARRGEPIVGEDGRLRSAALERASWTAVVRIPPQVLH 259
Cdd:COG3321   1007 AAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALAL 1086
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  260 DAVAAEALPLVAGVLGATLIGVLGGTIAGRRLGRDVASLAAPAGTPEAQSGVAEIAAVRRQLDDAAQRRRLSEDALRRSQ 339
Cdd:COG3321   1087 AAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAA 1166
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  340 LQTQLSMDEAVSARARAEAAAASLRELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPA 419
Cdd:COG3321   1167 LLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVA 1246
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  420 DTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLERELDGHRHHLEMLVASR 499
Cdd:COG3321   1247 ALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALL 1326
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  500 TAELEAARAQADAASQAKSAFLANMSHEIRTPLNAILGFTHLMRRDAPDAVTAERLARVD 559
Cdd:COG3321   1327 AAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
envZ PRK09467
osmolarity sensor protein; Provisional
521-714 3.54e-07

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 53.76  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 521 LANMSHEIRTPLNAILGFTHLMRRDapDAVTAErlarvdgaaqhllAVLNDILDLSKI-----------EAGRLELHEhd 589
Cdd:PRK09467  233 MAGVSHDLRTPLTRIRLATEMMSEE--DGYLAE-------------SINKDIEECNAIieqfidylrtgQEMPMEMAD-- 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 590 fsLRELVSRCIEQVAERARTkalrLESDVDDVPDVLFGDSMRIAQALLNLLSNAVKFteqGGVSLQVRLlAREGPWLqlG 669
Cdd:PRK09467  296 --LNALLGEVIAAESGYERE----IETALQPGPIEVPMNPIAIKRALANLVVNAARY---GNGWIKVSS-GTEGKRA--W 363
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1819251900 670 FTVADTGIGIEAAKLGQLFTAFAQADatMARRFGGTGLGLAITRR 714
Cdd:PRK09467  364 FQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKR 406
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
634-730 3.89e-07

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 49.38  E-value: 3.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 634 QALLNLLSNAVKFTEQGG-VSLQVRLLARegpwlQLGFTVADTGIGIEAAKLGQLFTAFaqadATMARRFGG---TGLGL 709
Cdd:cd16945     7 QAINNLLDNAIDFSPEGGlIALQLEADTE-----GIELLVFDEGSGIPDYALNRVFERF----YSLPRPHSGqksTGLGL 77
                          90       100
                  ....*....|....*....|.
gi 1819251900 710 AITRRLALLMGGDVAVDSRVG 730
Cdd:cd16945    78 AFVQEVAQLHGGRITLRNRPD 98
PRK10766 PRK10766
two-component system response regulator TorR;
769-877 3.95e-07

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 51.96  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAMT 848
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR---SRSTVGIILVT 80
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK10766   81 GRTDSIDRIVGLEMGADDYVTKPLELREL 109
glnL PRK11073
nitrogen regulation protein NR(II);
375-715 4.31e-07

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 53.16  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 375 SSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSarTPADTVASLWRTLQAGETWRGEFVNRRKDGSEYVESAV 454
Cdd:PRK11073   18 NSILLLDDDLAIHYANPAAQQLLAQSSRKLFGTPLPELLS--YFSLNIELMRESLQAGQGFTDNEVTLVIDGRSHILSLT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 455 VTPLrsPEGrvtHFVAVSEDITERRRLERELDGHRHHlemlVASRtaELeaaraqadaasqaksafLANMSHEIRTPLNA 534
Cdd:PRK11073   96 AQRL--PEG---MILLEMAPMDNQRRLSQEQLQHAQQ----VAAR--DL-----------------VRGLAHEIKNPLGG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 535 ILGFTHLMRRDAPDAVTAERLARVDGAAQHLLAVLNDILdlskieaGRLELHEHdfslrelVSRCIEQVAERART----- 609
Cdd:PRK11073  148 LRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLL-------GPQRPGTH-------VTESIHKVAERVVQlvsle 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 610 --KALRLESDVD-DVPDVLFgDSMRIAQALLNLLSNAVK-FTEQGGV-------SLQV-------RLLARegpwlqlgFT 671
Cdd:PRK11073  214 lpDNVRLIRDYDpSLPELAH-DPDQIEQVLLNIVRNALQaLGPEGGTitlrtrtAFQLtlhgeryRLAAR--------ID 284
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1819251900 672 VADTGIGIEAAKLGQLFTAFAQAdatmarRFGGTGLGLAITRRL 715
Cdd:PRK11073  285 IEDNGPGIPPHLQDTLFYPMVSG------REGGTGLGLSIARNL 322
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
769-877 4.73e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 51.64  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMT 848
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLT 83
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK10161   84 ARGEEEDRVRGLETGADDYITKPFSPKEL 112
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
770-871 5.39e-07

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 48.73  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpaHAATPIVAMTA 849
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA---RSNVPVIMVTA 77
                          90       100
                  ....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKP 871
Cdd:cd17621    78 KDSEIDKVVGLELGADDYVTKP 99
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
769-877 8.98e-07

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 52.54  E-value: 8.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIVAMT 848
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSH--ETRTPVILMT 83
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK11361   84 AYAEVETAVEALRCGAFDYVIKPFDLDEL 112
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
213-742 1.02e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 52.21  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 213 LELRDAAGQAVARRGEPIVGEDGRLRSAALERASWTAVVRIPPQVLHDAVAAEALPLVAGVLGATLIGVLGGTIAGRRLG 292
Cdd:COG3920    15 ALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 293 RDVASLAAPAGTPEAQSGVAEIAAVRRQLDDAAQRRRLSEDALRRSQLQTQLSMDEAVSARARAEAAAASLRELSLAVEQ 372
Cdd:COG3920    95 AAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 373 TSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSARTPADTVASLWRTLQAGETWRGEFVNRRKDGSEYVES 452
Cdd:COG3920   175 AALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLL 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 453 AVVTPLRSPEGRVTHFVAVSED-ITERRRLERELDGHRHHLEMLvasrtaeleaaraqadaasqaksafLANMSHEIRTP 531
Cdd:COG3920   255 LLLLLLLLLLRALLLLAAGIRLvITERKRAEEELEASLEEKELL-------------------------LRELHHRVKNN 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 532 LNAILGFTHLMRRDAPDAVTAERLA----RVDGaaqhlLAVLNDILDLSKieagrlelHEHDFSLRELVSRCIEQVAERA 607
Cdd:COG3920   310 LQVVSSLLRLQARRADDPEAREALEesqnRIQA-----LALVHELLYQSE--------DWEGVDLRDYLRELLEPLRDSY 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 608 RTKALRLESDVDDVPdvLfgdSMRIAQAL---LN-LLSNAVK--FTEQGGVSLQVRLlAREGPWLQLgfTVADTGIGIEA 681
Cdd:COG3920   377 GGRGIRIELDGPDVE--L---PADAAVPLgliLNeLVTNALKhaFLSGEGGRIRVSW-RREDGRLRL--TVSDNGVGLPE 448
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819251900 682 aklgqlftafaqaDATMARRfggTGLGLAITRRLALLMGGDVAVDSrvGEGSRFSFSVRLR 742
Cdd:COG3920   449 -------------DVDPPAR---KGLGLRLIRALVRQLGGTLELDR--PEGTRVRITFPLA 491
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
770-881 1.06e-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: 48.64  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRA----LP-----AHA 840
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIREldpdLPvilitGHG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1819251900 841 ATP--IVAMTANAFgedrqacldagmdDHVAKPVDPAQLYSVL 881
Cdd:cd17549    81 DVPmaVEAMRAGAY-------------DFLEKPFDPERLLDVV 110
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
364-408 1.07e-06

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 46.62  E-value: 1.07e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1819251900  364 RELSLAVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGST 408
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
769-822 1.35e-06

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: 46.02  E-value: 1.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1819251900  769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMP 822
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
769-884 1.41e-06

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 48.01  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLE-MAGL-CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVA 846
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEqVPGFtVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA--AGHDVDVIV 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1819251900 847 MTANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHW 884
Cdd:cd19925    80 VTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
639-743 1.56e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 51.56  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 639 LLSNAVKF---TEQGGVSLQVRLLAREGpwlQLGFTVADTGIGIEAAKLGQLFTAFAQADatmarrfGGTGLGLA-ITRR 714
Cdd:COG2972   344 LVENAIEHgiePKEGGGTIRISIRKEGD---RLVITVEDNGVGMPEEKLEKLLEELSSKG-------EGRGIGLRnVRER 413
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1819251900 715 LALLMGGD--VAVDSRVGEGsrfsFSVRLRL 743
Cdd:COG2972   414 LKLYYGEEygLEIESEPGEG----TTVTIRI 440
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
815-881 1.67e-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: 47.72  E-value: 1.67e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 815 ILMDMQMPGVDGLEATRRIRALpaHAATPIVAMTanAFGE---DRQAcLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:cd17536    49 VITDIRMPGMDGLELIEKIREL--YPDIKIIILS--GYDDfeyAQKA-IRLGVVDYLLKPVDEEELEEAL 113
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
626-723 1.87e-06

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: 47.27  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 626 FGDSMRIAQALLNLLSNAVKFT--EQGGVSLQV----RLLAREGPWLQLGFTVADTGIGIEAAKLGQLFtafaQADATMA 699
Cdd:cd16932     1 YGDQIRLQQVLADFLLNAVRFTpsPGGWVEIKVsptkKQIGDGVHVIHLEFRITHPGQGLPEELVQEMF----EENQWTT 76
                          90       100
                  ....*....|....*....|....
gi 1819251900 700 RRfggtGLGLAITRRLALLMGGDV 723
Cdd:cd16932    77 QE----GLGLSISRKLVKLMNGDV 96
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
770-877 1.99e-06

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: 47.44  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpaHAATPIVAMTA 849
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA---RSDVPIIIISG 78
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 850 NAFGE-DRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17594    79 DRRDEiDRVVGLELGADDYLAKPFGLREL 107
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
769-890 2.11e-06

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 49.92  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMT 848
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLLT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAA 890
Cdd:PRK09836   80 ALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAA 121
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
774-871 2.32e-06

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 46.98  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 774 EDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVAMTANAFG 853
Cdd:cd17602     5 DDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGL 84
                          90
                  ....*....|....*...
gi 1819251900 854 EDRQACLDAGMDDHVAKP 871
Cdd:cd17602    85 VDRIRAKMAGASGYLTKP 102
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
770-871 2.40e-06

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: 47.03  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpahAATPIVAMTA 849
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT---SNVPIIMLTA 77
                          90       100
                  ....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKP 871
Cdd:cd17614    78 KDSEVDKVLGLELGADDYVTKP 99
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
768-881 3.04e-06

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: 47.02  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCV-DVADDGEAAVACAAAGDYAAILMDMQMPG-VDGLEATRRIRalpAHAATPIV 845
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIR---EKFDIPVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1819251900 846 AMTANAfgedrqacldagmDDH-------------VAKPVDPAQLYSVL 881
Cdd:cd17534    78 FLTAYS-------------DEEtleraketnpygyLVKPFNERELKAAI 113
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-734 5.93e-06

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: 45.99  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 628 DSMRIAQALLNLLSNAVKFTE-QGGVSLQVRLLAREGPWLQLGFTVADTGIGIEAAKLGQLFTAFaqadatMARRFGGTG 706
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEgRPSDVGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPY------VTTRPKGTG 74
                          90       100
                  ....*....|....*....|....*...
gi 1819251900 707 LGLAITRRLALLMGGDVAVDSRVGEGSR 734
Cdd:cd16944    75 LGLAIVKKIMEEHGGRISLSNREAGGAC 102
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
769-881 6.13e-06

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 48.27  E-value: 6.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLE-MAGL-CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHaaTPIVA 846
Cdd:COG3279     3 KILIVDDEPLARERLERLLEkYPDLeVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPP--PPIIF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1819251900 847 MTA------NAFgeDRQACldagmdDHVAKPVDPAQLYSVL 881
Cdd:COG3279    81 TTAydeyalEAF--EVNAV------DYLLKPIDEERLAKAL 113
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
638-741 7.81e-06

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: 45.46  E-value: 7.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 638 NLLSNAVKFTEQGGVSLQVRLLAREgpwlQLGFTVADTGIGIEAAKLGQLFTAFAQADAtmARRFGGTGLGLAITRRLAL 717
Cdd:cd16923     7 NLLSNAIKYSPENTRIYITSFLTDD----VVNIMFKNPSSHPLDFKLEKLFERFYRGDN--SRNTEGAGLGLSIAKAIIE 80
                          90       100
                  ....*....|....*....|....
gi 1819251900 718 LMGGDVAVDSrvgEGSRFSFSVRL 741
Cdd:cd16923    81 LHGGSASAEY---DDNHDLFKVRL 101
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
760-874 9.58e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 47.76  E-value: 9.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 760 ELRQRHAGARVLLAEDNPvnqEVGREL---LEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAL 836
Cdd:PRK10710    3 ELPIDENTPRILIVEDEP---KLGQLLidyLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRF 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1819251900 837 pahAATPIVAMTANAFGEDRQACLDAGMDDHVAKPVDP 874
Cdd:PRK10710   80 ---SDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSP 114
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-737 9.87e-06

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: 45.14  E-value: 9.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNA---VKFTEQGGVSLQVRLLAreGPWLqlgFTVADTGIGIEAAKLGQLFTAFAQAdatmaRRFG-GTGL 707
Cdd:cd16976     1 IQQVLMNLLQNAldaMGKVENPRIRIAARRLG--GRLV---LVVRDNGPGIAEEHLSRVFDPFFTT-----KPVGkGTGL 70
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 708 GLAITRRLALLMGGDVAVDSRVGEGSRFSF 737
Cdd:cd16976    71 GLSISYGIVEEHGGRLSVANEEGAGARFTF 100
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
769-833 1.09e-05

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 45.65  E-value: 1.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAG--LCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRI 833
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK10816 PRK10816
two-component system response regulator PhoP;
769-871 1.44e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 47.04  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMT 848
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRS--NDVSLPILVLT 79
                          90       100
                  ....*....|....*....|...
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKP 871
Cdd:PRK10816   80 ARESWQDKVEVLSAGADDYVTKP 102
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
437-478 1.57e-05

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 42.56  E-value: 1.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1819251900  437 GEFVNRRKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITER 478
Cdd:smart00086   2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
orf27 CHL00148
Ycf27; Reviewed
787-877 1.95e-05

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 47.02  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 787 LEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAMTANAFGEDRQACLDAGMDD 866
Cdd:CHL00148   26 LSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR---KESDVPIIMLTALGDVSDRITGLELGADD 102
                          90
                  ....*....|.
gi 1819251900 867 HVAKPVDPAQL 877
Cdd:CHL00148  103 YVVKPFSPKEL 113
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
638-736 1.95e-05

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: 44.20  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 638 NLLSNAVK-FTEQGGVSLQVRLLAR-EGPWLQLgfTVADTGIGIEAAKLGQLFTAFAQADATMARrfggtGLGLAITRRL 715
Cdd:cd16915     7 NLIDNALDaLAATGAPNKQVEVFLRdEGDDLVI--EVRDTGPGIAPELRDKVFERGVSTKGQGER-----GIGLALVRQS 79
                          90       100
                  ....*....|....*....|.
gi 1819251900 716 ALLMGGDVAVDSRVGEGSRFS 736
Cdd:cd16915    80 VERLGGSITVESEPGGGTTFS 100
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
770-875 1.96e-05

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 44.66  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVAD-----------DGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPA 838
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDsgkraleflglEDEEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1819251900 839 HAATPIVAMTANAFGEDRQACLDAGMDDHVAKPVDPA 875
Cdd:cd17581    81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLA 117
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-737 2.12e-05

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: 44.37  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 628 DSMRIAQALLNLLSNAVKFTEQGG-VSLQVRLLARegpwlQLGFTVADTGIGIEAAKLGQLFTAFAQADatMARRFGG-T 705
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGtVSISIYDEEE-----YLYFEIWDNGHGFSEQDLKKALELFYRDD--TSRRSGGhY 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819251900 706 GLGLAITRRLALLMGGDVAVDSRVGEGSRFSF 737
Cdd:cd16975    74 GMGLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
PRK09483 PRK09483
response regulator; Provisional
770-853 3.05e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 46.25  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNP-VNQEVGRELLEMAGL-CVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRI-RALP--------A 838
Cdd:PRK09483    4 VLLVDDHElVRAGIRRILEDIKGIkVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKIlRYTPdvkiimltV 83
                          90
                  ....*....|....*..
gi 1819251900 839 HAATPIVA--MTANAFG 853
Cdd:PRK09483   84 HTENPLPAkvMQAGAAG 100
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
768-883 3.59e-05

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 43.73  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIVAM 847
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVIVV 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVdpaQLYSVLLH 883
Cdd:cd17555    79 SGAGVMSDAVEALRLGAWDYLTKPI---EDLAVLEH 111
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
525-727 4.03e-05

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 47.37  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 525 SHEIRTPLNAILGFTHLMRRdapdAVTAERLARVDGA---AQHLLAVLNDILDLSKIEAGRLELHEHDFSLRELVSRCIE 601
Cdd:COG4192   441 AHELNQPLNAMSMYLFSAKK----ALEQENYAQLPTSldkIEGLIERMDKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWE 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 602 QVAERARTK--ALRLESDVDdvpdvLFGDSMRIAQALLNLLSNAVK-FTEQGGVSLQvrlLAREGPWLQLgfTVADTGIG 678
Cdd:COG4192   517 LVESRAKPQqiTLHIPDDLM-----VQGDQVLLEQVLVNLLVNALDaVATQPQISVD---LLSNAENLRV--AISDNGNG 586
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1819251900 679 IEAA-KLGQLFTAFAQAdatmarrfgGTGLGLAITRRLALLMGGDVAVDS 727
Cdd:COG4192   587 WPLVdKLFTPFTTTKEV---------GLGLGLSICRSIMQQFGGDLYLAS 627
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
634-736 4.86e-05

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


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 43.52  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 634 QALLNLLSNAVKFTEQGG----------VSLQVRLLARE-GPWLQLGFTVADTGIGIEAAKLGQLFTAFAqadaTMARRF 702
Cdd:cd16919     3 LAILNLAVNARDAMPEGGrltietsnqrVDADYALNYRDlIPGNYVCLEVSDTGSGMPAEVLRRAFEPFF----TTKEVG 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1819251900 703 GGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFS 736
Cdd:cd16919    79 KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVR 112
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
768-877 5.29e-05

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 43.55  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNP-VNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAATPIVA 846
Cdd:cd17575     1 IMVLLVDDQAiIGEAVRRALADEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIV 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1819251900 847 MTANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:cd17575    81 LSTKEEPEVKSEAFALGANDYLVKLPDKIEL 111
PRK10643 PRK10643
two-component system response regulator PmrA;
769-877 5.32e-05

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 45.41  E-value: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMT 848
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ--KKYTLPVLILT 79
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK10643   80 ARDTLEDRVAGLDVGADDYLVKPFALEEL 108
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
770-891 5.70e-05

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 45.57  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEAtrrIRALPAHAATPIVAMTA 849
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEF---IRDLRQWSAIPVIVLSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLHWLGRQAAG 891
Cdd:PRK10529   81 RSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSAT 122
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
787-873 8.41e-05

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 42.65  E-value: 8.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 787 LEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMTANAFGEDRQACLDAGMDD 866
Cdd:cd19919    20 LAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ--RHPDLPVIIMTAHSDLDSAVSAYQGGAFE 97

                  ....*..
gi 1819251900 867 HVAKPVD 873
Cdd:cd19919    98 YLPKPFD 104
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
608-736 1.17e-04

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 43.00  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 608 RTKALRLESDVDdvPDVLF----GDSMRIaqaLLNLLSNAVKFTEQggvslQVRLLAREGPWlQLGFTVADTGIGIEAAK 683
Cdd:cd16954    15 QRKGVSISLDIS--PELRFpgerNDLMEL---LGNLLDNACKWCLE-----FVEVTARQTDG-GLHLIVDDDGPGVPESQ 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1819251900 684 LGQLFTAFAQADatmaRRFGGTGLGLAITRRLALLMGGDVAV-DSRVGeGSRFS 736
Cdd:cd16954    84 RSKIFQRGQRLD----EQRPGQGLGLAIAKEIVEQYGGELSLsDSPLG-GARFE 132
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
786-877 1.44e-04

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: 43.94  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 786 LLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAatPIVAMTANAfgeDRQACLDA--- 862
Cdd:COG4566    18 LLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPL--PVIFLTGHG---DVPMAVRAmka 92
                          90
                  ....*....|....*
gi 1819251900 863 GMDDHVAKPVDPAQL 877
Cdd:COG4566    93 GAVDFLEKPFDDQAL 107
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
770-873 1.94e-04

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: 41.65  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPV-NQEVGRELLEmAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMT 848
Cdd:cd17573     1 ILLIEDDSTlGKEISKGLNE-KGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKE--KHPSIVVIVLS 77
                          90       100
                  ....*....|....*....|....*
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVD 873
Cdd:cd17573    78 DNPKTEQEIEAFKEGADDYIAKPFD 102
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
369-485 2.64e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 45.05  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  369 AVEQTSSSIVITDPEARIQYVNQAFLDQTGYSREEILGSTPERLRSartPAD--TVASLWRTLQAGE--TWRGEFVNRRK 444
Cdd:PRK09776   288 AMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTW---PEDlnKDLQQVEKLLSGEinSYSMEKRYYRR 364
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1819251900  445 DGsEYVESA-VVTPLRSPEGRVTHFVAVSEDITERRRLEREL 485
Cdd:PRK09776   365 DG-EVVWALlAVSLVRDTDGTPLYFIAQIEDINELKRTEQVN 405
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
815-873 7.20e-04

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 40.23  E-value: 7.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251900 815 ILMDMQMPGVDGLEATRRIRALpaHAATPIVAMTANAFGEDRQACLDAGMDDHVAKPVD 873
Cdd:cd17553    48 VLLDMKIPGMDGIEILKRMKVI--DENIRVIIMTAYGELDMIQESKELGALTHFAKPFD 104
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
769-849 8.51e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 42.56  E-value: 8.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAG--LCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpahAATPIVA 846
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALARDPdhEVVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAE---RPCPILI 78

                  ...
gi 1819251900 847 MTA 849
Cdd:PRK12555   79 VTS 81
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
770-882 8.55e-04

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 40.02  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVAD--DGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAAtpIVAM 847
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEasSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSAR--IVIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLL 882
Cdd:cd19931    79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALK 113
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
638-736 9.58e-04

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 42.59  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 638 NLLSN---AVKFTEQGGVSLQVRLlaREGpwlQLGFTVADTGIGIEAAKLGQLFTafaQADATMARrfgGTGLGLAITRR 714
Cdd:PRK11086  440 NLIENaleAVGGEEGGEISVSLHY--RNG---WLHCEVSDDGPGIAPDEIDAIFD---KGYSTKGS---NRGVGLYLVKQ 508
                          90       100
                  ....*....|....*....|..
gi 1819251900 715 LALLMGGDVAVDSRVGEGSRFS 736
Cdd:PRK11086  509 SVENLGGSIAVESEPGVGTQFF 530
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
770-881 9.98e-04

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 42.71  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIVAMTA 849
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL--NPAIPVLIMTA 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819251900 850 NAFGEDRQACLDAGMDDHVAKPVDPAQLYSVL 881
Cdd:PRK10365   86 YSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-735 1.06e-03

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 39.48  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 632 IAQALLNLLSNAVKFTEQGGVSLQVRLlAREGPWLQLgfTVADTGIGIEAAKLGQLFTAFaQADATMARRFG-GTGLGLA 710
Cdd:cd16953     1 LGQVLRNLIGNAISFSPPDTGRITVSA-MPTGKMVTI--SVEDEGPGIPQEKLESIFDRF-YTERPANEAFGqHSGLGLS 76
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 711 ITRRLALLMGGDVAVDSR----VGEGSRF 735
Cdd:cd16953    77 ISRQIIEAHGGISVAENHnqpgQVIGARF 105
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
770-883 1.61e-03

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: 39.15  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYA--AILMDMQMPGVDGLEATRRIRALPahaATPIVAM 847
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEfdLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQLYSVLLH 883
Cdd:cd17584    78 SADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQH 113
PRK11173 PRK11173
two-component response regulator; Provisional
769-877 2.08e-03

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 40.77  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAMT 848
Cdd:PRK11173    5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR---EQANVALMFLT 81
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK11173   82 GRDNEVDKILGLEIGADDYITKPFNPREL 110
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
786-877 2.14e-03

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: 38.73  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 786 LLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHaaTPIVAMTANafGEDRQA--CLDAG 863
Cdd:cd17537    19 LLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSN--IPIIFITGH--GDVPMAveAMKAG 94
                          90
                  ....*....|....
gi 1819251900 864 MDDHVAKPVDPAQL 877
Cdd:cd17537    95 AVDFLEKPFRDQVL 108
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
769-851 2.90e-03

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 38.25  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDG-EAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIVAM 847
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGaEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKI--DPDVKILFI 78

                  ....
gi 1819251900 848 TANA 851
Cdd:cd18160    79 SGGA 82
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
768-877 2.94e-03

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 40.33  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 768 ARVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALpaHAATPIVAM 847
Cdd:PRK11083    4 PTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAF--HPALPVIFL 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1819251900 848 TANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK11083   82 TARSDEVDRLVGLEIGADDYVAKPFSPREV 111
PRK10336 PRK10336
two-component system response regulator QseB;
769-871 2.98e-03

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 40.26  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHaaTPIVAMT 848
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQR--EPVLILT 79
                          90       100
                  ....*....|....*....|...
gi 1819251900 849 ANAFGEDRQACLDAGMDDHVAKP 871
Cdd:PRK10336   80 ARDALAERVEGLRLGADDYLCKP 102
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
787-871 3.17e-03

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: 37.81  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 787 LEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRalpAHAATPIVAMTANAFGEDRQACLDAGMDD 866
Cdd:cd19936    18 LEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR---QKSTLPVIFLTSKDDEIDEVFGLRMGADD 94

                  ....*
gi 1819251900 867 HVAKP 871
Cdd:cd19936    95 YITKP 99
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
72-178 4.02e-03

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 38.31  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900  72 ADQMLESrlAGLMMLAQGVDPSASLDEMRRLGESYARGYG--SHVLLVDADGRVAMNSrlPQDVEQPPLPRPAALDAAQA 149
Cdd:cd18773     4 ADLLLRS--LASALEALAALGSADREELQALLRRLLERNPeiSGIYVVDADGRVVASS--DRDPGGGDDDDDRDRFWYQA 79
                          90       100
                  ....*....|....*....|....*....
gi 1819251900 150 ALREGRPVVGNLFVGPIAGVPIVSVAVPL 178
Cdd:cd18773    80 AKATGKLVISEPYISRVTGKPVITLSRPI 108
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
770-849 4.40e-03

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


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 37.95  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 770 VLLAEDNPVNQEVGRELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMTA 849
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQE--RSLPTSVIVITA 78
PRK13560 PRK13560
hypothetical protein; Provisional
370-485 5.31e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 40.43  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 370 VEQTSSSIVITDPEARIQYVNQ-AFLDQTGYSREEILGST-----PER------------LRSARTPADTVASLWRTLQA 431
Cdd:PRK13560  338 IEAAPIAAIGLDADGNICFVNNnAAERMLGWSAAEVMGKPlpgmdPELneefwcgdfqewYPDGRPMAFDACPMAKTIKG 417
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1819251900 432 GETWRGEFVNR-RKDGSEYVESAVVTPLRSPEGRVTHFVAVSEDITERRRLEREL 485
Cdd:PRK13560  418 GKIFDGQEVLIeREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQL 472
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
785-848 6.50e-03

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: 37.48  E-value: 6.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819251900 785 ELLEMAGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRAlpAHAATPIVAMT 848
Cdd:cd17550    16 GILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE--KYPDLPVIMIS 77
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
769-877 7.88e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 38.68  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 769 RVLLAEDNPVNQEVGRELLEM--AGLCVDVADDGEAAVACAAAGDYAAILMDMQMPGVDGLEATRRIRALPAHAAtpIVA 846
Cdd:PRK10403    8 QVLIVDDHPLMRRGVRQLLELdpGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQ--III 85
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1819251900 847 MTANAFGEDRQACLDAGMDDHVAKPVDPAQL 877
Cdd:PRK10403   86 LTVSDASSDVFALIDAGADGYLLKDSDPEVL 116
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
542-742 8.77e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 38.83  E-value: 8.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 542 MRRDAPDAVTAERLARVDGAAQHLLAVLNDILDlskieagrlELHEHDFSLRELVSRCIEQVAERARTKALRLESDVDDV 621
Cdd:COG4585    81 RLLDADPEAAREELEEIRELAREALAELRRLVR---------GLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251900 622 PDVLfgdSMRIAQALL----NLLSNAVKFTeqGGVSLQVRLLAREGpwlQLGFTVADTGIGIEAAKLGqlftafaqadat 697
Cdd:COG4585   152 PDRL---PPEVELALYrivqEALTNALKHA--GATRVTVTLEVDDG---ELTLTVRDDGVGFDPEAAP------------ 211
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1819251900 698 marrfgGTGLGLAITRRLALLMGGDVAVDSRVGEGSRFSFSVRLR 742
Cdd:COG4585   212 ------GGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
 
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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